LOCUS       ISP2_HEMAM               163 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Type-2 ice-structuring protein; AltName: Full=Type II
            antifreeze protein; Short=AFP; Flags: Precursor.
ACCESSION   P05140
VERSION     P05140.2
DBSOURCE    UniProtKB: locus ISP2_HEMAM, accession P05140;
            class: standard.
            created: Aug 13, 1987.
            sequence updated: Aug 1, 1990.
            annotation updated: Feb 22, 2023.
            xrefs: J02593.1, AAA49617.1, J05100.1, AAA49618.1, A34313, 2AFP_A
            xrefs (non-sequence databases): PDBsum:2AFP, AlphaFoldDB:P05140,
            BMRB:P05140, SMR:P05140, EvolutionaryTrace:P05140, GO:0005576,
            GO:0030246, CDD:cd00037, Gene3D:3.10.100.10, InterPro:IPR002353,
            InterPro:IPR001304, InterPro:IPR016186, InterPro:IPR018378,
            InterPro:IPR016187, PANTHER:PTHR22803:SF124, PANTHER:PTHR22803,
            Pfam:PF00059, PRINTS:PR00356, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    3D-structure; Antifreeze protein; Direct protein sequencing;
            Disulfide bond; Lectin; Secreted; Signal.
SOURCE      Hemitripterus americanus (sea raven)
  ORGANISM  Hemitripterus americanus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Actinopterygii; Neopterygii; Teleostei; Neoteleostei;
            Acanthomorphata; Eupercaria; Perciformes; Cottioidei; Cottales;
            Agonidae; Hemitripterinae; Hemitripterus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Ng,N.F., Trinh,K.Y. and Hew,C.L.
  TITLE     Structure of an antifreeze polypeptide precursor from the sea
            raven, Hemitripterus americanus
  JOURNAL   J Biol Chem 261 (33), 15690-15695 (1986)
   PUBMED   3782083
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Hayes,P.H., Scott,G.K., Ng,N.F., Hew,C.L. and Davies,P.L.
  TITLE     Cystine-rich type II antifreeze protein precursor is initiated from
            the third AUG codon of its mRNA
  JOURNAL   J Biol Chem 264 (31), 18761-18767 (1989)
   PUBMED   2572595
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF
            36-41; 52-63; 95-97; 111-116 AND 121-137, SUBCELLULAR LOCATION, AND
            PTM.
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Ng,N.F. and Hew,C.L.
  TITLE     Structure of an antifreeze polypeptide from the sea raven.
            Disulfide bonds and similarity to lectin-binding proteins
  JOURNAL   J Biol Chem 267 (23), 16069-16075 (1992)
   PUBMED   1644794
  REMARK    PRELIMINARY DISULFIDE BONDS, AND SIMILARITY TO C-TYPE LECTINS.
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Gronwald,W., Loewen,M.C., Lix,B., Daugulis,A.J., Sonnichsen,F.D.,
            Davies,P.L. and Sykes,B.D.
  TITLE     The solution structure of type II antifreeze protein reveals a new
            member of the lectin family
  JOURNAL   Biochemistry 37 (14), 4712-4721 (1998)
   PUBMED   9537986
  REMARK    STRUCTURE BY NMR, AND DISULFIDE BONDS.
COMMENT     On Nov 22, 2005 this sequence version replaced gi:1072445.
            [FUNCTION] Antifreeze proteins lower the blood freezing point.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000269|PubMed:2572595}.
            [PTM] The N-terminus is blocked. {ECO:0000269|PubMed:2572595}.
            [SEQUENCE CAUTION] Sequence=AAA49617.1; Type=Erroneous initiation;
            Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Hemitripterus americanus"
                     /db_xref="taxon:8094"
     Protein         1..163
                     /product="Type-2 ice-structuring protein"
                     /note="Type II antifreeze protein; AFP"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..17
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          18..34
                     /region_name="Propeptide"
                     /note="/evidence=ECO:0000305|PubMed:2572595.
                     /id=PRO_0000017544."
     Region          35..163
                     /region_name="Mature chain"
                     /note="Type-2 ice-structuring protein.
                     /evidence=ECO:0000305|PubMed:2572595. /id=PRO_0000017545."
     Region          38
                     /region_name="Conflict"
                     /note="P -> G (in Ref. 2; AAA49618).
                     /evidence=ECO:0000305."
     Region          39..163
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          41..159
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Bond            bond(41,52)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:9537986."
     Region          43..45
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Region          49..53
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Region          62..72
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Bond            bond(69,159)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:9537986."
     Region          80..82
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Region          83..91
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Bond            bond(103,134)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:9537986."
     Region          103..107
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Region          110..114
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Region          122..124
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Bond            bond(123,145)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:9537986."
     Site            order(133,137,139,145,147..150,153..155)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(135,151)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:9537986."
     Region          141..144
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
     Region          159..161
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2AFP."
ORIGIN
        1 mltvsllvca mmaltqandd kilkgtatea gpvsqrappn cpagwqplgd rciyyettam
       61 twalaetncm klgghlasih sqeehsfiqt lnagvvwigg saclqagawt wsdgtpmnfr
      121 swcstkpddv laaccmqmta aadqcwddlp cpashksvca mtf
//
LOCUS       ISP2_BRASG               168 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Type-2 ice-structuring protein; AltName: Full=Type II
            antifreeze protein; AltName: Full=lpAFP; Flags: Precursor.
ACCESSION   A0ZT93
VERSION     A0ZT93.1
DBSOURCE    UniProtKB: locus ISP2_BRASG, accession A0ZT93;
            class: standard.
            created: Sep 12, 2018.
            sequence updated: Jan 23, 2007.
            annotation updated: Feb 22, 2023.
            xrefs: AB283044.1, BAF37106.1, 2ZIB_A
            xrefs (non-sequence databases): PDBsum:2ZIB, AlphaFoldDB:A0ZT93,
            SMR:A0ZT93, EvolutionaryTrace:A0ZT93, GO:0005576, GO:0030246,
            CDD:cd00037, Gene3D:3.10.100.10, InterPro:IPR002353,
            InterPro:IPR001304, InterPro:IPR016186, InterPro:IPR018378,
            InterPro:IPR016187, PANTHER:PTHR22802, PANTHER:PTHR22802:SF439,
            Pfam:PF00059, PRINTS:PR00356, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    3D-structure; Antifreeze protein; Disulfide bond; Lectin; Secreted;
            Signal.
SOURCE      Brachyopsis segaliensis
  ORGANISM  Brachyopsis segaliensis
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Actinopterygii; Neopterygii; Teleostei; Neoteleostei;
            Acanthomorphata; Eupercaria; Perciformes; Cottioidei; Cottales;
            Agonidae; Brachyopsinae; Brachyopsis.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Nishimiya,Y., Kondo,H., Yasui,M., Sugimoto,H., Noro,N., Sato,R.,
            Suzuki,M., Miura,A. and Tsuda,S.
  TITLE     Crystallization and preliminary X-ray crystallographic analysis of
            Ca2+-independent and Ca2+-dependent species of the type II
            antifreeze protein
  JOURNAL   Acta Crystallogr. F Struct. Biol. Commun. 62, 538-541 (2006)
   PUBMED   16754975
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], CRYSTALLIZATION, AND SUBCELLULAR
            LOCATION.
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Nishimiya,Y., Kondo,H., Takamichi,M., Sugimoto,H., Suzuki,M.,
            Miura,A. and Tsuda,S.
  TITLE     Crystal structure and mutational analysis of Ca2+-independent type
            II antifreeze protein from longsnout poacher, Brachyopsis rostratus
  JOURNAL   J Mol Biol 382 (3), 734-746 (2008)
   PUBMED   18674542
  REMARK    X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) OF 42-168, FUNCTION,
            DISULFIDE BONDS, AND MUTAGENESIS OF ILE-99; ALA-112 AND LEU-153.
COMMENT     [FUNCTION] Has antifreeze activity to protect fish blood from
            freezing at subzero sea water temperatures (Probable). Binds to ice
            crystals and inhibits their growth. The thermal hysteresis (TH)
            activity, the ability to lower the blood freezing point, is
            approximately 0.45 degrees Celsius at 0.15 mM for this protein
            (PubMed:18674542). {ECO:0000269|PubMed:18674542,
            ECO:0000305|PubMed:18674542}.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000269|PubMed:16754975}.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Brachyopsis segaliensis"
                     /db_xref="taxon:1633465"
     Protein         1..168
                     /product="Type-2 ice-structuring protein"
                     /note="Type II antifreeze protein; lpAFP"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..17
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          18..34
                     /region_name="Propeptide"
                     /note="/evidence=ECO:0000250|UniProtKB:P05140.
                     /id=PRO_0000445011."
     Region          35..168
                     /region_name="Mature chain"
                     /note="Type-2 ice-structuring protein.
                     /evidence=ECO:0000250|UniProtKB:P05140.
                     /id=PRO_5002631706."
     Region          45..163
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Bond            bond(45,56)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000269|PubMed:18674542,
                     ECO:0007744|PDB:2ZIB."
     Region          50..52
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
     Region          52..164
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          55..64
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
     Region          66..75
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
     Bond            bond(73,163)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:18674542, ECO:0007744|PDB:2ZIB."
     Region          78..80
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
     Region          86..95
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
     Site            99
                     /site_type="mutagenized"
                     /note="I->F: Has 60% thermal hysteresis (TH) activity of
                     that of the wild-type. Has 60% thermal hysteresis (TH)
                     activity of that of the wild-type; when associated with
                     F-112. /evidence=ECO:0000269|PubMed:18674542."
     Region          100..105
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
     Bond            bond(107,138)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000269|PubMed:18674542,
                     ECO:0007744|PDB:2ZIB."
     Site            112
                     /site_type="mutagenized"
                     /note="A->F: No effect on thermal hysteresis (TH)
                     activity. Has 60% thermal hysteresis (TH) activity of that
                     of the wild-type; when associated with F-99.
                     /evidence=ECO:0000269|PubMed:18674542."
     Bond            bond(127,149)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000269|PubMed:18674542,
                     ECO:0007744|PDB:2ZIB."
     Site            order(137,141,143,149,151..154,157..159)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(139,155)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:18674542, ECO:0007744|PDB:2ZIB."
     Region          139..142
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
     Region          150..153
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
     Site            153
                     /site_type="mutagenized"
                     /note="L->F: Nearly identical thermal hysteresis (TH)
                     activity with that of the wild-type.
                     /evidence=ECO:0000269|PubMed:18674542."
     Region          159..166
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2ZIB."
ORIGIN
        1 mltvsllvca mmaltqadhd gvlkgtatea gevspvfrsr ralvcpagwt lhgqrcfyse
       61 atamtwdlae ancvnkgghl asihsleeql yikdivagiv wiggsackva gawswtdgtp
      121 vdyrtwcptk pndilsdccm qmtaavdkcw ddlpcpasha sicakaai
//
LOCUS       ISP2_OSMMO               175 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Type-2 ice-structuring protein; AltName: Full=Type II
            antifreeze protein; Short=AFP; Flags: Precursor.
ACCESSION   Q01758
VERSION     Q01758.1
DBSOURCE    UniProtKB: locus ISP2_OSMMO, accession Q01758;
            class: standard.
            created: Jul 1, 1993.
            sequence updated: Jul 1, 1993.
            annotation updated: Feb 22, 2023.
            xrefs: M96154.1, AAA49442.1, JH0626
            xrefs (non-sequence databases): AlphaFoldDB:Q01758, SMR:Q01758,
            GO:0005576, GO:0030246, CDD:cd00037, Gene3D:3.10.100.10,
            InterPro:IPR002353, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR016187, PANTHER:PTHR46784,
            PANTHER:PTHR46784:SF1, Pfam:PF00059, PRINTS:PR00356, SMART:SM00034,
            SUPFAM:SSF56436, PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Antifreeze protein; Direct protein sequencing; Disulfide bond;
            Lectin; Secreted; Signal.
SOURCE      Osmerus mordax (rainbow smelt)
  ORGANISM  Osmerus mordax
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Actinopterygii; Neopterygii; Teleostei; Stomiati; Osmeriformes;
            Osmeridae; Osmerus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Ewart,K.V., Rubinsky,B. and Fletcher,G.L.
  TITLE     Structural and functional similarity between fish antifreeze
            proteins and calcium-dependent lectins
  JOURNAL   Biochem Biophys Res Commun 185 (1), 335-340 (1992)
   PUBMED   1599470
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-65; 69-78;
            145-154 AND 161-173.;
            TISSUE=Liver
COMMENT     On Jul 18, 2007 this sequence version replaced gi:85534.
            [FUNCTION] Antifreeze proteins lower the blood freezing point.
            [SUBCELLULAR LOCATION] Secreted.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Osmerus mordax"
                     /db_xref="taxon:8014"
     Protein         1..175
                     /product="Type-2 ice-structuring protein"
                     /note="Type II antifreeze protein; AFP"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..16
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          17..33
                     /region_name="Propeptide"
                     /note="/evidence=ECO:0000255. /id=PRO_0000017546."
     Region          34..175
                     /region_name="Mature chain"
                     /note="Type-2 ice-structuring protein.
                     /id=PRO_0000017547."
     Region          36..163
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          38..159
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Bond            bond(38,49)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(66,159)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(103,134)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(123,145)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(133,137,139,145,147..150,153..155)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(135,151)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mlaallvcam valtraangd tgkeavmtgs sgknltecpt dwkmfngrcf lfnplqlhwa
       61 haqiscmkdg anlasihsle eyafvkeltt aglipawigg sdchvstywf wmdstsmdft
      121 dwcaaqpdft ltecciqinv gvgkcwndtp cthlhasvca kpatvipevt ppsim
//
LOCUS       LECG_THANI               159 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Galactose-specific lectin nattectin; Short=CTL;
            Flags: Precursor.
ACCESSION   Q66S03
VERSION     Q66S03.1
DBSOURCE    UniProtKB: locus LECG_THANI, accession Q66S03;
            class: standard.
            created: Mar 1, 2005.
            sequence updated: Oct 11, 2004.
            annotation updated: Feb 22, 2023.
            xrefs: AY707913.1, AAU11827.1
            xrefs (non-sequence databases): AlphaFoldDB:Q66S03, SMR:Q66S03,
            GO:0005576, GO:0030246, GO:0046872, GO:0090729, GO:0006954,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR016187, PANTHER:PTHR22803:SF141, PANTHER:PTHR22803,
            Pfam:PF00059, PRINTS:PR01504, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS50041
KEYWORDS    Calcium; Cleavage on pair of basic residues; Direct protein
            sequencing; Disulfide bond; Hemagglutinin; Inflammatory response;
            Lectin; Metal-binding; Secreted; Signal; Toxin.
SOURCE      Thalassophryne nattereri
  ORGANISM  Thalassophryne nattereri
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Actinopterygii; Neopterygii; Teleostei; Neoteleostei;
            Acanthomorphata; Batrachoidaria; Batrachoididae; Thalassophryne.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Lopes-Ferreira,M., Magalhaes,G.S., Fernandez,J.H.,
            Junqueira-de-Azevedo Ide,L., Le Ho,P., Lima,C., Valente,R.H. and
            Moura-da-Silva,A.M.
  TITLE     Structural and biological characterization of Nattectin, a new
            C-type lectin from the venomous fish Thalassophryne nattereri
  JOURNAL   Biochimie 93 (6), 971-980 (2011)
   PUBMED   21396978
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-41, FUNCTION,
            BIOASSAY, SUBUNIT, INDUCTION, AND MASS SPECTROMETRY.;
            TISSUE=Venom, and Venom gland
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Magalhaes,G.S., Lopes-Ferreira,M., Junqueira-de-Azevedo,I.L.M.,
            Ho,P.L. and Moura-da-Silva,A.M.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-AUG-2004) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            TISSUE=Venom gland
COMMENT     [FUNCTION] Galactose specific lectin that exhibits hemagglutination
            activity (minimum hemagluttination concentration = 2.5 ug/well) in
            a calcium-independent fashion. Has remarkable pro-inflammatory
            activity, inducing neutrophil mobilization in mice. Plays a crucial
            role in the innate immune system and chronic manifestations,
            especially in neutrophil mobilization.
            {ECO:0000269|PubMed:21396978}.
            [SUBUNIT] Monomer. {ECO:0000269|PubMed:21396978}.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000250}.
            [TISSUE SPECIFICITY] Expressed by the venom gland.
            [INDUCTION] Hemagglutination is completely inhibited by galactose.
            Is not inhibited by mannose, and the chelating agent EDTA.
            {ECO:0000269|PubMed:21396978}.
            [PTM] Not glycosylated. {ECO:0000269|PubMed:21396978}.
            [MASS SPECTROMETRY] Mass=15087; Method=MALDI;
            Evidence={ECO:0000269|PubMed:21396978}.
            [SIMILARITY] Belongs to the true venom lectin family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Thalassophryne nattereri"
                     /db_xref="taxon:289382"
     Protein         1..159
                     /product="Galactose-specific lectin nattectin"
                     /note="CTL"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..21
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          22..24
                     /region_name="Propeptide"
                     /note="/id=PRO_0000017566."
     Region          27..159
                     /region_name="Mature chain"
                     /note="Galactose-specific lectin nattectin.
                     /id=PRO_0000017567."
     Region          31..155
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Bond            bond(31,42)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          38..156
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(59,155)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          122..124
                     /region_name="Short sequence motif of biological interest"
                     /note="Galactose-binding."
     Site            order(130,134,136,141,143..146,149..151)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(132,147)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 masvphftvf lflacalgig anvtrratss cpkgwthhgs rcftfhrgsm dwasaeaaci
       61 rkggnlasih nrreqnfith lihklsgenr rtwiggndav kegmwfwsdg skfnykgwkk
      121 gqpdkhvpae hcaetnfkga fwnnalckvk rsflcaknl
//
LOCUS       LADD_ONCMY               190 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Ladderlectin; Flags: Precursor.
ACCESSION   P81018
VERSION     P81018.2
DBSOURCE    UniProtKB: locus LADD_ONCMY, accession P81018;
            class: standard.
            created: Nov 1, 1997.
            sequence updated: Oct 29, 2014.
            annotation updated: Feb 22, 2023.
            xrefs (non-sequence databases): AlphaFoldDB:P81018, SMR:P81018,
            GO:0005903, GO:0044194, GO:0005737, GO:0005829, GO:0005615,
            GO:0005886, GO:0030246, GO:0008061, Gene3D:3.10.100.10,
            InterPro:IPR001304, InterPro:IPR016186, InterPro:IPR016187,
            PANTHER:PTHR22803:SF141, PANTHER:PTHR22803, Pfam:PF00059,
            PRINTS:PR01504, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS50041
KEYWORDS    Alternative splicing; Calcium; Direct protein sequencing; Disulfide
            bond; Lectin; Signal.
SOURCE      Oncorhynchus mykiss (rainbow trout)
  ORGANISM  Oncorhynchus mykiss
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
            Salmoniformes; Salmonidae; Salmoninae; Oncorhynchus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Russell,S., Young,K.M., Smith,M., Hayes,M.A. and Lumsden,J.S.
  TITLE     Cloning, binding properties, and tissue localization of rainbow
            trout (Oncorhynchus mykiss) ladderlectin
  JOURNAL   Fish Shellfish Immunol 24 (6), 669-683 (2008)
   PUBMED   18407519
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE
            SPECIFICITY.
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Jensen,L.E., Thiel,S., Petersen,T.E. and Jensenuis,J.C.
  TITLE     A rainbow trout lectin with multimeric structure
  JOURNAL   Comp. Biochem. Physiol. 116B, 385-390 (1997)
   PUBMED   9149391
  REMARK    PROTEIN SEQUENCE OF 45-55.;
            TISSUE=Blood
COMMENT     On Nov 5, 2014 this sequence version replaced P81018.1.
            [FUNCTION] Lectin that binds sepharose in a calcium-dependent
            manner.
            [SUBUNIT] Multimeric.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1 {ECO:0000305}; Synonyms=RTLL-2
            {ECO:0000303|PubMed:18407519}; IsoId=P81018-1; Sequence=Displayed;
            Name=2 {ECO:0000305}; Synonyms=RTLL-1
            {ECO:0000303|PubMed:18407519}; IsoId=P81018-2; Sequence=VSP_057102.
            [TISSUE SPECIFICITY] Expressed in cells of the branchial
            epithelium, hepatic sinusoids, biliary epithelium, renal
            interstitium, skin, and sub-mucosal granular layer of the
            intestine. Highly expressed in caudal kidney. Moderately expressed
            in liver. Weakly expressed in gill, spleen, cranial kidney and
            skin. Isoform 1 is highly expressed in intestine. Isoform 2 is
            weakly expressed in intestine. {ECO:0000269|PubMed:18407519}.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Oncorhynchus mykiss"
                     /db_xref="taxon:8022"
     Protein         1..190
                     /product="Ladderlectin"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..18
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          10
                     /region_name="Conflict"
                     /note="L -> M (in Ref. 1; no nucleotide entry).
                     /evidence=ECO:0000305."
     Region          19..190
                     /region_name="Mature chain"
                     /note="Ladderlectin. /evidence=ECO:0000255.
                     /id=PRO_0000084351."
     Region          21..34
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:18407519. /id=VSP_057102."
     Region          52..175
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Region          54
                     /region_name="Conflict"
                     /note="T -> P (in Ref. 2; AA sequence).
                     /evidence=ECO:0000305."
     Region          60..179
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          101..105
                     /region_name="Conflict"
                     /note="EVVAS -> AIAGC (in Ref. 1; no nucleotide entry).
                     /evidence=ECO:0000305."
     Region          113
                     /region_name="Conflict"
                     /note="P -> T (in Ref. 1; no nucleotide entry).
                     /evidence=ECO:0000305."
     Site            order(151,155,158,163,165..168,171..173)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(153,169)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          159
                     /region_name="Conflict"
                     /note="R -> G (in Ref. 1; no nucleotide entry).
                     /evidence=ECO:0000305."
     Region          167
                     /region_name="Conflict"
                     /note="I -> M (in Ref. 1; no nucleotide entry).
                     /evidence=ECO:0000305."
ORIGIN
        1 mamltislll caavalngat vlelfqdfeq alhlgakged ervvaaenrn qcptgwfqfg
       61 srcfmfveta rswplaerhc vslganlasv hssaeyqflq evvasktggf stpwiggfda
      121 vqdrlwfwsd gsefdyqnwk kgepnnsggr epcivinwrd eyrwndincg nsfpsgvlqk
      181 nveiqknept
//
LOCUS       AJL2_ANGJA               166 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Lactose-binding lectin l-2; AltName: Full=Ajl-2;
            Flags: Precursor.
ACCESSION   Q90WJ8
VERSION     Q90WJ8.2
DBSOURCE    UniProtKB: locus AJL2_ANGJA, accession Q90WJ8;
            class: standard.
            created: Dec 7, 2004.
            sequence updated: Jun 1, 2002.
            annotation updated: Feb 22, 2023.
            xrefs: AB050703.2, BAB47156.2
            xrefs (non-sequence databases): AlphaFoldDB:Q90WJ8, SMR:Q90WJ8,
            GO:0005576, GO:0030246, GO:0050829, GO:0043152, CDD:cd00037,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR016187, PANTHER:PTHR22801:SF53,
            PANTHER:PTHR22801, Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide
            bond; Hemagglutinin; Lectin; Secreted; Signal.
SOURCE      Anguilla japonica (Japanese eel)
  ORGANISM  Anguilla japonica
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Actinopterygii; Neopterygii; Teleostei; Anguilliformes;
            Anguillidae; Anguilla.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Tasumi,S., Ohira,T., Kawazoe,I., Suetake,H., Suzuki,Y. and Aida,K.
  TITLE     Primary structure and characteristics of a lectin from skin mucus
            of the Japanese eel Anguilla japonica
  JOURNAL   J Biol Chem 277 (30), 27305-27311 (2002)
   PUBMED   11959866
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-64, FUNCTION,
            SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
            SPECTROMETRY.;
            TISSUE=Skin mucus {ECO:0000269|PubMed:11959866}
COMMENT     [FUNCTION] Involved in host defense at the body surface. Causes
            agglutination and suppresses the growth of the Gram-negative
            bacterium E.coli K12. Possesses calcium-independent
            hemagglutinating activity. {ECO:0000269|PubMed:11959866}.
            [SUBUNIT] Homodimer; disulfide-linked.
            {ECO:0000269|PubMed:11959866}.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000269|PubMed:11959866}.
            [TISSUE SPECIFICITY] Skin; contained within club cells which are a
            component of the epidermis in combination with epithelial cells and
            mucus cells (at protein level). {ECO:0000269|PubMed:11959866}.
            [MASS SPECTROMETRY] Mass=31743; Method=MALDI;
            Evidence={ECO:0000269|PubMed:11959866}.
            [MISCELLANEOUS] Binds lactose inhibiting its agglutination
            activity. {ECO:0000269|PubMed:11959866}.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Anguilla japonica"
                     /db_xref="taxon:7937"
     gene            1..166
                     /gene="l-2"
     Protein         1..166
                     /product="Lactose-binding lectin l-2"
                     /note="Ajl-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..24
                     /region_name="Signal"
                     /note="/evidence=ECO:0000269|PubMed:11959866."
     Region          25..166
                     /region_name="Mature chain"
                     /note="Lactose-binding lectin l-2.
                     /evidence=ECO:0000269|PubMed:11959866.
                     /id=PRO_0000017565."
     Region          34..160
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Bond            bond(34,45)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9NNX6,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          41..161
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(62,160)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9NNX6,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(134,138,140,146,148..151,154..156)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(136,152)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9NNX6,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mvsfklpafl cvavlssmal vshgavlglc egacpegwve hknrcylhva ekktwldael
       61 nclhhggnla sehsedehqf lkdlhkgsdd pfwiglsavh egrswlwsdg tsasaegdfs
      121 mwnpgepnda ggkedcvhdn yggqkhwndi kcdllfpsic vlrmve
//
LOCUS       NCAN_HUMAN              1321 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=Neurocan core protein; AltName: Full=Chondroitin
            sulfate proteoglycan 3; Flags: Precursor.
ACCESSION   O14594
VERSION     O14594.3
DBSOURCE    UniProtKB: locus NCAN_HUMAN, accession O14594;
            class: standard.
            extra accessions:Q9UPK6
            created: Jan 27, 2003.
            sequence updated: Nov 13, 2007.
            annotation updated: Sep 13, 2023.
            xrefs: AF026547.1, AAC80576.1, AC003110.1, AAB86655.1, AC005254.1,
            AAC25581.1, NP_004377.2
            xrefs (non-sequence databases): CCDS:CCDS12397.1,
            AlphaFoldDB:O14594, SMR:O14594, BioGRID:107845, IntAct:O14594,
            STRING:9606.ENSP00000252575, DrugBank:DB02379, DrugBank:DB08818,
            DrugBank:DB04396, GlyConnect:1550, GlyCosmos:O14594, GlyGen:O14594,
            iPTMnet:O14594, PhosphoSitePlus:O14594, BioMuta:NCAN, jPOST:O14594,
            MassIVE:O14594, PaxDb:O14594, PeptideAtlas:O14594,
            Antibodypedia:28403, DNASU:1463, Ensembl:ENST00000252575.11,
            Ensembl:ENSP00000252575.4, Ensembl:ENSG00000130287.14, GeneID:1463,
            KEGG:hsa:1463, MANE-Select:ENST00000252575.11, UCSC:uc002nlz.4,
            AGR:HGNC:2465, CTD:1463, DisGeNET:1463, GeneCards:NCAN, HGNC:2465,
            HPA:ENSG00000130287, MIM:600826, neXtProt:NX_O14594,
            OpenTargets:ENSG00000130287, PharmGKB:PA162396986,
            VEuPathDB:HostDB:ENSG00000130287, eggNOG:ENOG502QQ78,
            GeneTree:ENSGT00940000158649, HOGENOM:CLU_000303_0_1_1,
            InParanoid:O14594, OMA:YPRRRAN, OrthoDB:5402504at2759,
            PhylomeDB:O14594, TreeFam:TF332134, PathwayCommons:O14594,
            Reactome:R-HSA-1971475, Reactome:R-HSA-2022870,
            Reactome:R-HSA-2022923, Reactome:R-HSA-2024101,
            Reactome:R-HSA-3000178, Reactome:R-HSA-3560783,
            Reactome:R-HSA-3560801, Reactome:R-HSA-3595172,
            Reactome:R-HSA-3595174, Reactome:R-HSA-3595177,
            Reactome:R-HSA-373760, Reactome:R-HSA-419037,
            Reactome:R-HSA-4420332, SignaLink:O14594, BioGRID-ORCS:1463,
            ChiTaRS:NCAN, GeneWiki:Neurocan, GenomeRNAi:1463, Pharos:O14594,
            PRO:PR:O14594, Proteomes:UP000005640, RNAct:O14594,
            Bgee:ENSG00000130287, ExpressionAtlas:O14594, Genevisible:O14594,
            GO:0005576, GO:0005615, GO:0005796, GO:0043202, GO:0072534,
            GO:0045202, GO:0005509, GO:0030246, GO:0005540, GO:0007155,
            GO:0007417, GO:0010001, GO:0002052, GO:0001501, CDD:cd00033,
            CDD:cd00054, CDD:cd05902, CDD:cd03517, CDD:cd03520,
            Gene3D:2.10.70.10, Gene3D:2.60.40.10, Gene3D:2.10.25.10,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR016187, InterPro:IPR001881,
            InterPro:IPR000742, InterPro:IPR000152, InterPro:IPR018097,
            InterPro:IPR007110, InterPro:IPR036179, InterPro:IPR013783,
            InterPro:IPR003599, InterPro:IPR013106, InterPro:IPR000538,
            InterPro:IPR035976, InterPro:IPR000436, PANTHER:PTHR22804,
            PANTHER:PTHR22804:SF24, Pfam:PF00008, Pfam:PF00059, Pfam:PF00084,
            Pfam:PF07686, Pfam:PF00193, PRINTS:PR01265, SMART:SM00032,
            SMART:SM00034, SMART:SM00181, SMART:SM00179, SMART:SM00409,
            SMART:SM00445, SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF57196,
            SUPFAM:SSF48726, PROSITE:PS00010, PROSITE:PS00615, PROSITE:PS50041,
            PROSITE:PS00022, PROSITE:PS01186, PROSITE:PS50026, PROSITE:PS01187,
            PROSITE:PS50835, PROSITE:PS01241, PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
            Glycoprotein; Hyaluronic acid; Immunoglobulin domain; Lectin;
            Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1321)
  AUTHORS   Prange,C.K., Pennacchio,L.A., Lieuallen,K., Fan,W. and Lennon,G.G.
  TITLE     Characterization of the human neurocan gene, CSPG3
  JOURNAL   Gene 221 (2), 199-205 (1998)
   PUBMED   9795216
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-1254.
REFERENCE   2  (residues 1 to 1321)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   3  (residues 1 to 1321)
  AUTHORS   Halim,A., Ruetschi,U., Larson,G. and Nilsson,J.
  TITLE     LC-MS/MS characterization of O-glycosylation sites and glycan
            structures of human cerebrospinal fluid glycoproteins
  JOURNAL   J Proteome Res 12 (2), 573-584 (2013)
   PUBMED   23234360
  REMARK    GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
REFERENCE   4  (residues 1 to 1321)
  AUTHORS   Noborn,F., Gomez Toledo,A., Sihlbom,C., Lengqvist,J., Fries,E.,
            Kjellen,L., Nilsson,J. and Larson,G.
  TITLE     Identification of chondroitin sulfate linkage region glycopeptides
            reveals prohormones as a novel class of proteoglycans
  JOURNAL   Mol Cell Proteomics 14 (1), 41-49 (2015)
   PUBMED   25326458
  REMARK    SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT
            SER-381 AND SER-411.
COMMENT     On Nov 14, 2007 this sequence version replaced O14594.2.
            [FUNCTION] May modulate neuronal adhesion and neurite growth during
            development by binding to neural cell adhesion molecules (NG-CAM
            and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic
            acid.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000269|PubMed:25326458}.
            [TISSUE SPECIFICITY] Detected in cerebrospinal fluid (at protein
            level) (PubMed:25326458). Brain. {ECO:0000269|PubMed:25326458}.
            [PTM] O-glycosylated; contains chondroitin sulfate.
            {ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:25326458}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Neurocan;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_hum_Ctlect_213'.
FEATURES             Location/Qualifiers
     source          1..1321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..1321
                     /gene="NCAN"
                     /gene_synonym="CSPG3"
                     /gene_synonym="NEUR"
     Protein         1..1321
                     /product="Neurocan core protein"
                     /note="Chondroitin sulfate proteoglycan 3"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          23..1321
                     /region_name="Mature chain"
                     /note="Neurocan core protein. /id=PRO_0000017516."
     Region          38..153
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          41..162
                     /region_name="Ig_Neurocan"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), neurocan;
                     cd05902"
                     /db_xref="CDD:409483"
     Region          41..44
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409483"
     Region          47..49
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409483"
     Region          53..61
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409483"
     Bond            bond(59,140)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          70
                     /region_name="Variant"
                     /note="A -> T (in dbSNP:rs2228601). /id=VAR_024521."
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409483"
     Region          90..93
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409483"
     Region          92
                     /region_name="Variant"
                     /note="P -> S (in dbSNP:rs2228603). /id=VAR_020213."
     Region          111..116
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409483"
     Region          122..128
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409483"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          136..143
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409483"
     Region          153..162
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409483"
     Region          160..255
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          160..254
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            170..171
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(182,253)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(206,227)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          259..357
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          261..356
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            268..269
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(280,355)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(304,325)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          362..414
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            381
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:25326458."
     Site            411
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:25326458."
     Region          <421..964
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          456..479
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          494..513
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          532..579
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          682..731
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          708..712
                     /region_name="Region of interest in the sequence"
                     /note="O-glycosylated at one site."
     Region          710..731
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          820..844
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          876..955
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          887..918
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          936..955
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1008..1044
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          1012..1042
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Bond            bond(1012,1023)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1017,1032)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            1026
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(1034,1043)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1046..1082
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1046..1082
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(1046,1049,1063)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(1050,1061)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1055,1070)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1072,1081)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1084..1213
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          1088..1211
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(1088,1099)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1116,1208)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(1182,1186,1188,1194,1196..1199,1202..1204)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(1184,1200)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1213..1273
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          1215..1271
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(1215,1258)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            1223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(1225,1245)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          1234
                     /region_name="Conflict"
                     /note="Y -> N (in Ref. 1; AAC80576).
                     /evidence=ECO:0000305."
     Bond            bond(1244,1271)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1254
                     /region_name="Variant"
                     /note="A -> V (in dbSNP:rs1064389).
                     /evidence=ECO:0000269|PubMed:9795216. /id=VAR_016176."
     Region          1275..1321
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1275..1306
                     /region_name="Compositionally biased region"
                     /note="Basic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1282
                     /region_name="Conflict"
                     /note="R -> G (in Ref. 1; AAC80576).
                     /evidence=ECO:0000305."
     Region          1307..1321
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
        1 mgapfvwalg llmlqmllfv ageqgtqdit daserglhmq klgsgsvqaa laelvalpcl
       61 ftlqprpsaa rdaprikwtk vrtasgqrqd lpilvakdnv vrvakswqgr vslpsyprrr
      121 anatlllgpl rasdsglyrc qvvrgiedeq dlvplevtgv vfhyrsardr yaltfaeaqe
      181 acrlssaiia aprhlqaafe dgfdncdagw lsdrtvrypi tqsrpgcygd rsslpgvrsy
      241 grrnpqelyd vycfarelgg evfyvgparr ltlagaraqc rrqgaalasv gqlhlawheg
      301 ldqcdpgwla dgsvrypiqt prrrcggpap gvrtvyrfan rtgfpspaer fdaycfrahh
      361 ptsqhgdlet pssgdegeil saegppvrel eptleeeevv tpdfqeplvs sgeeetlile
      421 ekqesqqtls ptpgdpmlas wptgevwlst vapspsdmga gtaasshtev aptdpmprrr
      481 grfkglngry fqqqepepgl qggmeasaqp ptseaavnqm epplamavte mlgsgqsrsp
      541 wadltnevdm pgagsaggks spepwlwppt mvppsisghs rapvleleka egpsarpatp
      601 dlfwspleat vsapspapwe afpvatspdl pmmamlrgpk ewmlphptpi steanrveah
      661 geatatapps paaetkvysl plsltptgqg geampttpes pradfretge tspaqvnkae
      721 hsssspwpsv nrnvavgfvp tetateptgl rgipgsesgv fdtaesptsg lqatvdevqd
      781 pwpsvyskgl dasspsaplg spgvflvpkv tpnlepwvat degptvnpmd stvtpapsda
      841 sgiwepgsqv feeaesttls pqvaldtsiv tplttleqgd kvgvpamstl gssssqphpe
      901 pedqvetqgt sgasvpphqs splgkpavpp gtptaasvge sasvssgept vpwdpsstll
      961 pvtlgiedfe levlagspgv esfweevasg eepalpgtpm nagaeevhsd pcennpclhg
     1021 gtcnangtmy gcscdqgfag enceididdc lcspcenggt cidevngfvc lclpsyggsf
     1081 cekdtegcdr gwhkfqghcy ryfahrrawe daekdcrrrs ghltsvhspe ehsfinsfgh
     1141 entwiglndr iverdfqwtd ntglqfenwr enqpdnffag gedcvvmvah esgrwndvpc
     1201 nynlpyvckk gtvlcgpppa venasligar kakynvhatv ryqcnegfaq hhvatircrs
     1261 ngkwdrpqiv ctkprrshrm rrhhhhhqhh hqhhhhksrk errkhkkhpt edwekdegnf
     1321 c
//
LOCUS       NCAN_PANTR              1321 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=Neurocan core protein; AltName: Full=Chondroitin
            sulfate proteoglycan 3; Flags: Precursor.
ACCESSION   Q5IS41
VERSION     Q5IS41.1
DBSOURCE    UniProtKB: locus NCAN_PANTR, accession Q5IS41;
            class: standard.
            created: Mar 15, 2005.
            sequence updated: Feb 15, 2005.
            annotation updated: Sep 13, 2023.
            xrefs: AY665287.1, AAV74325.1, NP_001029342.1
            xrefs (non-sequence databases): AlphaFoldDB:Q5IS41, SMR:Q5IS41,
            STRING:9598.ENSPTRP00000018312, GlyCosmos:Q5IS41, PaxDb:Q5IS41,
            GeneID:468775, KEGG:ptr:468775, CTD:1463, eggNOG:ENOG502QQ78,
            InParanoid:Q5IS41, OrthoDB:5402504at2759, Proteomes:UP000002277,
            GO:0005615, GO:0072534, GO:0045202, GO:0005509, GO:0030246,
            GO:0005540, GO:0007155, GO:0007417, GO:0010001, GO:0002052,
            GO:0001501, CDD:cd00033, CDD:cd00054, CDD:cd05902, CDD:cd03517,
            CDD:cd03520, Gene3D:2.10.70.10, Gene3D:2.60.40.10,
            Gene3D:2.10.25.10, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR016187,
            InterPro:IPR001881, InterPro:IPR000742, InterPro:IPR000152,
            InterPro:IPR018097, InterPro:IPR007110, InterPro:IPR036179,
            InterPro:IPR013783, InterPro:IPR003599, InterPro:IPR013106,
            InterPro:IPR000538, InterPro:IPR035976, InterPro:IPR000436,
            PANTHER:PTHR22804, PANTHER:PTHR22804:SF41, Pfam:PF00008,
            Pfam:PF00059, Pfam:PF00084, Pfam:PF07686, Pfam:PF00193,
            PRINTS:PR01265, SMART:SM00032, SMART:SM00034, SMART:SM00181,
            SMART:SM00179, SMART:SM00409, SMART:SM00445, SUPFAM:SSF56436,
            SUPFAM:SSF57535, SUPFAM:SSF57196, SUPFAM:SSF48726, PROSITE:PS00010,
            PROSITE:PS00615, PROSITE:PS50041, PROSITE:PS00022, PROSITE:PS01186,
            PROSITE:PS50026, PROSITE:PS01187, PROSITE:PS50835, PROSITE:PS01241,
            PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
            Glycoprotein; Hyaluronic acid; Immunoglobulin domain; Lectin;
            Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
SOURCE      Pan troglodytes (chimpanzee)
  ORGANISM  Pan troglodytes
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Pan.
REFERENCE   1  (residues 1 to 1321)
  AUTHORS   Dorus,S., Vallender,E.J., Evans,P.D., Anderson,J.R., Gilbert,S.L.,
            Mahowald,M., Wyckoff,G.J., Malcom,C.M. and Lahn,B.T.
  TITLE     Accelerated evolution of nervous system genes in the origin of Homo
            sapiens
  JOURNAL   Cell 119 (7), 1027-1040 (2004)
   PUBMED   15620360
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].
COMMENT     [FUNCTION] May modulate neuronal adhesion and neurite growth during
            development by binding to neural cell adhesion molecules (NG-CAM
            and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic
            acid (By similarity). {ECO:0000250}.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000250|UniProtKB:O14594}.
            [PTM] O-glycosylated; contains chondroitin sulfate.
            {ECO:0000250|UniProtKB:O14594}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..1321
                     /organism="Pan troglodytes"
                     /db_xref="taxon:9598"
     gene            1..1321
                     /gene="NCAN"
                     /gene_synonym="CSPG3"
     Protein         1..1321
                     /product="Neurocan core protein"
                     /note="Chondroitin sulfate proteoglycan 3"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          23..1321
                     /region_name="Mature chain"
                     /note="Neurocan core protein. /id=PRO_0000017518."
     Region          38..153
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          41..162
                     /region_name="Ig_Neurocan"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), neurocan;
                     cd05902"
                     /db_xref="CDD:409483"
     Region          41..44
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409483"
     Region          47..49
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409483"
     Region          53..61
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409483"
     Bond            bond(59,140)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409483"
     Region          90..93
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409483"
     Region          111..116
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409483"
     Region          122..128
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409483"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          136..143
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409483"
     Region          153..162
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409483"
     Region          160..255
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          160..254
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            170..171
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(182,253)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(206,227)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          259..357
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          261..356
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            268..269
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(280,355)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(304,325)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          362..414
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            381
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14594."
     Site            411
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14594."
     Region          455..479
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          455..469
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          493..518
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          <511..953
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          531..579
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          683..729
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          710..729
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          745..766
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          876..956
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          887..918
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          936..956
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1008..1044
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          1012..1042
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Bond            bond(1012,1023)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1017,1032)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            1026
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(1034,1043)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1046..1082
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1046..1082
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(1046,1049,1063)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(1050,1061)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1055,1070)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1072,1081)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1084..1213
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          1088..1211
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(1088,1099)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1116,1208)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(1182,1186,1188,1194,1196..1199,1202..1204)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(1184,1200)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1213..1273
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          1215..1271
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(1215,1258)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            1223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(1225,1245)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(1244,1271)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1275..1321
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1275..1306
                     /region_name="Compositionally biased region"
                     /note="Basic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1307..1321
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
        1 mgtpfvwalg llmlqmllfv ageqgtqdia daserglhmq klgsgsvqaa laelvalpcl
       61 ftlqpqpsaa rdaprikwtk vrtasgqrqd lpilvakdnv vkvakswqgr vslpsyprrr
      121 anatlllgpl rasdsglyrc qvvrgiedeq dlvplevtgv vfhyrsardr yaltfaeaqe
      181 acrlssaiia aprhlqaafe dgfdncdagw lsdrtvrypi tqsrpgcygd rsslpgvrsy
      241 grrnpqelyd vycfarelgg evfyvgparr ltlagaraqc rrqgaalasv gqlhlawheg
      301 ldqcdpgwla dgsvrypiqt prrrcggpap gvrtvyrfan rtgfpspaer fdaycfrahh
      361 ptsqhgdlet pssgdegeil saegppvrel eptleeeevv tpdfqeplvs sgeeeplile
      421 ekqesqqtls ptpgdpmlas wptgevwlst vapspsdmga gtaasshtev aptdpmprrr
      481 grfkglngry fqqqepepgl qggmeasaqp ptseaagnqm epplamavte mlgsgqsrsp
      541 wadltnevdm pgagsaggks spepwlwppt mvppsisghs rapvleleka egpsarpatp
      601 dlfwspleat vsapspapwe afpvatspdl pmmamlrgpk ewmlphptpi steanrveah
      661 geatttppps paaetkvysl plsltptgqg geampttpes pgadfretge tspaqvnkae
      721 hsssspwpsv nrnvavgfvp tetateptgl rgisgsesgv ldtaesptsg lqatvdevqd
      781 pwpsvyskgl gasspsaplg spgvflvpkv tpslepwvat degptvnpmd stvtlapsda
      841 sgiwepgsqv feeaesttls pqvaldtsiv tplttleqgd kvgvpamstl gssssqphpe
      901 pedqvetqgt sgasvpphqs splgkpavpp gtptaasvge sasvssgept vpwdpsstll
      961 pvtlgiedfe levlagspgv esfweevasg eepalpgtpm kagaeevhsd pcennpclhg
     1021 gtcnangtmy gcscdqgfag enceididdc lcspcenggt cidevngfvc lclpsyggsf
     1081 cekdtegcdr gwhkfqghcy ryfahrrawe daerdcrrrs ghltsvhsse ehsfinsfgh
     1141 entwiglndr iverdfqwtd ntglqfenwr enqpdnffag gedcvvmvah esgrwndvpc
     1201 nynlpyvckk gtvlcgpppa venasligar kakynvhatv ryqcnegfaq hhvatircrs
     1261 ngkwdrpqiv ctkprrshrm rrhhhhhqhh hqhhhhksrk errkhkkhpt edwekdegnf
     1321 c
//
LOCUS       LECG_PATPE               168 aa            linear   INV 22-FEB-2023
DEFINITION  RecName: Full=Alpha-N-acetylgalactosamine-specific lectin; AltName:
            Full=Alpha-N-acetylgalactosamine-binding lectin; AltName:
            Full=GalNAc-specific lectin; AltName: Full=Lectin; Short=ApL;
            AltName: Full=Tn antigen-specific lectin; Flags: Precursor.
ACCESSION   Q8WPD0
VERSION     Q8WPD0.1
DBSOURCE    UniProtKB: locus LECG_PATPE, accession Q8WPD0;
            class: standard.
            created: Oct 3, 2012.
            sequence updated: Mar 1, 2002.
            annotation updated: Feb 22, 2023.
            xrefs: AB062765.1, BAB78598.1, AB079848.1, BAB85109.1
            xrefs (non-sequence databases): AlphaFoldDB:Q8WPD0, SMR:Q8WPD0,
            GO:0030246, CDD:cd03589, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033988,
            InterPro:IPR016187, PANTHER:PTHR22803:SF145, PANTHER:PTHR22803,
            Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin;
            Signal.
SOURCE      Patiria pectinifera
  ORGANISM  Patiria pectinifera
            Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa;
            Asteroidea; Valvatacea; Valvatida; Asterinidae; Patiria.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Kakiuchi,M., Okino,N., Sueyoshi,N., Ichinose,S., Omori,A.,
            Kawabata,S., Yamaguchi,K. and Ito,M.
  TITLE     Purification, characterization, and cDNA cloning of
            alpha-N-acetylgalactosamine-specific lectin from starfish, Asterina
            pectinifera
  JOURNAL   Glycobiology 12 (2), 85-94 (2002)
   PUBMED   11886841
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-26; 51-74;
            88-107 AND 157-163, FUNCTION, SUBUNIT, AND VARIANTS VAL-4; SER-15;
            GLN-67; ALA-84 AND VAL-153.
COMMENT     [FUNCTION] Alpha-N-acetylgalactosamine-specific lectin. The
            oligomeric form has Ca(2+)-dependent hemagglutination activity
            towards sheep erythrocytes. Its hemagglutination activity is
            inhibited by various monosaccharides, oligosaccharides and
            glycopeptides, including inhibition by GalNAc, blood group A
            trisaccharide, Tn antigen, mucin and asialomucin.
            {ECO:0000269|PubMed:11886841}.
            [SUBUNIT] Monomer, homodimer and homooligomer.
            {ECO:0000269|PubMed:11886841}.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Patiria pectinifera"
                     /db_xref="taxon:7594"
     Protein         1..168
                     /product="Alpha-N-acetylgalactosamine-specific lectin"
                     /note="Alpha-N-acetylgalactosamine-binding lectin;
                     GalNAc-specific lectin; Lectin; Tn antigen-specific
                     lectin; ApL"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..18
                     /region_name="Signal"
                     /note="/evidence=ECO:0000269|PubMed:11886841."
     Region          4
                     /region_name="Variant"
                     /note="F -> V. /evidence=ECO:0000269|PubMed:11886841."
     Region          15
                     /region_name="Variant"
                     /note="F -> S. /evidence=ECO:0000269|PubMed:11886841."
     Region          19..168
                     /region_name="Mature chain"
                     /note="Alpha-N-acetylgalactosamine-specific lectin.
                     /evidence=ECO:0000269|PubMed:11886841.
                     /id=PRO_5000049722."
     Region          31..164
                     /region_name="CLECT_CEL-1_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in CEL-1 from Cucumaria echinata and Echinoidin from
                     Anthocidaris crassispina; cd03589"
                     /db_xref="CDD:153059"
     Site            order(32..33,39,62,64)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153059"
     Region          38..163
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(59,162)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          67
                     /region_name="Variant"
                     /note="L -> Q. /evidence=ECO:0000269|PubMed:11886841."
     Region          84
                     /region_name="Variant"
                     /note="T -> A. /evidence=ECO:0000269|PubMed:11886841."
     Site            order(103,107,130,134..135)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153059"
     Site            order(107,135)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153059"
     Site            order(127,129,134,140,150..151)
                     /site_type="other"
                     /note="carbohydrate binding [chemical binding]"
                     /db_xref="CDD:153059"
     Bond            bond(136,154)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          153
                     /region_name="Variant"
                     /note="A -> V. /evidence=ECO:0000269|PubMed:11886841."
ORIGIN
        1 maffralcfv llvgfaaacq pdcswkcppk cppmwtfyng ncyryfgtgk tydeaeshcq
       61 eftevglghl asiasaeenn llltmwksvr ttttgglwig lndqaeegnf iwtdgsavtf
      121 tdwattqpdn yqnedcahmr heldgddrwn diacsrafay vckmsttn
//
LOCUS       NCAN_RAT                1257 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Neurocan core protein; AltName: Full=245 kDa early
            postnatal core glycoprotein; AltName: Full=Chondroitin sulfate
            proteoglycan 3; Contains: RecName: Full=150 kDa adult core
            glycoprotein; Flags: Precursor.
ACCESSION   P55067
VERSION     P55067.1
DBSOURCE    UniProtKB: locus NCAN_RAT, accession P55067;
            class: standard.
            created: Oct 1, 1996.
            sequence updated: Oct 1, 1996.
            annotation updated: Sep 13, 2023.
            xrefs: M97161.1, AAC37679.1, S28764
            xrefs (non-sequence databases): AlphaFoldDB:P55067, SMR:P55067,
            IntAct:P55067, MINT:P55067, STRING:10116.ENSRNOP00000062123,
            GlyCosmos:P55067, GlyGen:P55067, iPTMnet:P55067, SwissPalm:P55067,
            PaxDb:P55067, UCSC:RGD:619941, AGR:RGD:619941, RGD:619941,
            eggNOG:ENOG502QQ78, InParanoid:P55067, PhylomeDB:P55067,
            Reactome:R-RNO-1971475, Reactome:R-RNO-2022870,
            Reactome:R-RNO-2022923, Reactome:R-RNO-2024101,
            Reactome:R-RNO-3000178, PRO:PR:P55067, Proteomes:UP000002494,
            GO:0005615, GO:0098982, GO:0098978, GO:0072534, GO:0098966,
            GO:0005886, GO:0045202, GO:0005509, GO:0030246, GO:0005540,
            GO:0007155, GO:0007417, GO:0010001, GO:0050804, GO:0002052,
            GO:0099175, GO:0051823, GO:0001501, CDD:cd00033, CDD:cd00054,
            CDD:cd03517, CDD:cd03520, Gene3D:2.10.70.10, Gene3D:2.60.40.10,
            Gene3D:2.10.25.10, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR016187,
            InterPro:IPR001881, InterPro:IPR000742, InterPro:IPR000152,
            InterPro:IPR018097, InterPro:IPR007110, InterPro:IPR036179,
            InterPro:IPR013783, InterPro:IPR003599, InterPro:IPR013106,
            InterPro:IPR000538, InterPro:IPR035976, InterPro:IPR000436,
            PANTHER:PTHR22804, PANTHER:PTHR22804:SF24, Pfam:PF00008,
            Pfam:PF00059, Pfam:PF00084, Pfam:PF07686, Pfam:PF00193,
            PRINTS:PR01265, SMART:SM00032, SMART:SM00034, SMART:SM00181,
            SMART:SM00179, SMART:SM00409, SMART:SM00445, SUPFAM:SSF56436,
            SUPFAM:SSF57535, SUPFAM:SSF57196, SUPFAM:SSF48726, PROSITE:PS00010,
            PROSITE:PS00615, PROSITE:PS50041, PROSITE:PS00022, PROSITE:PS01186,
            PROSITE:PS50026, PROSITE:PS01187, PROSITE:PS50835, PROSITE:PS01241,
            PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Calcium; Cell adhesion; Direct protein sequencing; Disulfide bond;
            EGF-like domain; Glycoprotein; Hyaluronic acid; Immunoglobulin
            domain; Lectin; Proteoglycan; Reference proteome; Repeat; Secreted;
            Signal; Sushi.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1257)
  AUTHORS   Rauch,U., Karthikeyan,L., Maurel,P., Margolis,R.U. and
            Margolis,R.K.
  TITLE     Cloning and primary structure of neurocan, a developmentally
            regulated, aggregating chondroitin sulfate proteoglycan of brain
  JOURNAL   J Biol Chem 267 (27), 19536-19547 (1992)
   PUBMED   1326557
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.;
            STRAIN=Sprague-Dawley; TISSUE=Brain
REFERENCE   2  (residues 1 to 1257)
  AUTHORS   Friedlander,D.R., Milev,P., Karthikeyan,L., Margolis,R.K.,
            Margolis,R.U. and Grumet,M.
  TITLE     The neuronal chondroitin sulfate proteoglycan neurocan binds to the
            neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, and
            inhibits neuronal adhesion and neurite outgrowth
  JOURNAL   J Cell Biol 125 (3), 669-680 (1994)
   PUBMED   7513709
  REMARK    CHARACTERIZATION.
REFERENCE   3  (residues 1 to 1257)
  AUTHORS   Parker,B.L., Thaysen-Andersen,M., Solis,N., Scott,N.E.,
            Larsen,M.R., Graham,M.E., Packer,N.H. and Cordwell,S.J.
  TITLE     Site-specific glycan-peptide analysis for determination of
            N-glycoproteome heterogeneity
  JOURNAL   J Proteome Res 12 (12), 5791-5800 (2013)
   PUBMED   24090084
  REMARK    GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121, AND IDENTIFICATION
            BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Brain
COMMENT     On Oct 25, 2005 this sequence version replaced gi:347041.
            [FUNCTION] May modulate neuronal adhesion and neurite growth during
            development by binding to neural cell adhesion molecules (NG-CAM
            and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic
            acid.
            [SUBCELLULAR LOCATION] Secreted.
            [TISSUE SPECIFICITY] Early postnatal and adult brain; not expressed
            in kidney, lung, liver and muscle.
            [PTM] Two isoforms were found that probably arise by proteolytic
            processing. The large isoform is predominant in early postnatal
            brain, the small isoform is found in adult brain.
            [PTM] O-glycosylated; contains chondroitin sulfate.
            {ECO:0000269|PubMed:7513709}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..1257
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..1257
                     /gene="Ncan"
                     /gene_synonym="Cspg3"
     Protein         1..1257
                     /product="Neurocan core protein"
                     /note="245 kDa early postnatal core glycoprotein;
                     Chondroitin sulfate proteoglycan 3"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
     Region          23..1257
                     /region_name="Mature chain"
                     /note="Neurocan core protein. /id=PRO_0000017519."
     Region          37..157
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          40..161
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:448366"
     Region          54..58
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Bond            bond(58,139)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          74..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084."
     Region          122..126
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          136..141
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          154..157
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          159..254
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          159..253
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            169..170
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(181,252)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(205,226)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          258..356
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          260..355
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            267..268
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(279,354)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(303,324)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            339
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          361..391
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            380
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14594."
     Region          <381..703
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            410
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14594."
     Region          447..493
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          447..474
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          550..610
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          557..579
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          639..1257
                     /region_name="Mature chain"
                     /note="150 kDa adult core glycoprotein.
                     /id=PRO_0000017520."
     Region          683..707
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            737
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            944
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:1326557."
     Region          949..985
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          953..983
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Bond            bond(953,964)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(958,973)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            967
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(975,984)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          987..1023
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          987..1023
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(987,990,1004)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(991,1002)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(996,1011)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1013,1022)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1025..1154
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          1029..1152
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(1029,1040)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1057,1149)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(1123,1127,1129,1135,1137..1140,1143..1145)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(1125,1141)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1154..1214
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          1156..1212
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(1156,1199)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            1164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(1166,1186)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(1185,1212)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1215..1257
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1215..1242
                     /region_name="Compositionally biased region"
                     /note="Basic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1243..1257
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
        1 mgaesvwasg llvlwllllv sgdqdtqdtt ttekglhmlk sgsgpiqaal aelvalpcff
       61 tlqprqsplg diprikwtkv qtasgqrqdl pilvakdnvv rvakgwqgrv slpayprhra
      121 natlllgplr asdsglyrcq vvkgiedeqd lvtlevtgvv fhyraardry altfaeaqea
      181 chlssatiaa prhlqaafed gfdncdagwl sdrtvrypit qsrpgcygdr sslpgvrsyg
      241 rrdpqelydv ycfarelgge vfyvgparrl tlagaralcq rqgaalasvg qlhlawhegl
      301 dqcdpgwlad gsvrypiqtp rrrcggsapg vrtvyrfanr tgfpapgarf daycfrahhh
      361 tpqrgdseip ssgdegeivs aegppapelk prlgeqevit pdfqeplvss gedepldltr
      421 tqasqetlas tpggptlasw lltgvtsstg vpspsslgvd meettpsgtq vaptptmrrg
      481 rfkglngrhf qqqgpedqll eaaeasaqpp tlevtadhmg psaateales dqshspwail
      541 tnevdvpgag slgsrslpes rkwspslisp stvpstdstp glkpgadeap gvksaihhpp
      601 wlpsepavps sipsealsav slqaspgdgs pdfpivamlr apklwllphs tlvpnvspip
      661 lspasplpss vpeeqavrpv sfgaedpetp fqttmaapge ashgspeads ieiegissmq
      721 atkhpisgpw asldssnvtv npvpsdagil gtesgvldlp gsptsdgqat vdmvlatwlp
      781 lpghgldtgs qstpmeahgv tmsveptval eggatkdpme atmdvvpstv datsgsepks
      841 sissthvvvt aagdqgtptl tptssegqvv aqeslgtlts lpshpwssla ssmdevasvs
      901 sgeptrlwdi pstlipvslg ldesdlkvva espglegfwe evasgqedpt dpcennpclh
      961 ggtcrtngtm ygcscdqgya genceididd clcspcengg tcidevngfi clclpsyggn
     1021 lcekdtegcd rgwhkfqghc yryfahrraw edaerdcrrr aghltsvhsp eehkfinsfg
     1081 henswiglnd rtverdfqwt dntglqyenw rekqpdnffa ggedcvvmva hengrwndvp
     1141 cnynlpyvck kgtvlcgppp avenaslvgv rkvkynvhat vryqcdegfs qhhvatircr
     1201 sngkwdrpqi vctkprrshr mrrhhhhphr hhkprkehrk hkrhpaedwe kdegdfc
//
LOCUS       NCAN_MOUSE              1268 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Neurocan core protein; AltName: Full=Chondroitin
            sulfate proteoglycan 3; Flags: Precursor.
ACCESSION   P55066
VERSION     P55066.1
DBSOURCE    UniProtKB: locus NCAN_MOUSE, accession P55066;
            class: standard.
            extra accessions:Q6P1E3,Q8C4F8
            created: Oct 1, 1996.
            sequence updated: Oct 1, 1996.
            annotation updated: Sep 13, 2023.
            xrefs: X84727.1, CAA59216.1, BC065118.1, AAH65118.1, AK082298.1,
            BAC38458.1, S52781, NP_031815.2
            xrefs (non-sequence databases): CCDS:CCDS22358.1,
            AlphaFoldDB:P55066, SMR:P55066, BioGRID:198950, IntAct:P55066,
            MINT:P55066, STRING:10090.ENSMUSP00000002412, GlyConnect:2545,
            GlyCosmos:P55066, GlyGen:P55066, iPTMnet:P55066,
            PhosphoSitePlus:P55066, SwissPalm:P55066, CPTAC:non-CPTAC-3484,
            MaxQB:P55066, PaxDb:P55066, PeptideAtlas:P55066,
            ProteomicsDB:287451, GeneID:13004, KEGG:mmu:13004, UCSC:uc009lys.2,
            AGR:MGI:104694, CTD:1463, MGI:104694, eggNOG:ENOG502QQ78,
            InParanoid:P55066, OrthoDB:5402504at2759, PhylomeDB:P55066,
            TreeFam:TF332134, Reactome:R-MMU-1971475, Reactome:R-MMU-2022870,
            Reactome:R-MMU-2022923, Reactome:R-MMU-2024101,
            Reactome:R-MMU-3000178, BioGRID-ORCS:13004, ChiTaRS:Ncan,
            PRO:PR:P55066, Proteomes:UP000000589, RNAct:P55066, GO:0005615,
            GO:0098982, GO:0098978, GO:0072534, GO:0098966, GO:0005886,
            GO:0045202, GO:0005509, GO:0030246, GO:0005540, GO:0007155,
            GO:0007417, GO:0010001, GO:0050804, GO:0002052, GO:0099175,
            GO:0051823, GO:0001501, CDD:cd00033, CDD:cd00054, CDD:cd03517,
            CDD:cd03520, Gene3D:2.10.70.10, Gene3D:2.60.40.10,
            Gene3D:2.10.25.10, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR016187,
            InterPro:IPR001881, InterPro:IPR000742, InterPro:IPR000152,
            InterPro:IPR018097, InterPro:IPR007110, InterPro:IPR036179,
            InterPro:IPR013783, InterPro:IPR003599, InterPro:IPR013106,
            InterPro:IPR000538, InterPro:IPR035976, InterPro:IPR000436,
            PANTHER:PTHR22804, PANTHER:PTHR22804:SF24, Pfam:PF00008,
            Pfam:PF00059, Pfam:PF00084, Pfam:PF07686, Pfam:PF00193,
            PRINTS:PR01265, SMART:SM00032, SMART:SM00034, SMART:SM00181,
            SMART:SM00179, SMART:SM00409, SMART:SM00445, SUPFAM:SSF56436,
            SUPFAM:SSF57535, SUPFAM:SSF57196, SUPFAM:SSF48726, PROSITE:PS00010,
            PROSITE:PS00615, PROSITE:PS50041, PROSITE:PS00022, PROSITE:PS01186,
            PROSITE:PS50026, PROSITE:PS01187, PROSITE:PS50835, PROSITE:PS01241,
            PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
            Glycoprotein; Hyaluronic acid; Immunoglobulin domain; Lectin;
            Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Rauch,U., Grimpe,B., Kulbe,G., Arnold-Ammer,I., Beier,D.R. and
            Fassler,R.
  TITLE     Structure and chromosomal localization of the mouse neurocan gene
  JOURNAL   Genomics 28 (3), 405-410 (1995)
   PUBMED   7490074
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=BALB/cJ; TISSUE=Brain
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=C57BL/6J; TISSUE=Brain
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Carninci,P., Kasukawa,T., Katayama,S., Gough,J., Frith,M.C.,
            Maeda,N., Oyama,R., Ravasi,T., Lenhard,B., Wells,C., Kodzius,R.,
            Shimokawa,K., Bajic,V.B., Brenner,S.E., Batalov,S., Forrest,A.R.,
            Zavolan,M., Davis,M.J., Wilming,L.G., Aidinis,V., Allen,J.E.,
            Ambesi-Impiombato,A., Apweiler,R., Aturaliya,R.N., Bailey,T.L.,
            Bansal,M., Baxter,L., Beisel,K.W., Bersano,T., Bono,H., Chalk,A.M.,
            Chiu,K.P., Choudhary,V., Christoffels,A., Clutterbuck,D.R.,
            Crowe,M.L., Dalla,E., Dalrymple,B.P., de Bono,B., Della Gatta,G.,
            di Bernardo,D., Down,T., Engstrom,P., Fagiolini,M., Faulkner,G.,
            Fletcher,C.F., Fukushima,T., Furuno,M., Futaki,S., Gariboldi,M.,
            Georgii-Hemming,P., Gingeras,T.R., Gojobori,T., Green,R.E.,
            Gustincich,S., Harbers,M., Hayashi,Y., Hensch,T.K., Hirokawa,N.,
            Hill,D., Huminiecki,L., Iacono,M., Ikeo,K., Iwama,A., Ishikawa,T.,
            Jakt,M., Kanapin,A., Katoh,M., Kawasawa,Y., Kelso,J., Kitamura,H.,
            Kitano,H., Kollias,G., Krishnan,S.P., Kruger,A., Kummerfeld,S.K.,
            Kurochkin,I.V., Lareau,L.F., Lazarevic,D., Lipovich,L., Liu,J.,
            Liuni,S., McWilliam,S., Madan Babu,M., Madera,M., Marchionni,L.,
            Matsuda,H., Matsuzawa,S., Miki,H., Mignone,F., Miyake,S.,
            Morris,K., Mottagui-Tabar,S., Mulder,N., Nakano,N., Nakauchi,H.,
            Ng,P., Nilsson,R., Nishiguchi,S., Nishikawa,S., Nori,F., Ohara,O.,
            Okazaki,Y., Orlando,V., Pang,K.C., Pavan,W.J., Pavesi,G.,
            Pesole,G., Petrovsky,N., Piazza,S., Reed,J., Reid,J.F., Ring,B.Z.,
            Ringwald,M., Rost,B., Ruan,Y., Salzberg,S.L., Sandelin,A.,
            Schneider,C., Schonbach,C., Sekiguchi,K., Semple,C.A., Seno,S.,
            Sessa,L., Sheng,Y., Shibata,Y., Shimada,H., Shimada,K., Silva,D.,
            Sinclair,B., Sperling,S., Stupka,E., Sugiura,K., Sultana,R.,
            Takenaka,Y., Taki,K., Tammoja,K., Tan,S.L., Tang,S., Taylor,M.S.,
            Tegner,J., Teichmann,S.A., Ueda,H.R., van Nimwegen,E., Verardo,R.,
            Wei,C.L., Yagi,K., Yamanishi,H., Zabarovsky,E., Zhu,S., Zimmer,A.,
            Hide,W., Bult,C., Grimmond,S.M., Teasdale,R.D., Liu,E.T.,
            Brusic,V., Quackenbush,J., Wahlestedt,C., Mattick,J.S., Hume,D.A.,
            Kai,C., Sasaki,D., Tomaru,Y., Fukuda,S., Kanamori-Katayama,M.,
            Suzuki,M., Aoki,J., Arakawa,T., Iida,J., Imamura,K., Itoh,M.,
            Kato,T., Kawaji,H., Kawagashira,N., Kawashima,T., Kojima,M.,
            Kondo,S., Konno,H., Nakano,K., Ninomiya,N., Nishio,T., Okada,M.,
            Plessy,C., Shibata,K., Shiraki,T., Suzuki,S., Tagami,M., Waki,K.,
            Watahiki,A., Okamura-Oho,Y., Suzuki,H., Kawai,J. and Hayashizaki,Y.
  CONSRTM   FANTOM Consortium; RIKEN Genome Exploration Research Group and
            Genome Science Group (Genome Network Project Core Group)
  TITLE     The transcriptional landscape of the mammalian genome
  JOURNAL   Science 309 (5740), 1559-1563 (2005)
   PUBMED   16141072
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1052-1268.;
            STRAIN=C57BL/6J; TISSUE=Cerebellum
            Erratum:[Science. 2006 Mar 24;311(5768):1713]
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Brain
COMMENT     On Mar 15, 2005 this sequence version replaced gi:1083430.
            [FUNCTION] May modulate neuronal adhesion and neurite growth during
            development by binding to neural cell adhesion molecules (NG-CAM
            and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic
            acid.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000250|UniProtKB:O14594}.
            [TISSUE SPECIFICITY] Brain.
            [PTM] O-glycosylated; contains chondroitin sulfate.
            {ECO:0000250|UniProtKB:O14594}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Neurocan;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_156'.
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..1268
                     /gene="Ncan"
                     /gene_synonym="Cspg3"
     Protein         1..1268
                     /product="Neurocan core protein"
                     /note="Chondroitin sulfate proteoglycan 3"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          23..1268
                     /region_name="Mature chain"
                     /note="Neurocan core protein. /id=PRO_0000017517."
     Region          37..157
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          40..161
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:448366"
     Region          54..58
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Bond            bond(58,139)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          74..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          122..126
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          136..141
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          154..157
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          159..254
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          159..253
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            169..170
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(181,252)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(205,226)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          258..356
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          260..355
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            267..268
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(279,354)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(303,324)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            339
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          363..391
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            380
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14594."
     Region          <400..851
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          406..442
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            410
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14594."
     Region          423..442
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          472..540
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          574..630
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          582
                     /region_name="Conflict"
                     /note="E -> D (in Ref. 2; AAH65118).
                     /evidence=ECO:0000305."
     Region          587
                     /region_name="Conflict"
                     /note="P -> A (in Ref. 2; AAH65118).
                     /evidence=ECO:0000305."
     Site            742
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          936
                     /region_name="Conflict"
                     /note="V -> D (in Ref. 2; AAH65118).
                     /evidence=ECO:0000305."
     Region          947
                     /region_name="Conflict"
                     /note="E -> K (in Ref. 2; AAH65118).
                     /evidence=ECO:0000305."
     Region          960..996
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          964..994
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Bond            bond(964,975)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(969,984)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            978
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(986,995)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          998..1034
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          998..1034
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(998,1001,1015)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(1002,1013)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1007,1022)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1024,1033)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1036..1165
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          1040..1163
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(1040,1051)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(1068,1160)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(1134,1138,1140,1146,1148..1151,1154..1156)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(1136,1152)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1165..1225
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          1167..1224
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(1167,1210)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            1175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(1177,1197)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(1196,1223)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          1228..1268
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1228..1253
                     /region_name="Compositionally biased region"
                     /note="Basic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1254..1268
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
        1 mgagsvwasg llllwllllv agdqdtqdtt atekglrmlk sgsgpvraal aelvalpcff
       61 tlqprlsslr diprikwtkv qtasgqrqdl pilvakdnvv rvakgwqgrv slpayprhra
      121 natlllgplr asdsglyrcq vvkgiedeqd lvtlevtgvv fhyraardry altfaeaqea
      181 crlssatiaa prhlqaafed gfdncdagwl sdrtvrypit qsrpgcygdr sslpgvrsyg
      241 rrdpqelydv ycfarelgge vfyvgparrl tlagaraqcq rqgaalasvg qlhlawhegl
      301 dqcdpgwlad gsvrypiqtp rrrcggpapg vrtvyrfanr tgfpapgarf daycfrahhh
      361 taqhgdseip ssgdegeivs aegppgrelk pslgeqevia pdfqeplmss gegeppdltw
      421 tqapeetlgs tpggptlasw pssekwlftg apssmgvssp sdmgvdmeat tplgtqvapt
      481 ptmrrgrfkg lngrhfqqqg pedqlpevae psaqpptlga tanhmrpsaa teasesdqsh
      541 spwailtnev depgagslgs rslpeslmws pslispsvps testpspkpg aaeapsvksa
      601 iphlprlpse ppapspgpse alsavslqas sadgspdfpi vamlrapklw llprstlvpn
      661 mtpvplspas plpswvpeeq avrpvslgae dletpfqtti aapveashrs pdadsieieg
      721 tssmratkhp isgpwaslds snvtmnpvps dagilgtesg vldlpgspts ggqatvekvl
      781 atwlplpgqg ldpgsqstpm eahgvavsme ptvaleggat egpmeatrev vpstadatwe
      841 sesrsaisst hiavtmaraq gmptltstss eghpepkgqm vaqeslepln tlpshpwssl
      901 vvpmdevasv ssgeptglwd ipstlipvsl gldesvlnvv aespsvegfw eevasgqedp
      961 tdpcennpcl hggtchtngt vygcscdqgy agenceidid dclcspceng gtcidevngf
     1021 iclclpsygg slcekdtegc drgwhkfqgh cyryfahrra wedaerdcrr raghltsvhs
     1081 peehkfinsf ghenswigln drtverdfqw tdntglqyen wrekqpdnff aggedcvvmv
     1141 ahesgrwndv pcnynlpyvc kkgtvlcgpp pavenaslvg vrkikynvha tvryqcdegf
     1201 sqhrvatirc rnngkwdrpq imcikprrsh rmrrhhhhph rhhkprkehr khkrhpaedw
     1261 ekdegdfc
//
LOCUS       CLC4E_HUMAN              219 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 4 member E; AltName:
            Full=C-type lectin superfamily member 9; AltName:
            Full=Macrophage-inducible C-type lectin; Short=MINCLE.
ACCESSION   Q9ULY5
VERSION     Q9ULY5.1
DBSOURCE    UniProtKB: locus CLC4E_HUMAN, accession Q9ULY5;
            class: standard.
            extra accessions:B2R6Q6
            created: Feb 15, 2005.
            sequence updated: May 1, 2000.
            annotation updated: Sep 13, 2023.
            xrefs: AB024718.1, BAA83755.1, AY358499.1, AAQ88863.1, AK312671.1,
            BAG35553.1, AC092746.9, CH471116.2, EAW88618.1, BC000715.2,
            AAH00715.1, NP_055173.1, 3WH2_A, 3WH3_A
            xrefs (non-sequence databases): CCDS:CCDS8594.1, PDBsum:3WH2,
            PDBsum:3WH3, AlphaFoldDB:Q9ULY5, SMR:Q9ULY5, BioGRID:117639,
            CORUM:Q9ULY5, IntAct:Q9ULY5, STRING:9606.ENSP00000299663,
            ChEMBL:CHEMBL4105898, DrugBank:DB04540, GuidetoPHARMACOLOGY:2929,
            UniLectin:Q9ULY5, GlyCosmos:Q9ULY5, GlyGen:Q9ULY5, iPTMnet:Q9ULY5,
            PhosphoSitePlus:Q9ULY5, BioMuta:CLEC4E, DMDM:59797976, EPD:Q9ULY5,
            MassIVE:Q9ULY5, PaxDb:Q9ULY5, PeptideAtlas:Q9ULY5,
            ProteomicsDB:85152, Antibodypedia:23066, DNASU:26253,
            Ensembl:ENST00000299663.8, Ensembl:ENSP00000299663.3,
            Ensembl:ENSG00000166523.8, GeneID:26253, KEGG:hsa:26253,
            MANE-Select:ENST00000299663.8, UCSC:uc001quo.2, AGR:HGNC:14555,
            CTD:26253, DisGeNET:26253, GeneCards:CLEC4E, HGNC:14555,
            HPA:ENSG00000166523, MIM:609962, neXtProt:NX_Q9ULY5,
            OpenTargets:ENSG00000166523, PharmGKB:PA26586,
            VEuPathDB:HostDB:ENSG00000166523, eggNOG:KOG4297,
            GeneTree:ENSGT00940000160666, HOGENOM:CLU_049894_7_5_1,
            InParanoid:Q9ULY5, OMA:RREFYIG, OrthoDB:2881452at2759,
            PhylomeDB:Q9ULY5, TreeFam:TF333341, PathwayCommons:Q9ULY5,
            Reactome:R-HSA-5621480, SignaLink:Q9ULY5, BioGRID-ORCS:26253,
            GenomeRNAi:26253, Pharos:Q9ULY5, PRO:PR:Q9ULY5,
            Proteomes:UP000005640, RNAct:Q9ULY5, Bgee:ENSG00000166523,
            ExpressionAtlas:Q9ULY5, Genevisible:Q9ULY5, GO:0042995, GO:0009897,
            GO:0016020, GO:0001891, GO:0030670, GO:0005886, GO:0005509,
            GO:0030246, GO:0051861, GO:0038187, GO:0061760, GO:0042742,
            GO:0038094, GO:0045087, GO:0002221, GO:0001819, GO:0002292,
            CDD:cd03590, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR033989, InterPro:IPR016187,
            PANTHER:PTHR22802:SF402, PANTHER:PTHR22802, Pfam:PF00059,
            SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS50041
KEYWORDS    3D-structure; Calcium; Cell membrane; Cell projection; Disulfide
            bond; Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
            Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
            Transmembrane helix.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Matsumoto,M., Tanaka,T., Kaisho,T., Sanjo,H., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A. and Akira,S.
  TITLE     A novel LPS-inducible C-type lectin is a transcriptional target of
            NF-IL6 in macrophages
  JOURNAL   J Immunol 163 (9), 5039-5048 (1999)
   PUBMED   10528209
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            TISSUE=Monocytic leukemia
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
            Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Scherer,S.E., Muzny,D.M., Buhay,C.J., Chen,R., Cree,A., Ding,Y.,
            Dugan-Rocha,S., Gill,R., Gunaratne,P., Harris,R.A., Hawes,A.C.,
            Hernandez,J., Hodgson,A.V., Hume,J., Jackson,A., Khan,Z.M.,
            Kovar-Smith,C., Lewis,L.R., Lozado,R.J., Metzker,M.L.,
            Milosavljevic,A., Miner,G.R., Montgomery,K.T., Morgan,M.B.,
            Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z., Steffen,D.,
            Lovering,R.C., Wheeler,D.A., Worley,K.C., Yuan,Y., Zhang,Z.,
            Adams,C.Q., Ansari-Lari,M.A., Ayele,M., Brown,M.J., Chen,G.,
            Chen,Z., Clerc-Blankenburg,K.P., Davis,C., Delgado,O., Dinh,H.H.,
            Draper,H., Gonzalez-Garay,M.L., Havlak,P., Jackson,L.R.,
            Jacob,L.S., Kelly,S.H., Li,L., Li,Z., Liu,J., Liu,W., Lu,J.,
            Maheshwari,M., Nguyen,B.V., Okwuonu,G.O., Pasternak,S., Perez,L.M.,
            Plopper,F.J., Santibanez,J., Shen,H., Tabor,P.E., Verduzco,D.,
            Waldron,L., Wang,Q., Williams,G.A., Zhang,J., Zhou,J., Allen,C.C.,
            Amin,A.G., Anyalebechi,V., Bailey,M., Barbaria,J.A., Bimage,K.E.,
            Bryant,N.P., Burch,P.E., Burkett,C.E., Burrell,K.L., Calderon,E.,
            Cardenas,V., Carter,K., Casias,K., Cavazos,I., Cavazos,S.R.,
            Ceasar,H., Chacko,J., Chan,S.N., Chavez,D., Christopoulos,C.,
            Chu,J., Cockrell,R., Cox,C.D., Dang,M., Dathorne,S.R., David,R.,
            Davis,C.M., Davy-Carroll,L., Deshazo,D.R., Donlin,J.E., D'Souza,L.,
            Eaves,K.A., Egan,A., Emery-Cohen,A.J., Escotto,M., Flagg,N.,
            Forbes,L.D., Gabisi,A.M., Garza,M., Hamilton,C., Henderson,N.,
            Hernandez,O., Hines,S., Hogues,M.E., Huang,M., Idlebird,D.G.,
            Johnson,R., Jolivet,A., Jones,S., Kagan,R., King,L.M., Leal,B.,
            Lebow,H., Lee,S., LeVan,J.M., Lewis,L.C., London,P.,
            Lorensuhewa,L.M., Loulseged,H., Lovett,D.A., Lucier,A.,
            Lucier,R.L., Ma,J., Madu,R.C., Mapua,P., Martindale,A.D.,
            Martinez,E., Massey,E., Mawhiney,S., Meador,M.G., Mendez,S.,
            Mercado,C., Mercado,I.C., Merritt,C.E., Miner,Z.L., Minja,E.,
            Mitchell,T., Mohabbat,F., Mohabbat,K., Montgomery,B., Moore,N.,
            Morris,S., Munidasa,M., Ngo,R.N., Nguyen,N.B., Nickerson,E.,
            Nwaokelemeh,O.O., Nwokenkwo,S., Obregon,M., Oguh,M., Oragunye,N.,
            Oviedo,R.J., Parish,B.J., Parker,D.N., Parrish,J., Parks,K.L.,
            Paul,H.A., Payton,B.A., Perez,A., Perrin,W., Pickens,A.,
            Primus,E.L., Pu,L.L., Puazo,M., Quiles,M.M., Quiroz,J.B.,
            Rabata,D., Reeves,K., Ruiz,S.J., Shao,H., Sisson,I., Sonaike,T.,
            Sorelle,R.P., Sutton,A.E., Svatek,A.F., Svetz,L.A., Tamerisa,K.S.,
            Taylor,T.R., Teague,B., Thomas,N., Thorn,R.D., Trejos,Z.Y.,
            Trevino,B.K., Ukegbu,O.N., Urban,J.B., Vasquez,L.I., Vera,V.A.,
            Villasana,D.M., Wang,L., Ward-Moore,S., Warren,J.T., Wei,X.,
            White,F., Williamson,A.L., Wleczyk,R., Wooden,H.S., Wooden,S.H.,
            Yen,J., Yoon,L., Yoon,V., Zorrilla,S.E., Nelson,D.,
            Kucherlapati,R., Weinstock,G. and Gibbs,R.A.
  CONSRTM   Baylor College of Medicine Human Genome Sequencing Center Sequence
            Production Team
  TITLE     The finished DNA sequence of human chromosome 12
  JOURNAL   Nature 440 (7082), 346-351 (2006)
   PUBMED   16541075
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Mural,R.J., Istrail,S., Sutton,G.G., Florea,L., Halpern,A.L.,
            Mobarry,C.M., Lippert,R., Walenz,B., Shatkay,H., Dew,I.,
            Miller,J.R., Flanigan,M.J., Edwards,N.J., Bolanos,R., Fasulo,D.,
            Halldorsson,B.V., Hannenhalli,S., Turner,R., Yooseph,S., Lu,F.,
            Nusskern,D.R., Shue,B.C., Zheng,X.H., Zhong,F., Delcher,A.L.,
            Huson,D.H., Kravitz,S.A., Mouchard,L., Reinert,K., Remington,K.A.,
            Clark,A.G., Waterman,M.S., Eichler,E.E., Adams,M.D.,
            Hunkapiller,M.W., Myers,E.W. and Venter,J.C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-SEP-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Kidney
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Bugarcic,A., Hitchens,K., Beckhouse,A.G., Wells,C.A., Ashman,R.B.
            and Blanchard,H.
  TITLE     Human and mouse macrophage-inducible C-type lectin (Mincle) bind
            Candida albicans
  JOURNAL   Glycobiology 18 (9), 679-685 (2008)
   PUBMED   18509109
  REMARK    FUNCTION AS RECEPTOR FOR CANDIDA ALBICANS, AND SUBUNIT.
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Wells,C.A., Salvage-Jones,J.A., Li,X., Hitchens,K., Butcher,S.,
            Murray,R.Z., Beckhouse,A.G., Lo,Y.L., Manzanero,S., Cobbold,C.,
            Schroder,K., Ma,B., Orr,S., Stewart,L., Lebus,D., Sobieszczuk,P.,
            Hume,D.A., Stow,J., Blanchard,H. and Ashman,R.B.
  TITLE     The macrophage-inducible C-type lectin, mincle, is an essential
            component of the innate immune response to Candida albicans
  JOURNAL   J Immunol 180 (11), 7404-7413 (2008)
   PUBMED   18490740
  REMARK    SUBCELLULAR LOCATION.
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Yamasaki,S., Ishikawa,E., Sakuma,M., Hara,H., Ogata,K. and Saito,T.
  TITLE     Mincle is an ITAM-coupled activating receptor that senses damaged
            cells
  JOURNAL   Nat Immunol 9 (10), 1179-1188 (2008)
   PUBMED   18776906
  REMARK    INTERACTION WITH FCER1G.
REFERENCE   10 (residues 1 to 219)
  AUTHORS   Miyake,Y., Toyonaga,K., Mori,D., Kakuta,S., Hoshino,Y., Oyamada,A.,
            Yamada,H., Ono,K., Suyama,M., Iwakura,Y., Yoshikai,Y. and
            Yamasaki,S.
  TITLE     C-type lectin MCL is an FcRgamma-coupled receptor that mediates the
            adjuvanticity of mycobacterial cord factor
  JOURNAL   Immunity 38 (5), 1050-1062 (2013)
   PUBMED   23602766
  REMARK    FUNCTION, AND TISSUE SPECIFICITY.
REFERENCE   11 (residues 1 to 219)
  AUTHORS   Furukawa,A., Kamishikiryo,J., Mori,D., Toyonaga,K., Okabe,Y.,
            Toji,A., Kanda,R., Miyake,Y., Ose,T., Yamasaki,S. and Maenaka,K.
  TITLE     Structural analysis for glycolipid recognition by the C-type
            lectins Mincle and MCL
  JOURNAL   Proc Natl Acad Sci U S A 110 (43), 17438-17443 (2013)
   PUBMED   24101491
  REMARK    X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 74-219 IN COMPLEX WITH
            CALCIUM, FUNCTION, MUTAGENESIS OF 169-GLU--ASN-171; ASN-172;
            ARG-183 AND 198-PHE-LEU-199, SUBCELLULAR LOCATION, AND MOTIF.
COMMENT     [FUNCTION] Calcium-dependent lectin that acts as a pattern
            recognition receptor (PRR) of the innate immune system: recognizes
            damage-associated molecular patterns (DAMPs) of abnormal self and
            pathogen-associated molecular patterns (PAMPs) of bacteria and
            fungi (PubMed:18509109, PubMed:23602766). The PAMPs notably include
            mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall
            glycolipid with potent adjuvant immunomodulatory functions
            (PubMed:23602766, PubMed:24101491). Interacts with signaling
            adapter Fc receptor gamma chain/FCER1G to form a functional complex
            in myeloid cells (By similarity). Binding of mycobacterial
            trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to
            phosphorylation of the immunoreceptor tyrosine-based activation
            motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and
            NF-kappa-B, consequently driving maturation of antigen-presenting
            cells and shaping antigen-specific priming of T-cells toward
            effector T-helper 1 and T-helper 17 cell subtypes (By similarity).
            Also recognizes alpha-mannose residues on pathogenic fungi of the
            genus Malassezia and mediates macrophage activation (By
            similarity). Through recognition of DAMPs released upon
            nonhomeostatic cell death, enables immune sensing of damaged self
            and promotes inflammatory cell infiltration into the damaged tissue
            (By similarity). {ECO:0000250|UniProtKB:Q9R0Q8,
            ECO:0000269|PubMed:18509109, ECO:0000269|PubMed:23602766,
            ECO:0000269|PubMed:24101491}.
            [SUBUNIT] Monomer and homodimer (PubMed:18509109). Interacts with
            signaling adapter Fc receptor gamma chain/FCER1G to form a
            functional complex; the interaction is direct (By similarity).
            Alternatively, acts as a bridge for interaction between CLEC4D and
            FCER1G. A heterodimer of CLEC4E and CLEC4D associates with FCER1G
            to form a functional complex (By similarity). Interacts with SAP130
            nuclear protein that is released from necrotic cells; the
            interaction is direct (By similarity).
            {ECO:0000250|UniProtKB:Q67EQ1, ECO:0000250|UniProtKB:Q9R0Q8,
            ECO:0000269|PubMed:18509109}.
            [INTERACTION] Q9ULY5; Q07325: CXCL9; NbExp=3; IntAct=EBI-12807010,
            EBI-3911467; Q9ULY5; Q92520: FAM3C; NbExp=3; IntAct=EBI-12807010,
            EBI-2876774; Q9ULY5; Q16617: NKG7; NbExp=4; IntAct=EBI-12807010,
            EBI-3919611.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000269|PubMed:18490740,
            ECO:0000305|PubMed:24101491}; Single-pass type II membrane protein
            {ECO:0000305}. Cell projection, phagocytic cup
            {ECO:0000250|UniProtKB:Q9R0Q8}.
            [TISSUE SPECIFICITY] Expressed in monocytes and macrophages.
            {ECO:0000269|PubMed:23602766}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Mincle;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_hum_Ctlect_00134'.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..219
                     /gene="CLEC4E"
                     /locus_tag="UNQ218/PRO244"
                     /gene_synonym="CLECSF9"
                     /gene_synonym="MINCLE"
     Protein         1..219
                     /product="C-type lectin domain family 4 member E"
                     /note="C-type lectin superfamily member 9;
                     Macrophage-inducible C-type lectin; MINCLE"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..219
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 4 member E.
                     /id=PRO_0000046619."
     Region          1..19
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          20..40
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          41..219
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Site            62
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          80..207
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(80,91)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          85..87
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
     Region          87..206
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          90..94
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
     Region          101..110
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(108,205)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          121..130
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
     Site            order(136,169,171,177,183..184,193..196)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Region          137..143
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
     Site            order(143,147,172,177..178)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(147,178)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Region          150..152
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
     Region          169..171
                     /region_name="Short sequence motif of biological interest"
                     /note="Confers specificity for glucose/mannose-type
                     carbohydrates. /evidence=ECO:0000303|PubMed:24101491."
     Site            169..171
                     /site_type="mutagenized"
                     /note="EPN->QPD,EPD: Impairs binding to
                     trehalose-6,6'-dimycolate.
                     /evidence=ECO:0000269|PubMed:24101491."
     Site            172
                     /site_type="mutagenized"
                     /note="N->Q: Impairs trehalose-6,6'-dimycolate
                     (TDM)-induced NF-kappa-B activation.
                     /evidence=ECO:0000269|PubMed:24101491."
     Region          174..182
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
     Bond            bond(179,197)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            183
                     /site_type="mutagenized"
                     /note="R->V: Reduces trehalose-6,6'-dimycolate
                     (TDM)-induced NF-kappa-B activation.
                     /evidence=ECO:0000269|PubMed:24101491."
     Region          192..196
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
     Site            198..199
                     /site_type="mutagenized"
                     /note="FL->AA: Reduces trehalose-6,6'-dimycolate
                     (TDM)-induced NF-kappa-B activation.
                     /evidence=ECO:0000269|PubMed:24101491."
     Region          201..208
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WH2."
ORIGIN
        1 mnsskssetq ctergcfssq mflwtvagip ilflsacfit rcvvtfrifq tcdekkfqlp
       61 enftelscyn ygsgsvkncc plnweyfqss cyffstdtis walslkncsa mgahlvvins
      121 qeeqeflsyk kpkmreffig lsdqvvegqw qwvdgtpltk slsfwdvgep nniatledca
      181 tmrdssnprq nwndvtcfln yfricemvgi nplnkgksl
//
LOCUS       CLC6A_BOVIN              206 aa            linear   MAM 28-JUN-2023
DEFINITION  RecName: Full=C-type lectin domain family 6 member A; AltName:
            Full=Dendritic cell-associated C-type lectin 2; Short=DC-associated
            C-type lectin 2; Short=Dectin-2.
ACCESSION   Q3LUH2
VERSION     Q3LUH2.1
DBSOURCE    UniProtKB: locus CLC6A_BOVIN, accession Q3LUH2;
            class: standard.
            extra accessions:Q3LUH1
            created: Jun 28, 2011.
            sequence updated: Oct 25, 2005.
            annotation updated: Jun 28, 2023.
            xrefs: DQ176046.1, ABA08411.1, DQ176047.1, ABA08412.1,
            NP_001029651.1
            xrefs (non-sequence databases): AlphaFoldDB:Q3LUH2, SMR:Q3LUH2,
            STRING:9913.ENSBTAP00000032278, GlyCosmos:Q3LUH2, PaxDb:Q3LUH2,
            Ensembl:ENSBTAT00000032346, Ensembl:ENSBTAP00000032279,
            Ensembl:ENSBTAG00000023635, GeneID:514979, KEGG:bta:514979,
            CTD:93978, VEuPathDB:HostDB:ENSBTAG00000023635, eggNOG:KOG4297,
            GeneTree:ENSGT00940000162938, HOGENOM:CLU_049894_7_5_1,
            InParanoid:Q3LUH2, OrthoDB:2881452at2759, Reactome:R-BTA-5621480,
            Reactome:R-BTA-6798695, Proteomes:UP000009136,
            Bgee:ENSBTAG00000023635, ExpressionAtlas:Q3LUH2, GO:0009897,
            GO:0005886, GO:0005509, GO:0030246, GO:0005537, GO:0038187,
            GO:0002250, GO:0061760, GO:0050832, GO:0045087, GO:0001819,
            GO:0043123, GO:2000318, CDD:cd03590, Gene3D:3.10.100.10,
            InterPro:IPR001304, InterPro:IPR016186, InterPro:IPR018378,
            InterPro:IPR033989, InterPro:IPR016187, PANTHER:PTHR46784,
            PANTHER:PTHR46784:SF1, Pfam:PF00059, SMART:SM00034,
            SUPFAM:SSF56436, PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Adaptive immunity; Alternative splicing; Calcium; Cell membrane;
            Disulfide bond; Glycoprotein; Immunity; Innate immunity; Lectin;
            Membrane; Metal-binding; Reference proteome; Signal-anchor;
            Transmembrane; Transmembrane helix.
SOURCE      Bos taurus (cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Bonkobara,M., Hoshino,M., Yagihara,H., Tamura,K., Isotani,M.,
            Tanaka,Y., Washizu,T. and Ariizumi,K.
  TITLE     Identification and gene expression of bovine C-type lectin dectin-2
  JOURNAL   Vet Immunol Immunopathol 110 (1-2), 179-186 (2006)
   PUBMED   16213030
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE
            SPECIFICITY.
COMMENT     On Jun 29, 2011 this sequence version replaced gi:122139907.
            [FUNCTION] Calcium-dependent lectin that acts as a pattern
            recognition receptor (PRR) of the innate immune system:
            specifically recognizes and binds alpha-mannans on C.albicans
            hypheas (By similarity). Binding of C.albicans alpha-mannans to
            this receptor complex leads to phosphorylation of the
            immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G,
            triggering activation of SYK, CARD9 and NF-kappa-B, consequently
            driving maturation of antigen-presenting cells and shaping
            antigen-specific priming of T-cells toward effector T-helper 1 and
            T-helper 17 cell subtypes (By similarity). Recognizes also, in a
            mannose-dependent manner, allergens from house dust mite and fungi,
            by promoting cysteinyl leukotriene production. Recognizes soluble
            elements from the eggs of Shistosoma mansoni altering adaptive
            immune responses (By similarity). {ECO:0000250|UniProtKB:Q6EIG7,
            ECO:0000250|UniProtKB:Q9JKF4}.
            [SUBUNIT] Associated with FCER1G (By similarity). Heterodimer with
            CLEC4D; this heterodimer forms a pattern recognition receptor (PRR)
            against fungal infection (By similarity).
            {ECO:0000250|UniProtKB:Q6EIG7, ECO:0000250|UniProtKB:Q9JKF4}.
            [SUBCELLULAR LOCATION] Cell membrane
            {ECO:0000250|UniProtKB:Q6EIG7}; Single-pass type II membrane
            protein {ECO:0000305}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1; IsoId=Q3LUH2-1; Sequence=Displayed; Name=2;
            IsoId=Q3LUH2-2; Sequence=VSP_041515.
            [TISSUE SPECIFICITY] Expressed at the highest levels in lymph
            nodes, at moderate levels in skin, small intestine, liver, and
            lung, and at lower levels in abomasum and spleen, but is not in the
            brain. Abundantly expressed by Langerhans cells compared to
            macrophages. {ECO:0000269|PubMed:16213030}.
            [DOMAIN] A short stretch of the intracellular domain (AA 8-14)
            proximal to the transmembrane domain is required for association
            with Fc receptor gamma chain. {ECO:0000250|UniProtKB:Q9JKF4}.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
     gene            1..206
                     /gene="CLEC6A"
                     /gene_synonym="DECTIN2"
     Protein         1..206
                     /product="C-type lectin domain family 6 member A"
                     /note="Dendritic cell-associated C-type lectin 2;
                     DC-associated C-type lectin 2; Dectin-2"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..206
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 6 member A.
                     /id=PRO_0000410824."
     Region          1..15
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          16..36
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          36..69
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:16213030. /id=VSP_041515."
     Region          37..206
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(61,75)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q6EIG7."
     Region          76..201
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(76,87)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q6EIG7,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          83..200
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(104,199)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(132,165,167,171,177..178,187..190)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(139,143,171..172)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(143,172)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(173,191)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mvregnaesc frmrlwciav lglallsacf ivscvvtyyf thgntgkrls elhthhsnlt
       61 cfsegtrvte kiwgccpgtw kpfgsscyfi sseenfwaks eqncigmgah lvvinteteq
      121 dfiiqqlnkt fsyflglsdp qgngnwqwid qtpykenvrf whqnepnfsa eecasvvfwd
      181 grgwgwndvf cdskrksice mkkiyl
//
LOCUS       LECE_HELCR               147 aa            linear   INV 22-FEB-2023
DEFINITION  RecName: Full=Echinoidin.
ACCESSION   P06027
VERSION     P06027.1
DBSOURCE    UniProtKB: locus LECE_HELCR, accession P06027;
            class: standard.
            created: Aug 13, 1987.
            sequence updated: Aug 13, 1987.
            annotation updated: Feb 22, 2023.
            xrefs: A26697
            xrefs (non-sequence databases): AlphaFoldDB:P06027, SMR:P06027,
            iPTMnet:P06027, GO:0005576, GO:0030246, CDD:cd03589,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033988, InterPro:IPR016187,
            PANTHER:PTHR22803:SF145, PANTHER:PTHR22803, Pfam:PF00059,
            SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
            Secreted.
SOURCE      Heliocidaris crassispina
  ORGANISM  Heliocidaris crassispina
            Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa;
            Echinoidea; Euechinoidea; Echinacea; Camarodonta; Echinidea;
            Echinometridae; Heliocidaris.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Giga,Y., Ikai,A. and Takahashi,K.
  TITLE     The complete amino acid sequence of echinoidin, a lectin from the
            coelomic fluid of the sea urchin Anthocidaris crassispina.
            Homologies with mammalian and insect lectins
  JOURNAL   J Biol Chem 262 (13), 6197-6203 (1987)
   PUBMED   3571253
  REMARK    PROTEIN SEQUENCE, AND GLYCOSYLATION AT SER-38.
COMMENT     On Jan 20, 2006 this sequence version replaced gi:85328.
            [FUNCTION] Role in the defense system of the organism against
            microorganisms. This lectin is specific for Gal-GalNAc.
            [SUBUNIT] Homodimer; disulfide-linked.
            [SUBCELLULAR LOCATION] Secreted.
            [TISSUE SPECIFICITY] Coelemic fluid.
            [PTM] The identity of the saccharide is not reported in
            PubMed:3571253, and it is unlikely to be N-acetylgalactosamine. The
            sugar attached to Ser-38 is represented simply as Hex.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Heliocidaris crassispina"
                     /db_xref="taxon:1043166"
     Protein         1..147
                     /product="Echinoidin"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..147
                     /region_name="Mature chain"
                     /note="Echinoidin. /id=PRO_0000046641."
     Region          1..143
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(2)
                     /bond_type="disulfide"
                     /note="Interchain."
     Region          3..143
                     /region_name="CLECT_CEL-1_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in CEL-1 from Cucumaria echinata and Echinoidin from
                     Anthocidaris crassispina; cd03589"
                     /db_xref="CDD:153059"
     Bond            bond(3,14)
                     /bond_type="disulfide"
     Site            order(4..5,11,34,36)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153059"
     Bond            bond(31,141)
                     /bond_type="disulfide"
     Site            38
                     /site_type="glycosylation"
                     /note="O-linked (Hex) serine.
                     /evidence=ECO:0000269|PubMed:3571253."
     Region          39..41
                     /region_name="Short sequence motif of biological interest"
                     /note="Cell attachment site. /evidence=ECO:0000255."
     Site            order(82,86,109,114..115)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153059"
     Site            order(86,115)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153059"
     Site            order(106,108,114,120,128..129)
                     /site_type="other"
                     /note="carbohydrate binding [chemical binding]"
                     /db_xref="CDD:153059"
     Bond            bond(116,132)
                     /bond_type="disulfide"
ORIGIN
        1 gccptfwtsf gsncyrffav sltwaegeqf cqsfsvpsrg didsighlvs ihseteqnfv
       61 yhyfetstkd dttpemwlgf ndrttegnfq wtdgspndft awvgsnpdny gsgedctqmv
      121 mgaglnwidl pcsstrhyli cklplwe
//
LOCUS       LECA_PLEWA               172 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Lectin; Flags: Precursor.
ACCESSION   Q02988
VERSION     Q02988.1
DBSOURCE    UniProtKB: locus LECA_PLEWA, accession Q02988;
            class: standard.
            created: Jun 1, 1994.
            sequence updated: Jun 1, 1994.
            annotation updated: Feb 22, 2023.
            xrefs: X69062.1, CAA48800.1, S32489
            xrefs (non-sequence databases): AlphaFoldDB:Q02988, SMR:Q02988,
            MEROPS:I63.002, GlyCosmos:Q02988, GO:0005576, GO:0030246,
            CDD:cd00037, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR016187,
            PANTHER:PTHR22803, PANTHER:PTHR22803:SF116, Pfam:PF00059,
            PRINTS:PR01504, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
            Secreted; Signal.
SOURCE      Pleurodeles waltl (Iberian ribbed newt)
  ORGANISM  Pleurodeles waltl
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Amphibia; Batrachia; Caudata; Salamandroidea; Salamandridae;
            Pleurodelinae; Pleurodeles.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Tiffoche,C., Chesnel,A., Jego,P. and Le Pennec,J.P.
  TITLE     Isolation and characterization of a cDNA clone encoding a
            Pleurodeles lectin
  JOURNAL   Eur J Biochem 213 (3), 901-907 (1993)
   PUBMED   8504829
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-34 AND
            28-53.;
            TISSUE=Oviduct
COMMENT     On Oct 25, 2005 this sequence version replaced gi:479197.
            [FUNCTION] May be involved in protection of eggs and embryos
            against microorganisms. Calcium-dependent lectin with specificity
            to D-glucose and D-glucosamine. Can agglutinate microorganisms in
            vivo.
            [SUBUNIT] Heterodimer. {ECO:0000305}.
            [SUBCELLULAR LOCATION] Secreted. Note=Secreted into the inner layer
            of egg jelly.
            [TISSUE SPECIFICITY] Anterior part of oviduct.
            [MISCELLANEOUS] Protein synthesis increases significantly under
            estradiol stimulation.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Pleurodeles waltl"
                     /db_xref="taxon:8319"
     gene            1..172
                     /gene="LEC"
     Protein         1..172
                     /product="Lectin"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..20
                     /region_name="Signal"
                     /note="/evidence=ECO:0000269|PubMed:8504829."
     Region          21..172
                     /region_name="Mature chain"
                     /note="Lectin. /id=PRO_0000017396."
     Region          36..172
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          37..165
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Bond            bond(65,164)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(138,142,144,150,152..155,158..160)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(140,156)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mvwcladlra yvlvllvisg lyqgsdqlip ekcgedctpg wdchfnsyyk yipnakswtd
       61 aefycqklyp gahlasihse dendflteit fknnsnypvv wvggsdcykd rsfvwtdgsq
      121 wdyqkwrqwe psntggrepc idfnfvtpgl wndehcdqkf pfickyttpc ry
//
LOCUS       CLC6A_MOUSE              209 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 6 member A; AltName:
            Full=C-type lectin superfamily member 10; AltName: Full=Dendritic
            cell-associated C-type lectin 2; Short=DC-associated C-type lectin
            2; Short=Dectin-2.
ACCESSION   Q9JKF4
VERSION     Q9JKF4.1
DBSOURCE    UniProtKB: locus CLC6A_MOUSE, accession Q9JKF4;
            class: standard.
            extra accessions:Q9JKF2,Q9JKF3
            created: Feb 15, 2005.
            sequence updated: Oct 1, 2000.
            annotation updated: Sep 13, 2023.
            xrefs: AF240357.1, AAF67177.1, AF240358.1, AAF67178.1, AF240359.1,
            AAF67179.1, BC023008.1, AAH23008.1, NP_001177250.1, NP_064385.1
            xrefs (non-sequence databases): CCDS:CCDS20512.1, CCDS:CCDS51895.1,
            AlphaFoldDB:Q9JKF4, SMR:Q9JKF4, STRING:10090.ENSMUSP00000024118,
            GlyCosmos:Q9JKF4, GlyGen:Q9JKF4, iPTMnet:Q9JKF4,
            PhosphoSitePlus:Q9JKF4, MaxQB:Q9JKF4, PaxDb:Q9JKF4,
            Antibodypedia:23055, DNASU:56620, Ensembl:ENSMUST00000024118,
            Ensembl:ENSMUSP00000024118, Ensembl:ENSMUSG00000023349,
            Ensembl:ENSMUST00000112554, Ensembl:ENSMUSP00000108173,
            GeneID:56620, KEGG:mmu:56620, UCSC:uc009dqe.2, UCSC:uc009dqf.2,
            AGR:MGI:1861231, CTD:56620, MGI:1861231,
            VEuPathDB:HostDB:ENSMUSG00000023349, eggNOG:KOG4297,
            GeneTree:ENSGT00940000162938, HOGENOM:CLU_049894_7_5_1,
            InParanoid:Q9JKF4, OMA:TYHFTYG, OrthoDB:2881452at2759,
            PhylomeDB:Q9JKF4, TreeFam:TF333341, Reactome:R-MMU-5621480,
            Reactome:R-MMU-6798695, BioGRID-ORCS:56620, PRO:PR:Q9JKF4,
            Proteomes:UP000000589, RNAct:Q9JKF4, Bgee:ENSMUSG00000023349,
            ExpressionAtlas:Q9JKF4, Genevisible:Q9JKF4, GO:0009897, GO:0005886,
            GO:0005509, GO:0030246, GO:0005537, GO:0038187, GO:0002250,
            GO:0061760, GO:0050832, GO:0001879, GO:0045087, GO:0001819,
            GO:0043123, GO:1902533, GO:0050731, GO:2000318, GO:0001878,
            GO:0002223, CDD:cd03590, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033989,
            InterPro:IPR016187, PANTHER:PTHR46784, PANTHER:PTHR46784:SF1,
            Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    Adaptive immunity; Alternative splicing; Calcium; Cell membrane;
            Disulfide bond; Glycoprotein; Immunity; Innate immunity; Lectin;
            Membrane; Metal-binding; Reference proteome; Signal-anchor;
            Transmembrane; Transmembrane helix.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Ariizumi,K., Shen,G.L., Shikano,S., Ritter,R. 3rd, Zukas,P.,
            Edelbaum,D., Morita,A. and Takashima,A.
  TITLE     Cloning of a second dendritic cell-associated C-type lectin
            (dectin-2) and its alternatively spliced isoforms
  JOURNAL   J Biol Chem 275 (16), 11957-11963 (2000)
   PUBMED   10766825
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
            SPECIFICITY.;
            STRAIN=BALB/cJ
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).;
            STRAIN=FVB/N-3; TISSUE=Mammary tumor
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Sato,K., Yang,X.L., Yudate,T., Chung,J.S., Wu,J., Luby-Phelps,K.,
            Kimberly,R.P., Underhill,D., Cruz,P.D. Jr. and Ariizumi,K.
  TITLE     Dectin-2 is a pattern recognition receptor for fungi that couples
            with the Fc receptor gamma chain to induce innate immune responses
  JOURNAL   J Biol Chem 281 (50), 38854-38866 (2006)
   PUBMED   17050534
  REMARK    FUNCTION, INTERACTION WITH FCER1G, AND MUTAGENESIS OF ARG-17.
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Robinson,M.J., Osorio,F., Rosas,M., Freitas,R.P., Schweighoffer,E.,
            Gross,O., Verbeek,J.S., Ruland,J., Tybulewicz,V., Brown,G.D.,
            Moita,L.F., Taylor,P.R. and Reis e Sousa,C.
  TITLE     Dectin-2 is a Syk-coupled pattern recognition receptor crucial for
            Th17 responses to fungal infection
  JOURNAL   J Exp Med 206 (9), 2037-2051 (2009)
   PUBMED   19703985
  REMARK    FUNCTION.
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Barrett,N.A., Maekawa,A., Rahman,O.M., Austen,K.F. and Kanaoka,Y.
  TITLE     Dectin-2 recognition of house dust mite triggers cysteinyl
            leukotriene generation by dendritic cells
  JOURNAL   J Immunol 182 (2), 1119-1128 (2009)
   PUBMED   19124755
  REMARK    FUNCTION.
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Spleen
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Saijo,S., Ikeda,S., Yamabe,K., Kakuta,S., Ishigame,H., Akitsu,A.,
            Fujikado,N., Kusaka,T., Kubo,S., Chung,S.H., Komatsu,R., Miura,N.,
            Adachi,Y., Ohno,N., Shibuya,K., Yamamoto,N., Kawakami,K.,
            Yamasaki,S., Saito,T., Akira,S. and Iwakura,Y.
  TITLE     Dectin-2 recognition of alpha-mannans and induction of Th17 cell
            differentiation is essential for host defense against Candida
            albicans
  JOURNAL   Immunity 32 (5), 681-691 (2010)
   PUBMED   20493731
  REMARK    DISRUPTION PHENOTYPE, AND FUNCTION.
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Ritter,M., Gross,O., Kays,S., Ruland,J., Nimmerjahn,F., Saijo,S.,
            Tschopp,J., Layland,L.E. and Prazeres da Costa,C.
  TITLE     Schistosoma mansoni triggers Dectin-2, which activates the Nlrp3
            inflammasome and alters adaptive immune responses
  JOURNAL   Proc Natl Acad Sci U S A 107 (47), 20459-20464 (2010)
   PUBMED   21059925
  REMARK    FUNCTION.
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Campuzano,A., Zhang,H., Ostroff,G.R., Dos Santos Dias,L.,
            Wuthrich,M., Klein,B.S., Yu,J.J., Lara,H.H., Lopez-Ribot,J.L. and
            Hung,C.Y.
  TITLE     CARD9-Associated Dectin-1 and Dectin-2 Are Required for Protective
            Immunity of a Multivalent Vaccine against Coccidioides posadasii
            Infection
  JOURNAL   J Immunol 204 (12), 3296-3306 (2020)
   PUBMED   32358020
  REMARK    FUNCTION.
COMMENT     [FUNCTION] Calcium-dependent lectin that acts as a pattern
            recognition receptor (PRR) of the innate immune system:
            specifically recognizes and binds alpha-mannans on C.albicans
            hypheas (PubMed:17050534, PubMed:19703985, PubMed:20493731).
            Binding of C.albicans alpha-mannans to this receptor complex leads
            to phosphorylation of the immunoreceptor tyrosine-based activation
            motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and
            NF-kappa-B, consequently driving maturation of antigen-presenting
            cells and shaping antigen-specific priming of T-cells toward
            effector T-helper 1 and T-helper 17 cell subtypes (PubMed:17050534,
            PubMed:19703985, PubMed:20493731, PubMed:32358020). Recognizes
            also, in a mannose-dependent manner, allergens from house dust mite
            and fungi, by promoting cysteinyl leukotriene production
            (PubMed:19124755). Recognizes soluble elements from the eggs of
            Shistosoma mansoni altering adaptive immune responses
            (PubMed:21059925). {ECO:0000269|PubMed:17050534,
            ECO:0000269|PubMed:19124755, ECO:0000269|PubMed:19703985,
            ECO:0000269|PubMed:20493731, ECO:0000269|PubMed:21059925,
            ECO:0000269|PubMed:32358020}.
            [SUBUNIT] Associated with FCER1G (PubMed:17050534). Heterodimer
            with CLEC4D; this heterodimer forms a pattern recognition receptor
            (PRR) against fungal infection (By similarity).
            {ECO:0000250|UniProtKB:Q6EIG7, ECO:0000269|PubMed:17050534}.
            [SUBCELLULAR LOCATION] Cell membrane
            {ECO:0000250|UniProtKB:Q6EIG7}; Single-pass type II membrane
            protein {ECO:0000305}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=3; Name=1; Synonyms=Alpha; IsoId=Q9JKF4-1;
            Sequence=Displayed; Name=2; Synonyms=Beta; IsoId=Q9JKF4-2;
            Sequence=VSP_012846; Name=3; Synonyms=Gamma; IsoId=Q9JKF4-3;
            Sequence=VSP_012847.
            [TISSUE SPECIFICITY] Expressed by the XS52 DC (dendritic cell) line
            (at protein level). Expressed constitutively by the epidermis, and
            skin resident DC appear to be the major source of this expression.
            Expressed in the spleen and thymus. Expression was undetectable in
            non-DC lines, including macrophage lines (J774 and Raw), T-cell
            lines (7-17, HDK-1, and D10), B-cell hybridoma (5C5), a
            keratinocyte line (Pam 212), and a fibroblast line (NS01).
            {ECO:0000269|PubMed:10766825}.
            [DOMAIN] A short stretch of the intracellular domain (AA 8-14)
            proximal to the transmembrane domain is required for association
            with Fc receptor gamma chain. {ECO:0000269|PubMed:17050534}.
            [DISRUPTION PHENOTYPE] Deficient mice are healthy, fertile, with
            normal lymphoid cells, but show reduced survival after intravenous
            Candida albicans infection (PubMed:20493731). In deficient mice
            fungal burden is higher in kidneys of mutant and in response to
            yeast antigen inflammatory cytokines and Th17 cells are reduced
            (PubMed:20493731). {ECO:0000269|PubMed:20493731}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Dectin-2;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_361'.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..209
                     /gene="Clec6a"
                     /gene_synonym="Clec4n"
                     /gene_synonym="Clecsf10"
                     /gene_synonym="Dectin2"
     Protein         1..209
                     /product="C-type lectin domain family 6 member A"
                     /note="C-type lectin superfamily member 10; Dendritic
                     cell-associated C-type lectin 2; DC-associated C-type
                     lectin 2; Dectin-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..209
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 6 member A.
                     /id=PRO_0000046636."
     Region          1..20
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Site            17
                     /site_type="mutagenized"
                     /note="R->V: Does not affect association with Fc receptor
                     gamma chain. /evidence=ECO:0000269|PubMed:17050534."
     Region          21..43
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          39..72
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:10766825. /id=VSP_012846."
     Region          44..209
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Bond            bond(64,78)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q6EIG7."
     Region          79..204
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(79,90)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          86..203
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(107,202)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(135,168,170,174,180..181,190..193)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Region          142..182
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 3).
                     /evidence=ECO:0000303|PubMed:10766825. /id=VSP_012847."
     Site            order(142,146,174..175)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(146,175)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Bond            bond(176,194)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mvqerqsqgk gvcwtlrlws aavismllls tcfiascvvt yqfimdqpsr rlyelhtyhs
       61 sltcfsegtm vsekmwgccp nhwksfgssc ylistkenfw stseqncvqm gahlvvinte
      121 aeqnfitqql neslsyflgl sdpqgngkwq widdtpfsqn vrfwhphepn lpeercvsiv
      181 ywnpskwgwn dvfcdskhns icemkkiyl
//
LOCUS       PGCB_RAT                 883 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Brevican core protein; AltName: Full=Brain-enriched
            hyaluronan-binding protein; Short=BEHAB; Flags: Precursor.
ACCESSION   P55068
VERSION     P55068.2
DBSOURCE    UniProtKB: locus PGCB_RAT, accession P55068;
            class: standard.
            extra accessions:Q62860,Q63040,Q63513
            created: Oct 1, 1996.
            sequence updated: Nov 1, 1997.
            annotation updated: Sep 13, 2023.
            xrefs: X79881.1, CAA56255.1, X86406.1, CAA60160.1, U37142.1,
            AAA87847.1, Z28366.1, CAA82215.1, A53908, S49126, NP_001028837.1,
            NP_037048.2
            xrefs (non-sequence databases): AlphaFoldDB:P55068, SMR:P55068,
            BioGRID:247431, IntAct:P55068, MINT:P55068,
            STRING:10116.ENSRNOP00000025496, GlyCosmos:P55068, GlyGen:P55068,
            iPTMnet:P55068, PhosphoSitePlus:P55068, SwissPalm:P55068,
            PaxDb:P55068, ABCD:P55068, GeneID:25393, KEGG:rno:25393,
            UCSC:RGD:2194, AGR:RGD:2194, CTD:63827, RGD:2194, eggNOG:KOG4297,
            InParanoid:P55068, OrthoDB:5402504at2759, PhylomeDB:P55068,
            Reactome:R-RNO-1474228, Reactome:R-RNO-1971475,
            Reactome:R-RNO-2022870, Reactome:R-RNO-2022923,
            Reactome:R-RNO-2024101, Reactome:R-RNO-3000178, PRO:PR:P55068,
            Proteomes:UP000002494, GO:0030424, GO:0043194, GO:0009986,
            GO:0030425, GO:0031012, GO:0005615, GO:0098982, GO:0098978,
            GO:0033268, GO:0072534, GO:0098966, GO:0098552, GO:0045202,
            GO:0097060, GO:0030246, GO:0005540, GO:0007160, GO:0007417,
            GO:0010001, GO:0042063, GO:0021766, GO:1990138, GO:0002052,
            GO:0048168, GO:0001501, GO:0060074, CDD:cd00033, CDD:cd00054,
            CDD:cd03517, CDD:cd03520, Gene3D:2.10.70.10, Gene3D:2.60.40.10,
            Gene3D:2.10.25.10, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR016187,
            InterPro:IPR000742, InterPro:IPR007110, InterPro:IPR036179,
            InterPro:IPR013783, InterPro:IPR003006, InterPro:IPR003599,
            InterPro:IPR013106, InterPro:IPR000538, InterPro:IPR035976,
            InterPro:IPR000436, PANTHER:PTHR22804, PANTHER:PTHR22804:SF59,
            Pfam:PF00008, Pfam:PF00059, Pfam:PF00084, Pfam:PF07686,
            Pfam:PF00193, PRINTS:PR01265, SMART:SM00032, SMART:SM00034,
            SMART:SM00181, SMART:SM00409, SMART:SM00406, SMART:SM00445,
            SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF48726, PROSITE:PS00615,
            PROSITE:PS50041, PROSITE:PS00022, PROSITE:PS01186, PROSITE:PS50026,
            PROSITE:PS50835, PROSITE:PS00290, PROSITE:PS01241, PROSITE:PS50963,
            PROSITE:PS50923
KEYWORDS    Alternative splicing; Direct protein sequencing; Disulfide bond;
            EGF-like domain; Extracellular matrix; Glycoprotein; GPI-anchor;
            Hyaluronic acid; Immunoglobulin domain; Lectin; Lipoprotein;
            Membrane; Phosphoprotein; Proteoglycan; Reference proteome; Repeat;
            Secreted; Signal; Sushi.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Seidenbecher,C.I., Richter,K., Rauch,U., Fassler,R., Garner,C.C.
            and Gundelfinger,E.D.
  TITLE     Brevican, a chondroitin sulfate proteoglycan of rat brain, occurs
            as secreted and cell surface glycosylphosphatidylinositol-anchored
            isoforms
  JOURNAL   J Biol Chem 270 (45), 27206-27212 (1995)
   PUBMED   7592978
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND GPI-ANCHOR AT SER-622 (ISOFORM 2).;
            STRAIN=Sprague-Dawley; TISSUE=Brain
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Yamada,H., Watanabe,K., Shimonaka,M., Yamasaki,M. and Yamaguchi,Y.
  TITLE     cDNA cloning and the identification of an aggrecanase-like cleavage
            site in rat brevican
  JOURNAL   Biochem Biophys Res Commun 216 (3), 957-963 (1995)
   PUBMED   7488217
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 396-407.;
            TISSUE=Brain
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Aspberg,A., Miura,R., Bourdoulous,S., Shimonaka,M., Heinegard,D.,
            Schachner,M., Ruoslahti,E. and Yamaguchi,Y.
  TITLE     The C-type lectin domains of lecticans, a family of aggregating
            chondroitin sulfate proteoglycans, bind tenascin-R by
            protein-protein interactions independent of carbohydrate moiety
  JOURNAL   Proc Natl Acad Sci U S A 94 (19), 10116-10121 (1997)
   PUBMED   9294172
  REMARK    INTERACTION WITH TNR.
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Jaworski,D.M., Kelly,G.M. and Hockfield,S.
  TITLE     BEHAB, a new member of the proteoglycan tandem repeat family of
            hyaluronan-binding proteins that is restricted to the brain
  JOURNAL   J Cell Biol 125 (2), 495-509 (1994)
   PUBMED   7512973
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 1-423.;
            STRAIN=Sprague-Dawley; TISSUE=Brain
            Erratum:[J Cell Biol 1997 Apr 21;137(2):521]
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Lundby,A., Secher,A., Lage,K., Nordsborg,N.B., Dmytriyev,A.,
            Lundby,C. and Olsen,J.V.
  TITLE     Quantitative maps of protein phosphorylation sites across 14
            different rat organs and tissues
  JOURNAL   Nat Commun 3, 876 (2012)
   PUBMED   22673903
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
            Publication Status: Online-Only
COMMENT     On or before Jul 18, 2007 this sequence version replaced
            gi:2143611, gi:1083609, gi:1705451.
            [FUNCTION] May play a role in the terminally differentiating and
            the adult nervous system during postnatal development. Could
            stabilize interactions between hyaluronan (HA) and brain
            proteoglycans. Isoform 2 may function as a chondroitin
            sulfate-bearing cell surface receptor.
            [SUBUNIT] Interacts with TNR. {ECO:0000269|PubMed:9294172}.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000250|UniProtKB:Q96GW7}.
            [SUBCELLULAR LOCATION] [Isoform 1]: Secreted, extracellular space,
            extracellular matrix.
            [SUBCELLULAR LOCATION] [Isoform 2]: Membrane; Lipid-anchor,
            GPI-anchor.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1; IsoId=P55068-1; Sequence=Displayed; Name=2;
            IsoId=P55068-2; Sequence=VSP_003076, VSP_003077.
            [TISSUE SPECIFICITY] Brain.
            [DEVELOPMENTAL STAGE] Isoform 1 increases from day P4 to P64.
            Isoform 2 increases after day P8.
            [PTM] O-glycosylated; contains chondroitin sulfate.
            {ECO:0000250|UniProtKB:Q96GW7}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
            [SEQUENCE CAUTION] Sequence=CAA82215.1; Type=Frameshift;
            Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..883
                     /gene="Bcan"
                     /gene_synonym="Behab"
     Protein         1..883
                     /product="Brevican core protein"
                     /note="Brain-enriched hyaluronan-binding protein; BEHAB"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          23..883
                     /region_name="Mature chain"
                     /note="Brevican core protein. /id=PRO_0000017513."
     Region          35..154
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          40..158
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:448366"
     Region          51..52
                     /region_name="Conflict"
                     /note="AL -> WV (in Ref. 4; CAA82215).
                     /evidence=ECO:0000305."
     Region          52..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Bond            bond(56,136)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          75..79
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          119..123
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          133..138
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          151..154
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          156..251
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          156..250
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            166..167
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(178,249)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(202,223)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          256..353
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          257..352
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            264..265
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(276,351)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(300,321)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          389..574
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            413
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:Q96GW7."
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903."
     Region          452..469
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          471..501
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          503
                     /region_name="Conflict"
                     /note="V -> L (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Region          518..519
                     /region_name="Conflict"
                     /note="TV -> PA (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Region          526
                     /region_name="Conflict"
                     /note="G -> R (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Region          541
                     /region_name="Conflict"
                     /note="G -> A (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Region          556
                     /region_name="Conflict"
                     /note="R -> S (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Region          573
                     /region_name="Conflict"
                     /note="E -> A (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Region          583
                     /region_name="Conflict"
                     /note="V -> L (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Region          622..658
                     /region_name="Domain"
                     /note="EGF-like.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            622
                     /site_type="lipid-binding"
                     /note="GPI-anchor amidated serine.
                     /evidence=ECO:0000305|PubMed:7592978."
     Region          625..645
                     /region_name="Splicing variant"
                     /note="DCIPSPCHNGGTCLEEKEGFR -> NSAEGSMPAFLLFLLLQLWDT (in
                     isoform 2). /evidence=ECO:0000305. /id=VSP_003076."
     Region          626..655
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Bond            bond(626,637)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(631,646)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          646..883
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2). /evidence=ECO:0000305.
                     /id=VSP_003077."
     Bond            bond(648,657)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          649
                     /region_name="Conflict"
                     /note="V -> L (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Region          658..786
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          664..787
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Region          670
                     /region_name="Conflict"
                     /note="P -> A (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Bond            bond(692,784)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          738
                     /region_name="Conflict"
                     /note="P -> A (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Site            order(758,762,764,770,772..775,778..780)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(760,776)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          789..849
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          791..848
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(791,834)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(801,821)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          809
                     /region_name="Conflict"
                     /note="R -> A (in Ref. 2; AAA87847).
                     /evidence=ECO:0000305."
     Bond            bond(820,847)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          859..883
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
        1 miplllslla alvltqapaa laddlkedss edrafrvrig aaqlrgvlgg alaipchvhh
       61 lrpppsrraa pgfprvkwtf lsgdrevevl varglrvkvn eayrfrvalp aypasltdvs
      121 lvlselrpnd sgvyrcevqh giddssdave vkvkgvvfly regsaryafs fagaqeacar
      181 igariatpeq lyaaylggye qcdagwlsdq tvrypiqnpr eacygdmdgy pgvrnygvvg
      241 pddlydvycy aedlngelfl gappgkltwe eardyclerg aqiastgqly aawnggldrc
      301 spgwladgsv rypiitpsqr cggglpgvkt lflfpnqtgf pskqnrfnvy cfrdsahpsa
      361 fseasspasd gleaivtvte kleelqlpqe avesesrgai ysipitedgg ggsstpedpa
      421 eaprtplese tqsvapptgs seeegealee eerfkdtetp keekeqenlw vwptelsspl
      481 ptgletehsl sqvsppaqav lqvgaspspr pprvhgptve tlqppgegsl tstpdgarev
      541 ggetgspels gvprereeag sssledgpsl lpetwapvgt revetpseek sgrtvltgts
      601 vqaqpvlptd sasrggvava pssgdcipsp chnggtclee kegfrclcvp gyggdlcdvg
      661 lhfcspgwep fqgacykhfs trrsweeaes qcralgahlt sictpeeqdf vndryreyqw
      721 iglndrtieg dflwsdgppl lyenwnpgqp dsyflsgenc vvmvwhdqgq wsdvpcnyhl
      781 sytckmglvs cgpppqlpla qifgrprlry avdtvlryrc rdglaqrnlp lircqenglw
      841 eapqiscvpr rparalrsmt apegprgqlp rqrkalltpp ssl
//
LOCUS       CLC4D_HUMAN              215 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 4 member D; AltName:
            Full=C-type lectin superfamily member 8; AltName: Full=C-type
            lectin-like receptor 6; Short=CLEC-6; AltName: Full=Dendritic
            cell-associated C-type lectin 3; Short=DC-associated C-type lectin
            3; Short=Dectin-3; AltName: CD_antigen=CD368.
ACCESSION   Q8WXI8
VERSION     Q8WXI8.2
DBSOURCE    UniProtKB: locus CLC4D_HUMAN, accession Q8WXI8;
            class: standard.
            extra accessions:Q8N5J5
            created: Feb 15, 2005.
            sequence updated: May 10, 2005.
            annotation updated: Sep 13, 2023.
            xrefs: AY297446.1, AAQ63173.1, AY486482.1, AAS59161.1, AY486483.1,
            AAS59162.1, AF411850.1, AAL37713.1, AY115592.1, AAM75389.1,
            BC032313.1, AAH32313.1, NP_525126.2, XP_011518934.1, 2LS8_A,
            3WHD_A, 3WHD_C
            xrefs (non-sequence databases): CCDS:CCDS8593.1, PDBsum:2LS8,
            PDBsum:3WHD, AlphaFoldDB:Q8WXI8, BMRB:Q8WXI8, SMR:Q8WXI8,
            BioGRID:130719, IntAct:Q8WXI8, STRING:9606.ENSP00000299665,
            UniLectin:Q8WXI8, GlyCosmos:Q8WXI8, GlyGen:Q8WXI8, iPTMnet:Q8WXI8,
            PhosphoSitePlus:Q8WXI8, BioMuta:CLEC4D, DMDM:73916933,
            MassIVE:Q8WXI8, PaxDb:Q8WXI8, PeptideAtlas:Q8WXI8, ABCD:Q8WXI8,
            Antibodypedia:1467, DNASU:338339, Ensembl:ENST00000299665.3,
            Ensembl:ENSP00000299665.2, Ensembl:ENSG00000166527.8,
            GeneID:338339, KEGG:hsa:338339, MANE-Select:ENST00000299665.3,
            UCSC:uc001qun.4, AGR:HGNC:14554, CTD:338339, DisGeNET:338339,
            GeneCards:CLEC4D, HGNC:14554, HPA:ENSG00000166527, MIM:609964,
            neXtProt:NX_Q8WXI8, OpenTargets:ENSG00000166527,
            PharmGKB:PA134916109, VEuPathDB:HostDB:ENSG00000166527,
            eggNOG:KOG4297, GeneTree:ENSGT00940000162400,
            HOGENOM:CLU_049894_7_5_1, InParanoid:Q8WXI8, OMA:QWIPWVI,
            OrthoDB:2881452at2759, PhylomeDB:Q8WXI8, TreeFam:TF333341,
            PathwayCommons:Q8WXI8, Reactome:R-HSA-5621480,
            Reactome:R-HSA-6798695, SignaLink:Q8WXI8, BioGRID-ORCS:338339,
            GenomeRNAi:338339, Pharos:Q8WXI8, PRO:PR:Q8WXI8,
            Proteomes:UP000005640, RNAct:Q8WXI8, Bgee:ENSG00000166527,
            ExpressionAtlas:Q8WXI8, Genevisible:Q8WXI8, GO:0009897, GO:0101003,
            GO:0005886, GO:0035579, GO:0070821, GO:0030246, GO:0034987,
            GO:0005537, GO:0046872, GO:0038187, GO:0002250, GO:0061760,
            GO:0042742, GO:0038094, GO:0043123, GO:0030887, GO:0002292,
            CDD:cd03590, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR033989, InterPro:IPR016187,
            PANTHER:PTHR46784, PANTHER:PTHR46784:SF1, Pfam:PF00059,
            SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS50041
KEYWORDS    3D-structure; Adaptive immunity; Calcium; Cell membrane; Disulfide
            bond; Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
            Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
            Transmembrane helix.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Arce,I., Martinez-Munoz,L., Roda-Navarro,P. and Fernandez-Ruiz,E.
  TITLE     The human C-type lectin CLECSF8 is a novel monocyte/macrophage
            endocytic receptor
  JOURNAL   Eur J Immunol 34 (1), 210-220 (2004)
   PUBMED   14971047
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
            INDUCTION.
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Flornes,L.M., Bryceson,Y.T., Spurkland,A., Lorentzen,J.C.,
            Dissen,E. and Fossum,S.
  TITLE     Identification of lectin-like receptors expressed by antigen
            presenting cells and neutrophils and their mapping to a novel gene
            complex
  JOURNAL   Immunogenetics 56 (7), 506-517 (2004)
   PUBMED   15368084
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            TISSUE=Macrophage
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Colonna,M.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-JUL-2001) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-32.
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Ma,J. and Liew,C.-C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-MAY-2002) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-32.;
            TISSUE=Peripheral blood
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Blood
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Miyake,Y., Toyonaga,K., Mori,D., Kakuta,S., Hoshino,Y., Oyamada,A.,
            Yamada,H., Ono,K., Suyama,M., Iwakura,Y., Yoshikai,Y. and
            Yamasaki,S.
  TITLE     C-type lectin MCL is an FcRgamma-coupled receptor that mediates the
            adjuvanticity of mycobacterial cord factor
  JOURNAL   Immunity 38 (5), 1050-1062 (2013)
   PUBMED   23602766
  REMARK    FUNCTION.
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Zhu,L.L., Zhao,X.Q., Jiang,C., You,Y., Chen,X.P., Jiang,Y.Y.,
            Jia,X.M. and Lin,X.
  TITLE     C-type lectin receptors Dectin-3 and Dectin-2 form a heterodimeric
            pattern-recognition receptor for host defense against fungal
            infection
  JOURNAL   Immunity 39 (2), 324-334 (2013)
   PUBMED   23911656
  REMARK    FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLEC6A.
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Furukawa,A., Kamishikiryo,J., Mori,D., Toyonaga,K., Okabe,Y.,
            Toji,A., Kanda,R., Miyake,Y., Ose,T., Yamasaki,S. and Maenaka,K.
  TITLE     Structural analysis for glycolipid recognition by the C-type
            lectins Mincle and MCL
  JOURNAL   Proc Natl Acad Sci U S A 110 (43), 17438-17443 (2013)
   PUBMED   24101491
  REMARK    X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 61-215 IN COMPLEX WITH
            CALCIUM, AND MUTAGENESIS OF GLU-173 AND ASP-175.
COMMENT     On Aug 30, 2005 this sequence version replaced gi:59797958.
            [FUNCTION] Calcium-dependent lectin that acts as a pattern
            recognition receptor (PRR) of the innate immune system: recognizes
            damage-associated molecular patterns (DAMPs) of pathogen-associated
            molecular patterns (PAMPs) of bacteria and fungi (PubMed:23602766,
            PubMed:23911656). The PAMPs include alpha-mannans on C.albicans
            hypheas and mycobacterial trehalose 6,6'-dimycolate (TDM)
            (PubMed:23602766, PubMed:23911656). Interacts with signaling
            adapter Fc receptor gamma chain/FCER1G, likely via CLEC4E, to form
            a functional complex in myeloid cells (By similarity). Binding of
            mycobacterial TDM or C.albicans alpha-mannans to this receptor
            complex leads to phosphorylation of the immunoreceptor
            tyrosine-based activation motif (ITAM) of FCER1G, triggering
            activation of SYK, CARD9 and NF-kappa-B, consequently driving
            maturation of antigen-presenting cells and shaping antigen-specific
            priming of T-cells toward effector T-helper 1 and T-helper 17 cell
            subtypes (PubMed:23602766, PubMed:23911656). The heterodimer formed
            with CLEC6A is active against fungal infection (PubMed:23911656).
            Functions as an endocytic receptor (PubMed:14971047). May be
            involved in antigen uptake at the site of infection, either for
            clearance of the antigen, or for processing and further
            presentation to T-cells (PubMed:14971047).
            {ECO:0000250|UniProtKB:Q69FH1, ECO:0000269|PubMed:14971047,
            ECO:0000269|PubMed:23602766, ECO:0000269|PubMed:23911656}.
            [SUBUNIT] Heterodimer with CLEC4E; disulfide-linked (By
            similarity). CLEC4E acts as a bridge for interaction between CLEC4D
            and FCER1G to form a functional complex (By similarity).
            Heterodimer with CLEC6A; this heterodimer forms a pattern
            recognition receptor (PRR) against fungal infection
            (PubMed:23911656). {ECO:0000250|UniProtKB:Q69FH1,
            ECO:0000269|PubMed:23911656}.
            [INTERACTION] Q8WXI8; P35609: ACTN2; NbExp=3; IntAct=EBI-12703404,
            EBI-77797; Q8WXI8; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-12703404,
            EBI-12109402; Q8WXI8; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-12703404,
            EBI-10266796; Q8WXI8; Q8N966: ZDHHC22; NbExp=3;
            IntAct=EBI-12703404, EBI-10268111.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000269|PubMed:23911656};
            Single-pass type II membrane protein {ECO:0000305}.
            [TISSUE SPECIFICITY] Expressed weakly in peripheral blood
            leukocytes, bone marrow and spleen. Expression is confined mostly
            in monocytes and macrophage and seems to be up-regulated by IL-6,
            IL-10, TNF-alpha and IFN-gamma. {ECO:0000269|PubMed:14971047}.
            [INDUCTION] By autocrine inflammatory stimuli.
            {ECO:0000269|PubMed:14971047}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=MCL;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_hum_Ctlect_365'.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..215
                     /gene="CLEC4D"
                     /gene_synonym="CLECSF8"
                     /gene_synonym="MCL"
     Protein         1..215
                     /product="C-type lectin domain family 4 member D"
                     /note="C-type lectin superfamily member 8; C-type
                     lectin-like receptor 6; Dendritic cell-associated C-type
                     lectin 3; CLEC-6; DC-associated C-type lectin 3; Dectin-3"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..215
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 4 member D.
                     /id=PRO_0000046616."
     Region          1..17
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          18..38
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          32
                     /region_name="Variant"
                     /note="S -> G (in dbSNP:rs4304840).
                     /evidence=ECO:0000269|Ref.3, ECO:0000269|Ref.4.
                     /id=VAR_021261."
     Region          39..215
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          63..67
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Region          81..85
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Region          84..208
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(84,95)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          88..91
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Region          91..208
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          94..103
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          105..113
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(112,207)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          114..116
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Region          118..120
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:2LS8."
     Region          125..132
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Site            order(140,173,175,180,186..187,195..198)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Region          141..147
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Site            order(147,151,176,180..181)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Region          150..152
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Site            order(151,181)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Site            173
                     /site_type="mutagenized"
                     /note="E->Q: No effect on already low affinity binding to
                     trehalose-6,6'-dimycolate.
                     /evidence=ECO:0000269|PubMed:24101491."
     Site            175
                     /site_type="mutagenized"
                     /note="D->N: No effect on already low affinity binding to
                     trehalose-6,6'-dimycolate.
                     /evidence=ECO:0000269|PubMed:24101491."
     Region          181..187
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Bond            bond(182,199)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          189..198
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Region          203..210
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
     Region          212..214
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:3WHD."
ORIGIN
        1 mglekpqskl eggmhpqlip sviavvfill lsvcfiascl vthhnfsrck rgtgvhkleh
       61 haklkcikek selksaegst wnccpidwra fqsncyfplt dnktwaeser ncsgmgahlm
      121 tisteaeqnf iiqfldrrls yflglrdena kgqwrwvdqt pfnprrvfwh knepdnsqge
      181 ncvvlvynqd kwawndvpcn feasrickip gttln
//
LOCUS       LIT2_MOUSE               173 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Lithostathine-2; AltName: Full=Islet of Langerhans
            regenerating protein 2; Short=REG-2; AltName: Full=Pancreatic stone
            protein 2; Short=PSP; AltName: Full=Pancreatic thread protein 2;
            Short=PTP; Flags: Precursor.
ACCESSION   Q08731
VERSION     Q08731.1
DBSOURCE    UniProtKB: locus LIT2_MOUSE, accession Q08731;
            class: standard.
            created: Nov 1, 1995.
            sequence updated: Nov 1, 1995.
            annotation updated: Sep 13, 2023.
            xrefs: D14011.1, BAA03112.1, B47148, NP_033069.1
            xrefs (non-sequence databases): CCDS:CCDS20256.1,
            AlphaFoldDB:Q08731, SMR:Q08731, STRING:10090.ENSMUSP00000023906,
            MEROPS:I63.002, iPTMnet:Q08731, PhosphoSitePlus:Q08731,
            PaxDb:Q08731, PeptideAtlas:Q08731, ProteomicsDB:292336,
            DNASU:19693, Ensembl:ENSMUST00000023906,
            Ensembl:ENSMUSP00000023906, Ensembl:ENSMUSG00000023140,
            GeneID:19693, KEGG:mmu:19693, UCSC:uc009cjz.1, AGR:MGI:97896,
            CTD:19693, MGI:97896, VEuPathDB:HostDB:ENSMUSG00000023140,
            eggNOG:KOG4297, GeneTree:ENSGT00940000162393,
            HOGENOM:CLU_049894_18_0_1, InParanoid:Q08731, OMA:CYYFMED,
            OrthoDB:2902508at2759, PhylomeDB:Q08731, BioGRID-ORCS:19693,
            ChiTaRS:Reg2, PRO:PR:Q08731, Proteomes:UP000000589, RNAct:Q08731,
            Bgee:ENSMUSG00000023140, ExpressionAtlas:Q08731,
            Genevisible:Q08731, GO:0062023, GO:0005615, GO:0140678, GO:0070492,
            GO:0042834, GO:0038023, GO:0061844, GO:0044278, GO:0042552,
            GO:0008284, GO:0043434, GO:0001967, Gene3D:3.10.100.10,
            InterPro:IPR001304, InterPro:IPR016186, InterPro:IPR018378,
            InterPro:IPR016187, PANTHER:PTHR22803:SF131, PANTHER:PTHR22803,
            Pfam:PF00059, PRINTS:PR01504, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Disulfide bond; Lectin; Reference proteome; Secreted; Signal.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Unno,M., Yonekura,H., Nakagawara,K., Watanabe,T., Miyashita,H.,
            Moriizumi,S., Okamoto,H., Itoh,T. and Teraoka,H.
  TITLE     Structure, chromosomal localization, and expression of mouse reg
            genes, reg I and reg II. A novel type of reg gene, reg II, exists
            in the mouse genome
  JOURNAL   J Biol Chem 268 (21), 15974-15982 (1993)
   PUBMED   8340418
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA].;
            STRAIN=C57BL/6J
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver, and Pancreas
COMMENT     On Jun 10, 2005 this sequence version replaced gi:539922.
            [FUNCTION] Might act as an inhibitor of spontaneous calcium
            carbonate precipitation.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000250}.
            [TISSUE SPECIFICITY] Expressed only in regenerating islets and
            normal exocrine pancreas, but not in normal pancreatic islets.
            Expressed strongly in pancreas, weakly in liver, but not at all in
            gall bladder.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Litho/Reg 1beta;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_183'.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..173
                     /gene="Reg2"
     Protein         1..173
                     /product="Lithostathine-2"
                     /note="Islet of Langerhans regenerating protein 2;
                     Pancreatic stone protein 2; Pancreatic thread protein 2;
                     REG-2; PSP; PTP"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000250."
     Region          23..173
                     /region_name="Mature chain"
                     /note="Lithostathine-2. /id=PRO_0000017427."
     Region          41..171
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          43..171
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(43,54)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(71,169)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(142,146,148,155,157..160,163..165)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(144,161)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 maqnnvylil flclmflsys qgqvaeedfp laekdlpsak incpeganay gsycyylied
       61 rltwgeadlf cqnmnaghlv silsqaesnf vaslvkesgt tasnvwtglh dpksnrrwhw
      121 ssgslflfks watgapstan rgycvsltsn taykkwkden ceaqysfvck fra
//
LOCUS       PGCB_HUMAN               911 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=Brevican core protein; AltName: Full=Brain-enriched
            hyaluronan-binding protein; Short=BEHAB; AltName: Full=Chondroitin
            sulfate proteoglycan 7; Flags: Precursor.
ACCESSION   Q96GW7
VERSION     Q96GW7.2
DBSOURCE    UniProtKB: locus PGCB_HUMAN, accession Q96GW7;
            class: standard.
            extra accessions:D3DVC2,Q5SZ10,Q5T3I5,Q8TBB9,Q9HBK1,Q9HBK4
            created: Aug 16, 2004.
            sequence updated: Jun 21, 2005.
            annotation updated: Sep 13, 2023.
            xrefs: AF228710.1, AAG23134.1, AF229053.1, AAG23135.1, AY358372.1,
            AAQ88738.1, AL365181.24, AL590666.8, CH471121.2, EAW52927.1,
            EAW52928.1, EAW52929.1, EAW52930.1, BC009117.1, AAH09117.1,
            BC022938.1, AAH22938.1, BC027971.1, AAH27971.1, NP_068767.3,
            NP_940819.1, XP_011508168.1
            xrefs (non-sequence databases): CCDS:CCDS1149.1, CCDS:CCDS1150.1,
            AlphaFoldDB:Q96GW7, SMR:Q96GW7, BioGRID:121964, IntAct:Q96GW7,
            STRING:9606.ENSP00000331210, GlyCosmos:Q96GW7, GlyGen:Q96GW7,
            iPTMnet:Q96GW7, PhosphoSitePlus:Q96GW7, BioMuta:BCAN,
            DMDM:68067899, jPOST:Q96GW7, MassIVE:Q96GW7, PaxDb:Q96GW7,
            PeptideAtlas:Q96GW7, ProteomicsDB:76671, ProteomicsDB:76672,
            TopDownProteomics:Q96GW7-2, ABCD:Q96GW7, Antibodypedia:2188,
            DNASU:63827, Ensembl:ENST00000329117.10, Ensembl:ENSP00000331210.4,
            Ensembl:ENSG00000132692.19, Ensembl:ENST00000361588.5,
            Ensembl:ENSP00000354925.5, GeneID:63827, KEGG:hsa:63827,
            MANE-Select:ENST00000329117.10, UCSC:uc001fpo.4, AGR:HGNC:23059,
            CTD:63827, DisGeNET:63827, GeneCards:BCAN, HGNC:23059,
            HPA:ENSG00000132692, MIM:600347, neXtProt:NX_Q96GW7,
            OpenTargets:ENSG00000132692, PharmGKB:PA134868393,
            VEuPathDB:HostDB:ENSG00000132692, eggNOG:KOG4297,
            GeneTree:ENSGT00940000157343, HOGENOM:CLU_000303_0_0_1,
            InParanoid:Q96GW7, OMA:APQISCV, OrthoDB:5402504at2759,
            PhylomeDB:Q96GW7, TreeFam:TF332134, PathwayCommons:Q96GW7,
            Reactome:R-HSA-1474228, Reactome:R-HSA-1971475,
            Reactome:R-HSA-2022870, Reactome:R-HSA-2022923,
            Reactome:R-HSA-2024101, Reactome:R-HSA-3000178,
            Reactome:R-HSA-3560783, Reactome:R-HSA-3560801,
            Reactome:R-HSA-3595172, Reactome:R-HSA-3595174,
            Reactome:R-HSA-3595177, Reactome:R-HSA-4420332, SignaLink:Q96GW7,
            BioGRID-ORCS:63827, ChiTaRS:BCAN, GeneWiki:Brevican,
            GenomeRNAi:63827, Pharos:Q96GW7, PRO:PR:Q96GW7,
            Proteomes:UP000005640, RNAct:Q96GW7, Bgee:ENSG00000132692,
            ExpressionAtlas:Q96GW7, Genevisible:Q96GW7, GO:0005576, GO:0005615,
            GO:0098978, GO:0005796, GO:0043202, GO:0072534, GO:0098552,
            GO:0045202, GO:0030246, GO:0005540, GO:0007155, GO:0007417,
            GO:0010001, GO:0021766, GO:0002052, GO:0001501, GO:0060074,
            CDD:cd00033, CDD:cd00054, CDD:cd03517, CDD:cd03520,
            Gene3D:2.10.70.10, Gene3D:2.60.40.10, Gene3D:2.10.25.10,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR016187, InterPro:IPR000742,
            InterPro:IPR007110, InterPro:IPR036179, InterPro:IPR013783,
            InterPro:IPR003006, InterPro:IPR003599, InterPro:IPR013106,
            InterPro:IPR000538, InterPro:IPR035976, InterPro:IPR000436,
            PANTHER:PTHR22804, Pfam:PF00008, Pfam:PF00059, Pfam:PF00084,
            Pfam:PF07686, Pfam:PF00193, PRINTS:PR01265, SMART:SM00032,
            SMART:SM00034, SMART:SM00181, SMART:SM00409, SMART:SM00406,
            SMART:SM00445, SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF48726,
            PROSITE:PS00615, PROSITE:PS50041, PROSITE:PS00022, PROSITE:PS01186,
            PROSITE:PS50026, PROSITE:PS50835, PROSITE:PS00290, PROSITE:PS01241,
            PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Alternative splicing; Disulfide bond; EGF-like domain;
            Extracellular matrix; Glycoprotein; GPI-anchor; Hyaluronic acid;
            Immunoglobulin domain; Lectin; Lipoprotein; Membrane;
            Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted;
            Signal; Sushi.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Gary,S.C., Zerillo,C.A., Chiang,V.L., Gaw,J.U., Gray,G. and
            Hockfield,S.
  TITLE     cDNA cloning, chromosomal localization, and expression analysis of
            human BEHAB/brevican, a brain specific proteoglycan regulated
            during cortical development and in glioma
  JOURNAL   Gene 256 (1-2), 139-147 (2000)
   PUBMED   11054543
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DEVELOPMENTAL
            STAGE.;
            TISSUE=Brain cortex
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
            LYS-504.
            Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Gregory,S.G., Barlow,K.F., McLay,K.E., Kaul,R., Swarbreck,D.,
            Dunham,A., Scott,C.E., Howe,K.L., Woodfine,K., Spencer,C.C.,
            Jones,M.C., Gillson,C., Searle,S., Zhou,Y., Kokocinski,F.,
            McDonald,L., Evans,R., Phillips,K., Atkinson,A., Cooper,R.,
            Jones,C., Hall,R.E., Andrews,T.D., Lloyd,C., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Anderson,F., Andrew,R.W., Ashwell,R.I.,
            Aubin,K., Babbage,A.K., Bagguley,C.L., Bailey,J., Beasley,H.,
            Bethel,G., Bird,C.P., Bray-Allen,S., Brown,J.Y., Brown,A.J.,
            Buckley,D., Burton,J., Bye,J., Carder,C., Chapman,J.C., Clark,S.Y.,
            Clarke,G., Clee,C., Cobley,V., Collier,R.E., Corby,N.,
            Coville,G.J., Davies,J., Deadman,R., Dunn,M., Earthrowl,M.,
            Ellington,A.G., Errington,H., Frankish,A., Frankland,J., French,L.,
            Garner,P., Garnett,J., Gay,L., Ghori,M.R., Gibson,R., Gilby,L.M.,
            Gillett,W., Glithero,R.J., Grafham,D.V., Griffiths,C.,
            Griffiths-Jones,S., Grocock,R., Hammond,S., Harrison,E.S., Hart,E.,
            Haugen,E., Heath,P.D., Holmes,S., Holt,K., Howden,P.J., Hunt,A.R.,
            Hunt,S.E., Hunter,G., Isherwood,J., James,R., Johnson,C.,
            Johnson,D., Joy,A., Kay,M., Kershaw,J.K., Kibukawa,M.,
            Kimberley,A.M., King,A., Knights,A.J., Lad,H., Laird,G., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Loveland,J., Lovell,J., Lush,M.J.,
            Lyne,R., Martin,S., Mashreghi-Mohammadi,M., Matthews,L.,
            Matthews,N.S., McLaren,S., Milne,S., Mistry,S., Moore,M.J.,
            Nickerson,T., O'Dell,C.N., Oliver,K., Palmeiri,A., Palmer,S.A.,
            Parker,A., Patel,D., Pearce,A.V., Peck,A.I., Pelan,S., Phelps,K.,
            Phillimore,B.J., Plumb,R., Rajan,J., Raymond,C., Rouse,G.,
            Saenphimmachak,C., Sehra,H.K., Sheridan,E., Shownkeen,R., Sims,S.,
            Skuce,C.D., Smith,M., Steward,C., Subramanian,S., Sycamore,N.,
            Tracey,A., Tromans,A., Van Helmond,Z., Wall,M., Wallis,J.M.,
            White,S., Whitehead,S.L., Wilkinson,J.E., Willey,D.L., Williams,H.,
            Wilming,L., Wray,P.W., Wu,Z., Coulson,A., Vaudin,M., Sulston,J.E.,
            Durbin,R., Hubbard,T., Wooster,R., Dunham,I., Carter,N.P.,
            McVean,G., Ross,M.T., Harrow,J., Olson,M.V., Beck,S., Rogers,J.,
            Bentley,D.R., Banerjee,R., Bryant,S.P., Burford,D.C., Burrill,W.D.,
            Clegg,S.M., Dhami,P., Dovey,O., Faulkner,L.M., Gribble,S.M.,
            Langford,C.F., Pandian,R.D., Porter,K.M. and Prigmore,E.
  TITLE     The DNA sequence and biological annotation of human chromosome 1
  JOURNAL   Nature 441 (7091), 315-321 (2006)
   PUBMED   16710414
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
            Erratum:[Nature. 2006 Oct 26;443(7114):1013. Banerjee, R [added];
            Bryant, SP [added]; Burford, DC [added]; Burrill, WDH [added];
            Clegg, SM [added]; Dhami, P [added]; Dovey, O [added]; Faulkner, LM
            [added]; Gribble, SM [added]; Langford, CF [added]; Pandian, RD
            [added]; Porter, KM [added]; Prigmore, E]
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Mural,R.J., Istrail,S., Sutton,G.G., Florea,L., Halpern,A.L.,
            Mobarry,C.M., Lippert,R., Walenz,B., Shatkay,H., Dew,I.,
            Miller,J.R., Flanigan,M.J., Edwards,N.J., Bolanos,R., Fasulo,D.,
            Halldorsson,B.V., Hannenhalli,S., Turner,R., Yooseph,S., Lu,F.,
            Nusskern,D.R., Shue,B.C., Zheng,X.H., Zhong,F., Delcher,A.L.,
            Huson,D.H., Kravitz,S.A., Mouchard,L., Reinert,K., Remington,K.A.,
            Clark,A.G., Waterman,M.S., Eichler,E.E., Adams,M.D.,
            Hunkapiller,M.W., Myers,E.W. and Venter,J.C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-SEP-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).;
            TISSUE=Brain
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Nilsson,J., Ruetschi,U., Halim,A., Hesse,C., Carlsohn,E.,
            Brinkmalm,G. and Larson,G.
  TITLE     Enrichment of glycopeptides for glycan structure and attachment
            site identification
  JOURNAL   Nat Methods 6 (11), 809-811 (2009)
   PUBMED   19838169
  REMARK    GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-906, AND
            STRUCTURE OF CARBOHYDRATES.;
            TISSUE=Cerebrospinal fluid
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Noborn,F., Gomez Toledo,A., Sihlbom,C., Lengqvist,J., Fries,E.,
            Kjellen,L., Nilsson,J. and Larson,G.
  TITLE     Identification of chondroitin sulfate linkage region glycopeptides
            reveals prohormones as a novel class of proteoglycans
  JOURNAL   Mol Cell Proteomics 14 (1), 41-49 (2015)
   PUBMED   25326458
  REMARK    SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT
            SER-418.
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Felemban,M., Dorgau,B., Hunt,N.C., Hallam,D., Zerti,D., Bauer,R.,
            Ding,Y., Collin,J., Steel,D., Krasnogor,N., Al-Aama,J., Lindsay,S.,
            Mellough,C. and Lako,M.
  TITLE     Extracellular matrix component expression in human pluripotent stem
            cell-derived retinal organoids recapitulates retinogenesis in vivo
            and reveals an important role for IMPG1 and CD44 in the development
            of photoreceptors and interphotoreceptor matrix
  JOURNAL   Acta Biomater 74, 207-221 (2018)
   PUBMED   29777959
  REMARK    TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
COMMENT     On or before Feb 9, 2010 this sequence version replaced
            gi:74756169, gi:74744772, gi:51316515.
            [FUNCTION] May play a role in the terminally differentiating and
            the adult nervous system during postnatal development. Could
            stabilize interactions between hyaluronan (HA) and brain
            proteoglycans.
            [SUBUNIT] Interacts with TNR. {ECO:0000250}.
            [INTERACTION] Q96GW7; Q06481-5: APLP2; NbExp=3; IntAct=EBI-2690445,
            EBI-25646567; Q96GW7; P05067: APP; NbExp=3; IntAct=EBI-2690445,
            EBI-77613; Q96GW7; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-2690445,
            EBI-9087876; Q96GW7; P07948: LYN; NbExp=3; IntAct=EBI-2690445,
            EBI-79452.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000269|PubMed:25326458}.
            [SUBCELLULAR LOCATION] [Isoform 1]: Secreted, extracellular space,
            extracellular matrix.
            [SUBCELLULAR LOCATION] [Isoform 2]: Membrane; Lipid-anchor,
            GPI-anchor.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1; IsoId=Q96GW7-1; Sequence=Displayed; Name=2;
            IsoId=Q96GW7-2; Sequence=VSP_011184, VSP_011185.
            [TISSUE SPECIFICITY] Expressed in the retina, specifically in the
            inner nuclear layer, inner plexiform layer and ganglion cell layer
            (at protein level) (PubMed:29777959). Detected in cerebrospinal
            fluid (at protein level) (PubMed:25326458).
            {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:29777959}.
            [DEVELOPMENTAL STAGE] Expressed between 6 and 19 weeks
            post-conception (WPC) in the outer neuroblastic zone, inner
            neuroblastic zone, and inner plexiform layer of the retina (at
            protein level) (PubMed:29777959). Expressed at the surface ectoderm
            at 6 WPC and the neural retinal at 6 to 8 WPC (at protein level)
            (PubMed:29777959). Expressed in the interphotoreceptor matrix and
            abundantly in developing photoreceptors between 12 and 19 WPC (at
            protein level) (PubMed:29777959). Isoform 1: Highly expressed from
            birth through 8 years of age and is down-regulated by 20 years of
            age to low levels that are maintained in the normal adult cortex
            (PubMed:11054543). Isoform 2: Expressed at uniformly low levels
            throughout development (PubMed:11054543).
            {ECO:0000269|PubMed:11054543, ECO:0000269|PubMed:29777959}.
            [PTM] O-glycosylated; contains chondroitin sulfate
            (PubMed:25326458). O-glycosylated with a core 1 or possibly core 8
            glycan (PubMed:19838169). {ECO:0000269|PubMed:19838169,
            ECO:0000269|PubMed:25326458}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Brevican;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_hum_Ctlect_212'.
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..911
                     /gene="BCAN"
                     /locus_tag="UNQ2525/PRO6018"
                     /gene_synonym="BEHAB"
                     /gene_synonym="CSPG7"
     Protein         1..911
                     /product="Brevican core protein"
                     /note="Brain-enriched hyaluronan-binding protein;
                     Chondroitin sulfate proteoglycan 7; BEHAB"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          23..911
                     /region_name="Mature chain"
                     /note="Brevican core protein. /id=PRO_0000017511."
     Region          36..155
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          39..159
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:448366"
     Region          53..57
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Bond            bond(57,137)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          76..80
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..124
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          134..139
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..155
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          157..252
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          157..251
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            167..168
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Region          175
                     /region_name="Conflict"
                     /note="A -> T (in Ref. 5; AAH22938).
                     /evidence=ECO:0000305."
     Bond            bond(179,250)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(203,224)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          257..354
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          258..353
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            265..266
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(277,352)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(301,322)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          356
                     /region_name="Variant"
                     /note="S -> L (in dbSNP:rs12065791). /id=VAR_050123."
     Region          391..641
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            418
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:25326458."
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55068."
     Region          453..479
                     /region_name="Compositionally biased region"
                     /note="Acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          <499..654
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          504
                     /region_name="Variant"
                     /note="E -> K (in dbSNP:rs1056695).
                     /evidence=ECO:0000269|PubMed:12975309. /id=VAR_019551."
     Region          520..530
                     /region_name="Region of interest in the sequence"
                     /note="O-glycosylated at two sites."
     Region          540..545
                     /region_name="Region of interest in the sequence"
                     /note="O-glycosylated at two sites."
     Region          569..575
                     /region_name="Region of interest in the sequence"
                     /note="O-glycosylated at one site."
     Region          616..633
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          646..682
                     /region_name="Domain"
                     /note="EGF-like.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            646
                     /site_type="lipid-binding"
                     /note="GPI-anchor amidated alanine.
                     /evidence=ECO:0000255."
     Region          649..671
                     /region_name="Splicing variant"
                     /note="DCVPSPCHNGGTCLEEEEGVRCL -> NSAQGSTALSILLLFFPLQLWVT
                     (in isoform 2). /evidence=ECO:0000303|PubMed:11054543.
                     /id=VSP_011184."
     Region          650..679
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Bond            bond(650,661)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(655,670)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          672..911
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:11054543. /id=VSP_011185."
     Bond            bond(672,681)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          688..811
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(688,699)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          695..809
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(716,808)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(782,786,788,794,796..799,802..804)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(784,800)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          813..873
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          815..872
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(815,858)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(825,845)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(844,871)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            905
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000305|PubMed:19838169."
     Site            906
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000305|PubMed:19838169."
ORIGIN
        1 maqlflplla alvlaqapaa ladvlegdss edrafrvria gdaplqgvlg galtipchvh
       61 ylrpppsrra vlgsprvkwt flsrgreaev lvargvrvkv neayrfrval paypasltdv
      121 slalselrpn dsgiyrcevq hgiddssdav evkvkgvvfl yregsaryaf sfsgaqeaca
      181 rigahiatpe qlyaaylggy eqcdagwlsd qtvrypiqtp reacygdmdg fpgvrnygvv
      241 dpddlydvyc yaedlngelf lgdppekltl eearaycqer gaeiattgql yaawdggldh
      301 cspgwladgs vrypivtpsq rcggglpgvk tlflfpnqtg fpnkhsrfnv ycfrdsaqps
      361 aipeasnpas npasdgleai vtvtetleel qlpqeatese srgaiysipi medggggsst
      421 pedpaeaprt llefetqsmv pptgfseeeg kaleeeekye deeekeeeee eeevedealw
      481 awpselsspg peaslptepa aqeeslsqap aravlqpgas plpdgeseas rpprvhgppt
      541 etlptprern laspspstlv earevgeatg gpelsgvprg eseetgsseg apsllpatra
      601 pegtreleap sednsgrtap agtsvqaqpv lptdsasrgg vavvpasgdc vpspchnggt
      661 cleeeegvrc lclpgyggdl cdvglrfcnp gwdafqgacy khfstrrswe eaetqcrmyg
      721 ahlasistpe eqdfinnryr eyqwiglndr tiegdflwsd gvpllyenwn pgqpdsyfls
      781 gencvvmvwh dqgqwsdvpc nyhlsytckm glvscgpppe lplaqvfgrp rlryevdtvl
      841 ryrcreglaq rnlplircqe ngrweapqis cvprrparal hpeedpegrq grllgrwkal
      901 lippsspmpg p
//
LOCUS       CSPG2_CHICK             3562 aa            linear   VRT 13-SEP-2023
DEFINITION  RecName: Full=Versican core protein; AltName: Full=Chondroitin
            sulfate proteoglycan core protein 2; Short=Chondroitin sulfate
            proteoglycan 2; AltName: Full=Large fibroblast proteoglycan;
            AltName: Full=PG-M; Flags: Precursor.
ACCESSION   Q90953
VERSION     Q90953.1
DBSOURCE    UniProtKB: locus CSPG2_CHICK, accession Q90953;
            class: standard.
            extra accessions:Q90945
            created: Nov 1, 1997.
            sequence updated: Nov 1, 1997.
            annotation updated: Sep 13, 2023.
            xrefs: X60226.1, CAA42787.1, D13542.1, BAA02742.1, A47171,
            NP_990118.1
            xrefs (non-sequence databases): SMR:Q90953,
            STRING:9031.ENSGALP00000025144, GlyCosmos:Q90953, PaxDb:Q90953,
            GeneID:395565, KEGG:gga:395565, CTD:1462,
            VEuPathDB:HostDB:geneid_395565, eggNOG:ENOG502QRBE,
            InParanoid:Q90953, PhylomeDB:Q90953, PRO:PR:Q90953,
            Proteomes:UP000000539, GO:0005615, GO:0033165, GO:0072534,
            GO:0001750, GO:0045202, GO:0005509, GO:0030246, GO:0005540,
            GO:0007155, GO:0007417, GO:0010001, GO:0002052, GO:0001501,
            CDD:cd00033, CDD:cd03588, CDD:cd00054, CDD:cd03517, CDD:cd03520,
            Gene3D:2.10.70.10, Gene3D:2.60.40.10, Gene3D:2.10.25.10,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033987, InterPro:IPR016187,
            InterPro:IPR001881, InterPro:IPR000742, InterPro:IPR000152,
            InterPro:IPR018097, InterPro:IPR007110, InterPro:IPR036179,
            InterPro:IPR013783, InterPro:IPR003599, InterPro:IPR013106,
            InterPro:IPR000538, InterPro:IPR035976, InterPro:IPR000436,
            PANTHER:PTHR22804, PANTHER:PTHR22804:SF6, Pfam:PF00008,
            Pfam:PF00059, Pfam:PF00084, Pfam:PF07686, Pfam:PF00193,
            PRINTS:PR01265, SMART:SM00032, SMART:SM00034, SMART:SM00181,
            SMART:SM00179, SMART:SM00409, SMART:SM00406, SMART:SM00445,
            SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF57196, SUPFAM:SSF48726,
            PROSITE:PS00010, PROSITE:PS00615, PROSITE:PS50041, PROSITE:PS00022,
            PROSITE:PS01186, PROSITE:PS50026, PROSITE:PS01187, PROSITE:PS50835,
            PROSITE:PS01241, PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Alternative splicing; Calcium; Cell projection; Disulfide bond;
            EGF-like domain; Extracellular matrix; Glycoprotein; Hyaluronic
            acid; Immunoglobulin domain; Lectin; Proteoglycan; Reference
            proteome; Repeat; Secreted; Signal; Sushi.
SOURCE      Gallus gallus (chicken)
  ORGANISM  Gallus gallus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
            Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
            Phasianidae; Phasianinae; Gallus.
REFERENCE   1  (residues 1 to 3562)
  AUTHORS   Shinomura,T., Nishida,Y., Ito,K. and Kimata,K.
  TITLE     cDNA cloning of PG-M, a large chondroitin sulfate proteoglycan
            expressed during chondrogenesis in chick limb buds. Alternative
            spliced multiforms of PG-M and their relationships to versican
  JOURNAL   J Biol Chem 268 (19), 14461-14469 (1993)
   PUBMED   8314802
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0 AND V1).;
            STRAIN=White leghorn; TISSUE=Limb bud
COMMENT     On Oct 25, 2005 this sequence version replaced gi:422696.
            [FUNCTION] May play a role in intercellular signaling and in
            connecting cells with the extracellular matrix. May take part in
            the regulation of cell motility, growth and differentiation. Binds
            hyaluronic acid.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000250|UniProtKB:P13611}. Cell projection, cilium,
            photoreceptor outer segment {ECO:0000250|UniProtKB:P13611}.
            Secreted, extracellular space, extracellular matrix,
            interphotoreceptor matrix {ECO:0000250|UniProtKB:P13611}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Comment=Additional isoforms seem to exist.; Name=V0;
            IsoId=Q90953-1; Sequence=Displayed; Name=V1; IsoId=Q90953-2;
            Sequence=VSP_003093.
            [TISSUE SPECIFICITY] Prechondrogenic condensation area of
            developing limb buds.
            [DEVELOPMENTAL STAGE] Disappears after the cartilage development.
FEATURES             Location/Qualifiers
     source          1..3562
                     /organism="Gallus gallus"
                     /db_xref="taxon:9031"
     gene            1..3562
                     /gene="VCAN"
                     /gene_synonym="CSPG2"
     Protein         1..3562
                     /product="Versican core protein"
                     /note="Chondroitin sulfate proteoglycan core protein 2;
                     Large fibroblast proteoglycan; PG-M; Chondroitin sulfate
                     proteoglycan 2"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..26
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          27..3562
                     /region_name="Mature chain"
                     /note="Versican core protein. /id=PRO_0000017525."
     Region          27..151
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:448366"
     Region          27..143
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          40..44
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Bond            bond(44,129)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          62..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          112..116
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          126..131
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          144..147
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          149..244
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          149..243
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            159..160
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(171,242)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(195,216)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          250..346
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          250..345
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            257..258
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(269,344)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(293,314)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            329
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          466..490
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          475..489
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          485..1411
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V1).
                     /evidence=ECO:0000303|PubMed:8314802. /id=VSP_003093."
     Region          509..530
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            529
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            709
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            723
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            948
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          951..1020
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          968..1000
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1167..1187
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1167..1181
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1207..1237
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1409
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1479
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1523
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1530
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1625
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1628
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            1751
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1856..1875
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1988
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2030..2063
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2030..2046
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2082
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            2088
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2089
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2386
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          2463..2482
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2496..2522
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2642
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2679
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2748
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2762
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2918..2947
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2984..3006
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            3069
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          3108..3144
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          3111..3131
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            3194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            3232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          3254..3290
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          3256..3290
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Bond            bond(3258,3269)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3263,3278)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3280,3289)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3292..3328
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          3292..3328
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(3292,3295,3309)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(3296,3307)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3301,3316)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3318,3327)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3334..3457
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Bond            bond(3334,3345)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3341..3455
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(3352,3384..3387,3416,3426,3434,3436,3442,3445,
                     3447..3449)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Bond            bond(3362,3454)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(3395,3399,3422,3428..3429)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3399,3429)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3419,3421,3428,3442..3443)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Bond            bond(3430,3446)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3459..3519
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          3461..3517
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(3461,3504)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(3471,3491)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(3490,3517)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            3545
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
ORIGIN
        1 mllniksiiw mcstlaitym lpkvkaekkt lvkgslsgts vlpcffsttp tiassyaaey
       61 lrikwskvel dksgkdaket tvlvaqngni kigqnykdrv svpthseetg dasltfsrlr
      121 asdagvyrcd vmygvedtqg ivslavdgvv fhyraatsry tlnftqaqqt cldngavias
      181 peqlkaayed gfeqcdagwl sdqtvrypir hprigcfgdk mgkkgvrtyg rrfpnetydv
      241 ycyvehmqde vvhvsvpekl tfeeakelcr krdgvlasvg nmyvawrngf dqcdygwlad
      301 gsvrypasva rpqcgggllg vrtlyryenq tgfpypdskf daycyerkki vsepttvklv
      361 ttlktdsvel ssakvtlkps vfessvteva vtktkvpawe eatletedtk mttevaeekr
      421 emevlmenik lttllpqtvt dgeispydtl grteydvspr ltestsaale vehtyseael
      481 seeqgrsest edafltsvvf qdstavakss tgswedietg dtqkhdgdnq teqievgpvm
      541 tatdslvpas qrelprtgss vsltkenlyl gshstkeptk ksmeaksdkk lttvvipkal
      601 ftdqydlttg gegresmytv mpdrvsgval vsipesdvpa vsetlmdela vttgqsstad
      661 estpfikfss sateldneas aegsredlkd vhlttssgip vsftlftane tgsevtalse
      721 stsapqkfee gitsvlhssq qtegsailek qektkepems tidakvlyit tvvpasvtag
      781 segrfgsekf thtppvsgmw lqtdkdqvym teetshtkri eldteddisg meptsspgqi
      841 ieytkhlgap vsavtdetkt smetaetesd eevvsadfdq tkgttevfht sssldlekft
      901 lskipedess atvksfssss gtvlptavat vlevtdhead etsgyvlnmt fstpegeqrk
      961 atekspatsa edevstgtei skytmteggq issvtsaeke svaalqeree qpsvglpetk
     1021 epfkftdvte iettvpqreg dtslvpvtvg sedigemqvt dhtsfdsiih teatvtstka
     1081 sevfpkelst kdqdrelgta mgstlpvtsv qmheqkttag fespqtttqe khdemgsayd
     1141 emypatelsv palmlteygq vsgpvetstr slhltgtpka etatdqeeki teavpvtfgt
     1201 qakvyeskgt ttreedrdvg swnsvlppht mlsspstags islltlgasp sqtpegsgis
     1261 eeleevktvp fssratdktt visdlttssi savdkiqpts askpfvssks priipeedee
     1321 vtssdiivid esispskasa eddltgkmve peidkeyfts statavarpt apptvmeate
     1381 alqpqevspt shpdsgtdir lyviqitgnd tdhpvnefld lfsrhilpha vdethtdaes
     1441 aqtepctsds vqdsseyiil dpffpnfmdf eeeeedcent tdvttppalq fingkqqvts
     1501 apkstkaeea rsdqiesvah sknvtfsqin etntfiiset easgtmqpsk agevmgafev
     1561 tqptadvaml epvysgesev tttdkyleit svyeqspkkn ketvmwhgte esstkdtknl
     1621 llitnessgd gstesdlsrs vfteiltmss hedsekisht tsvptilsve rsavtaapsa
     1681 dsdtatvgid vkdlipkggt atpgnyykst ikldaefpfe snpeatshtt kpdmtassfi
     1741 vlegsgdvee nstlasamtt etavaetlsv qdtslgsgtv lpteisvtis eitpalpggt
     1801 rilystfdqs seatvstnfv selimeqvvg ssvatekkve dekevqttvy ssqeisttda
     1861 kgkseldefg sttnevrtvs qeptplreiv pitgtmhsei kkvtatpflr eklfinegsa
     1921 eepadlfags ptrkvvstds pftdsgsgdi dvitesatlt svpsrsviet qtvkhegnin
     1981 visvslkntt teyeehigtg gpvtsvsstg sdglteesev aiemsenvfs tenqgeptqe
     2041 avptytapsd iksrlgsrre vtshvtpvir tkdletaevt sspesvvnns tldtmvthgt
     2101 iravaestes kkgkgsfsav slgkilmieh gsgeelkvds sttklmsngp tekllgshfs
     2161 ffdqgsgeae tltesftkas vsptgkpepq eqygrktvsm psavvhayta epnelvtste
     2221 hditslqtvt dtemeekaan eltvtsfatn lplsedvhsw edrpreilpk aiessgeate
     2281 dpffistqan hehveflsvp tirphseenk veaesdekil lpfnndrvte savierkyls
     2341 spftdteqee elvqnifpte diprlfltpk eekptnneli sdplfsgqgs gdeftvipsv
     2401 eslavkettn tlspwpfhpa svgpklstdk tqvfesgstd snaeineeit ttaaelteta
     2461 ysmatsspal eeessshsns kdkdithyfl viedpynkem dhrrgengts rplptpgdvs
     2521 leesshmltt ddvtpvsvil setpylemgk slatsatkmp srvlpessge gsgwdgvsds
     2581 fapdtlthst apsvmevelt asshipgvys evmtthvpgd gsqtvitgla slfteekeiv
     2641 anrtaadpkt gtseeltsdt gmsldiipvv ddrrhvtlnv svygditlie erlqipsekt
     2701 tiidmdhsks mpediisvqt mpnlvirstq vsddnmkaee dkydsilnfs tveensfgsg
     2761 dnlslttsiq pssesvtagh gpklvdkdlg sgyamqfate tltttvlnel giflptvpsl
     2821 vsphmphesk esefeakhig rtsttddvye pytsannqvi tdqsktmsis gfsgmgqees
     2881 gdkkpmipsl tpdltmetek alttdtfdvs mvttqsmsqh atvsssssee khstvymqtk
     2941 sasteyeetd svslnsvsqn pkssvtvwlv ngvskypevi ipstssakds dqsdhssdgt
     3001 fkevssdmaa tykppttdld ttvssllvfs pepesesist estphfnkfv terseetess
     3061 vndliieena tvsgdspsih dyptafwnfg ertstdvpkl stievefsse rvknpsqesd
     3121 rstererprl ssapvsdspn sievgvfkpd qeavtmltss lepldrslet qsallgpllg
     3181 qqeittissn iatnntapgn npysneqsti ssellntiel vtssfslpev tngsdfligt
     3241 svgsvegtav qipgqdpcks npclnggtcy prgsfyictc lpgfngeqce ldidecqsnp
     3301 crngatcidg lntftclclp syigalceqd tetcdygwhk fqgqcykyfa hrrtwdtaer
     3361 ecrlqgahlt silsheeqvf vnrighdyqw iglndkmfer dfrwtdgspl qyenwrpnqp
     3421 dsffsagedc vviiwhengq wndvpcnyhl tytckkgtva cgqppvvena ktfgkmkpry
     3481 einsliryhc kdgfiqrhip tircqgngrw dmpkitcmnp styqrtyskk yyykhsssgk
     3541 gtslnsskhy hrwirtwqds rr
//
LOCUS       CL17A_HUMAN              378 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 17, member A; AltName:
            Full=Prolectin.
ACCESSION   Q6ZS10
VERSION     Q6ZS10.2
DBSOURCE    UniProtKB: locus CL17A_HUMAN, accession Q6ZS10;
            class: standard.
            extra accessions:A8MX68,B2RTX0,B7ZMM4
            created: Feb 26, 2008.
            sequence updated: Jul 13, 2010.
            annotation updated: Sep 13, 2023.
            xrefs: AK127809.1, BAC87146.1, AC010527.5, AC140008.2, CH471106.1,
            EAW84437.1, BC140848.1, AAI40849.1, BC144665.1, AAI44666.1,
            NP_001191047.1, NP_997273.3
            xrefs (non-sequence databases): CCDS:CCDS46002.2, CCDS:CCDS56087.1,
            AlphaFoldDB:Q6ZS10, SMR:Q6ZS10, BioGRID:132718, IntAct:Q6ZS10,
            STRING:9606.ENSP00000393719, GlyCosmos:Q6ZS10, GlyGen:Q6ZS10,
            iPTMnet:Q6ZS10, PhosphoSitePlus:Q6ZS10, BioMuta:CLEC17A,
            DMDM:300669632, MassIVE:Q6ZS10, PaxDb:Q6ZS10, PeptideAtlas:Q6ZS10,
            ProteomicsDB:68178, ProteomicsDB:68179, ProteomicsDB:68180,
            Antibodypedia:50548, DNASU:388512, Ensembl:ENST00000339847.9,
            Ensembl:ENSP00000341620.5, Ensembl:ENSG00000187912.12,
            Ensembl:ENST00000417570.6, Ensembl:ENSP00000393719.2,
            Ensembl:ENST00000547437.5, Ensembl:ENSP00000450065.1,
            GeneID:388512, KEGG:hsa:388512, MANE-Select:ENST00000417570.6,
            UCSC:uc010dzn.3, AGR:HGNC:34520, CTD:388512, DisGeNET:388512,
            GeneCards:CLEC17A, HGNC:34520, HPA:ENSG00000187912, MIM:616838,
            neXtProt:NX_Q6ZS10, OpenTargets:ENSG00000187912,
            PharmGKB:PA164717947, VEuPathDB:HostDB:ENSG00000187912,
            eggNOG:KOG4297, GeneTree:ENSGT00940000163153,
            HOGENOM:CLU_063069_0_0_1, InParanoid:Q6ZS10, OMA:SFWEPEE,
            OrthoDB:3855735at2759, PhylomeDB:Q6ZS10, TreeFam:TF343491,
            PathwayCommons:Q6ZS10, SignaLink:Q6ZS10, BioGRID-ORCS:388512,
            GenomeRNAi:388512, Pharos:Q6ZS10, PRO:PR:Q6ZS10,
            Proteomes:UP000005640, RNAct:Q6ZS10, Bgee:ENSG00000187912,
            ExpressionAtlas:Q6ZS10, GO:0009986, GO:0009897, GO:0042806,
            GO:0042802, GO:0005537, GO:0046872, CDD:cd03590,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033989, InterPro:IPR016187,
            PANTHER:PTHR22803:SF145, PANTHER:PTHR22803, Pfam:PF00059,
            SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Alternative splicing; Calcium; Disulfide bond; Glycoprotein;
            Lectin; Mannose-binding; Membrane; Metal-binding; Receptor;
            Reference proteome; Signal-anchor; Transmembrane; Transmembrane
            helix.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Graham,S.A., Jegouzo,S.A., Yan,S., Powlesland,A.S., Brady,J.P.,
            Taylor,M.E. and Drickamer,K.
  TITLE     Prolectin, a glycan-binding receptor on dividing B cells in
            germinal centers
  JOURNAL   J Biol Chem 284 (27), 18537-18544 (2009)
   PUBMED   19419970
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), FUNCTION,
            SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
            PHOSPHORYLATION.;
            TISSUE=Spleen
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).;
            TISSUE=Peripheral blood monocyte
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Mural,R.J., Istrail,S., Sutton,G.G., Florea,L., Halpern,A.L.,
            Mobarry,C.M., Lippert,R., Walenz,B., Shatkay,H., Dew,I.,
            Miller,J.R., Flanigan,M.J., Edwards,N.J., Bolanos,R., Fasulo,D.,
            Halldorsson,B.V., Hannenhalli,S., Turner,R., Yooseph,S., Lu,F.,
            Nusskern,D.R., Shue,B.C., Zheng,X.H., Zhong,F., Delcher,A.L.,
            Huson,D.H., Kravitz,S.A., Mouchard,L., Reinert,K., Remington,K.A.,
            Clark,A.G., Waterman,M.S., Eichler,E.E., Adams,M.D.,
            Hunkapiller,M.W., Myers,E.W. and Venter,J.C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-JUL-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     On Jul 14, 2010 this sequence version replaced Q6ZS10.1.
            [FUNCTION] Cell surface receptor which may be involved in
            carbohydrate-mediated communication between cells in the germinal
            center. Binds glycans with terminal alpha-linked mannose or fucose
            residues. {ECO:0000269|PubMed:19419970}.
            [SUBUNIT] Oligomer; disulfide-linked.
            {ECO:0000269|PubMed:19419970}.
            [INTERACTION] Q6ZS10; P07307-3: ASGR2; NbExp=3;
            IntAct=EBI-11977093, EBI-12808270; Q6ZS10; P27449: ATP6V0C;
            NbExp=3; IntAct=EBI-11977093, EBI-721179; Q6ZS10; P56748: CLDN8;
            NbExp=3; IntAct=EBI-11977093, EBI-10215641; Q6ZS10; Q6ZS10:
            CLEC17A; NbExp=3; IntAct=EBI-11977093, EBI-11977093; Q6ZS10;
            Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-11977093, EBI-12019274; Q6ZS10;
            Q07325: CXCL9; NbExp=3; IntAct=EBI-11977093, EBI-3911467; Q6ZS10;
            Q92520: FAM3C; NbExp=3; IntAct=EBI-11977093, EBI-2876774; Q6ZS10;
            Q8TDT2: GPR152; NbExp=3; IntAct=EBI-11977093, EBI-13345167; Q6ZS10;
            P24593: IGFBP5; NbExp=4; IntAct=EBI-11977093, EBI-720480; Q6ZS10;
            O43639: NCK2; NbExp=3; IntAct=EBI-11977093, EBI-713635; Q6ZS10;
            Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-11977093, EBI-10317425; Q6ZS10;
            Q6UX06: OLFM4; NbExp=3; IntAct=EBI-11977093, EBI-2804156; Q6ZS10;
            Q96FA3: PELI1; NbExp=3; IntAct=EBI-11977093, EBI-448369; Q6ZS10;
            Q9HAT8: PELI2; NbExp=3; IntAct=EBI-11977093, EBI-448407; Q6ZS10;
            Q9NS64: RPRM; NbExp=4; IntAct=EBI-11977093, EBI-1052363; Q6ZS10;
            Q15436: SEC23A; NbExp=3; IntAct=EBI-11977093, EBI-81088; Q6ZS10;
            Q9BZL3: SMIM3; NbExp=6; IntAct=EBI-11977093, EBI-741850; Q6ZS10;
            P48230: TM4SF4; NbExp=3; IntAct=EBI-11977093, EBI-8650934; Q6ZS10;
            Q9NV12: TMEM140; NbExp=3; IntAct=EBI-11977093, EBI-2844246; Q6ZS10;
            Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-11977093, EBI-11994282;
            Q6ZS10; A2RU14: TMEM218; NbExp=3; IntAct=EBI-11977093,
            EBI-10173151; Q6ZS10; O00526: UPK2; NbExp=3; IntAct=EBI-11977093,
            EBI-10179682.
            [SUBCELLULAR LOCATION] Membrane {ECO:0000305}; Single-pass type II
            membrane protein {ECO:0000305}. Note=In fibroblasts, expressed on
            the cell surface. {ECO:0000269|PubMed:19419970}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=3; Name=1; IsoId=Q6ZS10-1; Sequence=Displayed; Name=2;
            IsoId=Q6ZS10-2; Sequence=VSP_039405, VSP_039406; Name=3;
            IsoId=Q6ZS10-3; Sequence=VSP_039407, VSP_039408.
            [TISSUE SPECIFICITY] Expressed on dividing B-cells of germinal
            centers in various tissues, including lymph nodes, tonsils,
            stomach, intestine, appendix and spleen.
            {ECO:0000269|PubMed:19419970}.
            [PTM] Phosphorylated on tyrosine residues.
            {ECO:0000269|PubMed:19419970}.
            [MISCELLANEOUS] [Isoform 2]: May be produced at very low levels due
            to a premature stop codon in the mRNA, leading to nonsense-mediated
            mRNA decay. {ECO:0000305}.
            [SEQUENCE CAUTION] Sequence=EAW84437.1; Type=Erroneous gene model
            prediction; Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..378
                     /gene="CLEC17A"
     Protein         1..378
                     /product="C-type lectin domain family 17, member A"
                     /note="Prolectin"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..378
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 17, member A.
                     /id=PRO_0000319428."
     Region          1..172
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          1..119
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          <6..153
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          85..99
                     /region_name="Compositionally biased region"
                     /note="Pro residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          173..193
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          194..378
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            237
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          248..265
                     /region_name="Splicing variant"
                     /note="DCRRITCPEGWLPFEGKC -> EFCGQGPWLSTGVLAGAE (in
                     isoform 2). /evidence=ECO:0000303|PubMed:15489334.
                     /id=VSP_039405."
     Region          254..374
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(254,265)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          261..373
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          266..378
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:15489334. /id=VSP_039406."
     Bond            bond(282,372)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            285
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          299..306
                     /region_name="Splicing variant"
                     /note="NFVAKAHG -> LLGARGTQ (in isoform 3).
                     /evidence=ECO:0000303|PubMed:14702039. /id=VSP_039407."
     Region          307..378
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 3).
                     /evidence=ECO:0000303|PubMed:14702039. /id=VSP_039408."
     Site            order(310,341,343,348,354..355,360..363)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(317,321,344,348..349)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(321,349)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Bond            bond(350,364)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mhnlysitgy pdppgtmeee eedddyenst ppykdlppkp gtmeeeeedd dyenstppyk
       61 dlppkpgtme eeeedddyen stppykdlpp kpgssapprp praaketekp plpckprnmt
      121 gldlaavtcp ppqlavnlep splqpslaat pvpwlnqrsg gpgccqkrwm vylcllvvts
      181 lflgclgltv tlikyqelme elrmlsfqqm twrtnmtgma glaglkhdia rvradtnqsl
      241 velwglldcr ritcpegwlp fegkcyyfsp stkswdearm fcqenyshlv iinsfaehnf
      301 vakahgsprv ywlglndraq egdwrwldgs pvtlsfwepe epnnihdedc atmnkggtwn
      361 dlscykttyw icerkcsc
//
LOCUS       PGCB_MOUSE               883 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Brevican core protein; Flags: Precursor.
ACCESSION   Q61361
VERSION     Q61361.2
DBSOURCE    UniProtKB: locus PGCB_MOUSE, accession Q61361;
            class: standard.
            extra accessions:Q80WT7
            created: Nov 1, 1997.
            sequence updated: Jul 27, 2011.
            annotation updated: Sep 13, 2023.
            xrefs: X87096.1, CAA60575.1, CH466547.2, EDL15323.1, BC052032.1,
            AAH52032.1, S57653, NP_001103228.1, NP_031555.2, XP_006500999.1,
            XP_006501000.1
            xrefs (non-sequence databases): CCDS:CCDS17462.1,
            AlphaFoldDB:Q61361, SMR:Q61361, BioGRID:198308, IntAct:Q61361,
            MINT:Q61361, STRING:10090.ENSMUSP00000088491, GlyConnect:2161,
            GlyCosmos:Q61361, GlyGen:Q61361, iPTMnet:Q61361,
            PhosphoSitePlus:Q61361, SwissPalm:Q61361, jPOST:Q61361,
            MaxQB:Q61361, PaxDb:Q61361, PeptideAtlas:Q61361,
            ProteomicsDB:288130, ABCD:Q61361, Antibodypedia:2188, DNASU:12032,
            Ensembl:ENSMUST00000090971, Ensembl:ENSMUSP00000088491,
            Ensembl:ENSMUSG00000004892, GeneID:12032, KEGG:mmu:12032,
            UCSC:uc008pto.2, AGR:MGI:1096385, CTD:63827, MGI:1096385,
            VEuPathDB:HostDB:ENSMUSG00000004892, eggNOG:KOG4297,
            GeneTree:ENSGT00940000157343, HOGENOM:CLU_000303_0_0_1,
            InParanoid:Q61361, OMA:APQISCV, OrthoDB:5402504at2759,
            PhylomeDB:Q61361, TreeFam:TF332134, Reactome:R-MMU-1474228,
            Reactome:R-MMU-1971475, Reactome:R-MMU-2022870,
            Reactome:R-MMU-2022923, Reactome:R-MMU-2024101,
            Reactome:R-MMU-3000178, BioGRID-ORCS:12032, ChiTaRS:Bcan,
            PRO:PR:Q61361, Proteomes:UP000000589, RNAct:Q61361,
            Bgee:ENSMUSG00000004892, ExpressionAtlas:Q61361,
            Genevisible:Q61361, GO:0030424, GO:0043194, GO:0009986, GO:0030425,
            GO:0031012, GO:0005615, GO:0098982, GO:0098978, GO:0033268,
            GO:0072534, GO:0098966, GO:0045202, GO:0097060, GO:0005509,
            GO:0030246, GO:0005540, GO:0007160, GO:0007417, GO:0010001,
            GO:0021766, GO:1990138, GO:0002052, GO:0001501, GO:0060074,
            CDD:cd00033, CDD:cd00054, CDD:cd03517, CDD:cd03520,
            Gene3D:2.10.70.10, Gene3D:2.60.40.10, Gene3D:2.10.25.10,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR016187, InterPro:IPR001881,
            InterPro:IPR000742, InterPro:IPR007110, InterPro:IPR036179,
            InterPro:IPR013783, InterPro:IPR003006, InterPro:IPR003599,
            InterPro:IPR013106, InterPro:IPR000538, InterPro:IPR035976,
            InterPro:IPR000436, PANTHER:PTHR22804, PANTHER:PTHR22804:SF47,
            Pfam:PF00008, Pfam:PF00059, Pfam:PF00084, Pfam:PF07686,
            Pfam:PF00193, PRINTS:PR01265, SMART:SM00032, SMART:SM00034,
            SMART:SM00181, SMART:SM00179, SMART:SM00409, SMART:SM00406,
            SMART:SM00445, SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF48726,
            PROSITE:PS00615, PROSITE:PS50041, PROSITE:PS00022, PROSITE:PS01186,
            PROSITE:PS50026, PROSITE:PS50835, PROSITE:PS00290, PROSITE:PS01241,
            PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Disulfide bond; EGF-like domain; Extracellular matrix;
            Glycoprotein; Hyaluronic acid; Immunoglobulin domain; Lectin;
            Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted;
            Signal; Sushi.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Rauch,U., Meyer,H., Brakebusch,C., Seidenbecher,C.,
            Gundelfinger,E.D., Beier,D.R. and Fassler,R.
  TITLE     Sequence and chromosomal localization of the mouse brevican gene
  JOURNAL   Genomics 44 (1), 15-21 (1997)
   PUBMED   9286696
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.;
            STRAIN=BALB/cJ; TISSUE=Brain
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Mural,R.J., Adams,M.D., Myers,E.W., Smith,H.O. and Venter,J.C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-JUL-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=C57BL/6J; TISSUE=Brain
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Bekku,Y., Su,W.D., Hirakawa,S., Fassler,R., Ohtsuka,A., Kang,J.S.,
            Sanders,J., Murakami,T., Ninomiya,Y. and Oohashi,T.
  TITLE     Molecular cloning of Bral2, a novel brain-specific link protein,
            and immunohistochemical colocalization with brevican in
            perineuronal nets
  JOURNAL   Mol Cell Neurosci 24 (1), 148-159 (2003)
   PUBMED   14550776
  REMARK    TISSUE SPECIFICITY.
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Brain cortex
REFERENCE   6  (residues 1 to 883)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Brain
REFERENCE   7  (residues 1 to 883)
  AUTHORS   Bekku,Y., Saito,M., Moser,M., Fuchigami,M., Maehara,A.,
            Nakayama,M., Kusachi,S., Ninomiya,Y. and Oohashi,T.
  TITLE     Bral2 is indispensable for the proper localization of brevican and
            the structural integrity of the perineuronal net in the brainstem
            and cerebellum
  JOURNAL   J Comp Neurol 520 (8), 1721-1736 (2012)
   PUBMED   22121037
  REMARK    TISSUE SPECIFICITY.
REFERENCE   8  (residues 1 to 883)
  AUTHORS   Felemban,M., Dorgau,B., Hunt,N.C., Hallam,D., Zerti,D., Bauer,R.,
            Ding,Y., Collin,J., Steel,D., Krasnogor,N., Al-Aama,J., Lindsay,S.,
            Mellough,C. and Lako,M.
  TITLE     Extracellular matrix component expression in human pluripotent stem
            cell-derived retinal organoids recapitulates retinogenesis in vivo
            and reveals an important role for IMPG1 and CD44 in the development
            of photoreceptors and interphotoreceptor matrix
  JOURNAL   Acta Biomater 74, 207-221 (2018)
   PUBMED   29777959
  REMARK    TISSUE SPECIFICITY.
COMMENT     On or before Jul 29, 2011 this sequence version replaced
            gi:81873334, Q61361.1.
            [FUNCTION] May play a role in the terminally differentiating and
            the adult nervous system during postnatal development. Could
            stabilize interactions between hyaluronan (HA) and brain
            proteoglycans.
            [SUBUNIT] Interacts with TNR. {ECO:0000250}.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000250}. Secreted {ECO:0000250|UniProtKB:Q96GW7}.
            [TISSUE SPECIFICITY] Expressed in the retina, specifically around
            the inner and outer segments of photoreceptors, retinal pigment
            epithelium, outer plexiform layer, and the ganglion cell layer (at
            protein level) (PubMed:29777959). Brain (PubMed:9286696,
            PubMed:14550776, PubMed:22121037). Expressed in the brainstem and
            cerebellum in a perineuronal net pattern (PubMed:14550776,
            PubMed:22121037). {ECO:0000269|PubMed:14550776,
            ECO:0000269|PubMed:22121037, ECO:0000269|PubMed:29777959,
            ECO:0000269|PubMed:9286696}.
            [PTM] O-glycosylated; contains chondroitin sulfate.
            {ECO:0000250|UniProtKB:Q96GW7}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Brevican;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_155'.
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..883
                     /gene="Bcan"
     Protein         1..883
                     /product="Brevican core protein"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          23..883
                     /region_name="Mature chain"
                     /note="Brevican core protein. /id=PRO_0000017512."
     Region          35..154
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          42
                     /region_name="Conflict"
                     /note="T -> A (in Ref. 1; CAA60575).
                     /evidence=ECO:0000305."
     Region          44..158
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:448366"
     Region          52..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Bond            bond(56,136)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          65
                     /region_name="Conflict"
                     /note="H -> R (in Ref. 1; CAA60575).
                     /evidence=ECO:0000305."
     Region          75..79
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          119..123
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          133..138
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          151..154
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          156..251
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          156..250
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            166..167
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(178,249)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(202,223)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079."
     Region          256..353
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          257..352
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            264..265
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(276,351)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(300,321)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          402..592
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            413
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:Q96GW7."
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55068."
     Region          448..471
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          473..>618
                     /region_name="Treacle"
                     /note="Treacher Collins syndrome protein Treacle;
                     pfam03546"
                     /db_xref="CDD:427362"
     Region          479..501
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          504
                     /region_name="Conflict"
                     /note="G -> D (in Ref. 1; CAA60575).
                     /evidence=ECO:0000305."
     Region          514
                     /region_name="Conflict"
                     /note="V -> F (in Ref. 1; CAA60575).
                     /evidence=ECO:0000305."
     Region          528..530
                     /region_name="Conflict"
                     /note="GSP -> WSA (in Ref. 1; CAA60575).
                     /evidence=ECO:0000305."
     Region          622..658
                     /region_name="Domain"
                     /note="EGF-like.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          626..655
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Bond            bond(626,637)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(631,646)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(648,657)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          658..786
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          664..787
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(664,675)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(692,784)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(758,762,764,770,772..775,778..780)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(760,776)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          789..849
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          791..848
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(791,834)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(801,821)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(820,847)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          854..883
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
        1 miplllslla alvltqapaa laddlkedss edrafrvrig atqlrgvlgg alaipchvhh
       61 lrpphsrraa pgfprvkwtf lsgdrevevl varglrvkvn eayrfrvalp aypasltdvs
      121 lvlselrpnd sgvyrcevqh giddssdave vkvkgvvfly regsaryafs fagaqeacar
      181 igariatpeq lyaaylggye qcdagwlsdq tvrypiqnpr eacsgdmdgy pgvrnygvvg
      241 pddlydvycy aedlngelfl gappskltwe eardyclerg aqiastgqly aawnggldrc
      301 spgwladgsv rypiitpsqr cggglpgvkt lflfpnqtgf pskqnrfnvy cfrdsahpsa
      361 sseasspasd gleaivtvte kleelqlpqe amesesrgai ysipisedgg ggsstpedpa
      421 eaprtplese tqsiapptes seeegvalee eerfkdleal eeekeqedlw vwprelsspl
      481 ptgsetehsl sqvsppaqav lqlgaspspg pprvrgppae tllppregsp tstpggarev
      541 ggetgspels gvpreseeag sssledgpsl lpatwapvgp reletpseek sgrtvlagts
      601 vqaqpvlptd sashggvava pssgdcipsp chnggtclee kegfrclclp gyggdlcdvg
      661 lhfcspgwea fqgacykhfs trrsweeaes qcralgahlt sictpeeqdf vndryreyqw
      721 iglndrtieg dflwsdgapl lyenwnpgqp dsyflsgenc vvmvwhdqgq wsdvpcnyhl
      781 sytckmglvs cgpppqlpla qifgrprlry avdtvlryrc rdglaqrnlp lircqenglw
      841 eapqiscvpr rpgralrsmd apegprgqls rhrkapltpp ssl
//
LOCUS       CLC4A_RAT                240 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 4 member A; AltName:
            Full=C-type lectin superfamily member 6; AltName: Full=Dendritic
            cell inhibitory receptor; AltName: CD_antigen=CD367.
ACCESSION   Q67EQ0
VERSION     Q67EQ0.1
DBSOURCE    UniProtKB: locus CLC4A_RAT, accession Q67EQ0;
            class: standard.
            created: Feb 15, 2005.
            sequence updated: Oct 11, 2004.
            annotation updated: Sep 13, 2023.
            xrefs: AY363176.2, AAR18686.1
            xrefs (non-sequence databases): AlphaFoldDB:Q67EQ0, SMR:Q67EQ0,
            STRING:10116.ENSRNOP00000037071, GlyCosmos:Q67EQ0, GlyGen:Q67EQ0,
            PaxDb:Q67EQ0, UCSC:RGD:1359662, AGR:RGD:1359662, RGD:1359662,
            eggNOG:KOG4297, InParanoid:Q67EQ0, PhylomeDB:Q67EQ0, PRO:PR:Q67EQ0,
            Proteomes:UP000002494, GO:0009897, GO:0005509, GO:0030246,
            GO:0005537, GO:0038187, GO:0002250, GO:0061760, GO:0042590,
            GO:0036037, GO:0050832, GO:0001879, GO:0045087, GO:0001818,
            GO:0032720, GO:0002470, GO:0001819, GO:0043123, GO:1902533,
            GO:0050731, GO:2000318, GO:0001878, GO:0002223, CDD:cd03590,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033989, InterPro:IPR016187,
            PANTHER:PTHR46784, PANTHER:PTHR46784:SF1, Pfam:PF00059,
            SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Adaptive immunity; Calcium; Cell membrane; Disulfide bond;
            Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
            Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
            Transmembrane helix.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Flornes,L.M., Bryceson,Y.T., Spurkland,A., Lorentzen,J.C.,
            Dissen,E. and Fossum,S.
  TITLE     Identification of lectin-like receptors expressed by antigen
            presenting cells and neutrophils and their mapping to a novel gene
            complex
  JOURNAL   Immunogenetics 56 (7), 506-517 (2004)
   PUBMED   15368084
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.;
            STRAIN=PVG
COMMENT     [FUNCTION] C-type lectin receptor that binds carbohydrates mannose
            and fucose but also weakly interacts with N-acetylglucosamine
            (GlcNAc) in a Ca(2+)-dependent manner. Involved in regulating
            immune reactivity. Once triggered by antigen, it is internalized by
            clathrin-dependent endocytosis and delivers its antigenic cargo
            into the antigen presentation pathway resulting in cross-priming of
            CD8(+) T cells. This cross-presentation and cross-priming are
            enhanced by TLR7 and TLR8 agonists with increased expansion of the
            CD8(+) T cells, high production of IFNG and TNF with reduced levels
            of IL4, IL5 and IL13. In plasmacytoid dendritic cells, inhibits
            TLR9-mediated IFNA and TNF production. May be involved via its ITIM
            motif (immunoreceptor tyrosine-based inhibitory motifs) in the
            inhibition of B-cell-receptor-mediated calcium mobilization and
            protein tyrosine phosphorylation. {ECO:0000250|UniProtKB:Q9UMR7}.
            [SUBUNIT] May interact with PTPN6 via its ITIM site.
            {ECO:0000250|UniProtKB:Q9UMR7}.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000305}; Single-pass
            type II membrane protein {ECO:0000305}; Extracellular side
            {ECO:0000250|UniProtKB:Q9UMR7}.
            [TISSUE SPECIFICITY] Expressed by myeloid cells (dendritic cells,
            macrophages, and neutrophils) and B-cells.
            {ECO:0000269|PubMed:15368084}.
            [DOMAIN] Contains 1 copy of a cytoplasmic motif that is referred to
            as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This
            motif is involved in modulation of cellular responses. The
            phosphorylated ITIM motif can bind the SH2 domain of several
            SH2-containing phosphatases. {ECO:0000250|UniProtKB:Q9UMR7}.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..240
                     /gene="Clec4a"
                     /gene_synonym="Clecsf6"
                     /gene_synonym="Dcir"
     Protein         1..240
                     /product="C-type lectin domain family 4 member A"
                     /note="C-type lectin superfamily member 6; Dendritic cell
                     inhibitory receptor"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..240
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 4 member A.
                     /id=PRO_0000046614."
     Region          1..48
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          5..10
                     /region_name="Short sequence motif of biological interest"
                     /note="ITIM motif."
     Region          18..38
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          49..69
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          70..240
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          107..235
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(107,118)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          129..235
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(140,233)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(168,200,202,206,212..213,221..224)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(175,178,203,206..207)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(178,207)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(208,225)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 maseityaev riknesnssv tysgspaapr ekptrhlskp gsllvpftsl mvlllllait
       61 flvafiiyfq kysqfleekk aikgithkel nciknvllme ekswsccpkn wkpfgshcyw
      121 vtkhtstysk aswseseknc fsmgahllvi hskeeqdfit gilnrdaayf iglwdsghrq
      181 wqwvsqtpyn asatfwhkge pssddekcvi inhlnsgwgw ndipcsgkqq svcqmkkiql
//
LOCUS       DCAL2_DRONO              142 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Dromaiocalcin-2; Short=DCA-2.
ACCESSION   P84616
VERSION     P84616.2
DBSOURCE    UniProtKB: locus DCAL2_DRONO, accession P84616;
            class: standard.
            created: Aug 30, 2005.
            sequence updated: Feb 7, 2006.
            annotation updated: Feb 22, 2023.
            xrefs (non-sequence databases): AlphaFoldDB:P84616, SMR:P84616,
            iPTMnet:P84616, GO:0005576, GO:0030246, CDD:cd03594,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR016187, PANTHER:PTHR22803, PANTHER:PTHR22803:SF116,
            Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS50041
KEYWORDS    Direct protein sequencing; Disulfide bond; Extracellular matrix;
            Lectin; Phosphoprotein; Secreted.
SOURCE      Dromaius novaehollandiae (emu)
  ORGANISM  Dromaius novaehollandiae
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
            Coelurosauria; Aves; Palaeognathae; Casuariiformes; Dromaiidae;
            Dromaius.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Mann,K. and Siedler,F.
  TITLE     Amino acid sequences and phosphorylation sites of emu and rhea
            eggshell C-type lectin-like proteins
  JOURNAL   Comp. Biochem. Physiol. 143B, 160-170 (2006)
   PUBMED   16403478
  REMARK    PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-62
            AND SER-68.;
            TISSUE=Eggshell matrix
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Mann,K.
  TITLE     Identification of the major proteins of the organic matrix of emu
            (Dromaius novaehollandiae) and rhea (Rhea americana) eggshell
            calcified layer
  JOURNAL   Br Poult Sci 45 (4), 483-490 (2004)
   PUBMED   15484722
  REMARK    PROTEIN SEQUENCE OF 1-30.;
            TISSUE=Eggshell matrix {ECO:0000269|PubMed:15484722}
COMMENT     On Mar 21, 2006 this sequence version replaced gi:73919010.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix. Note=Eggshell matrix.
            [PTM] A minor form with some unmodified Ser-68 and partial
            phosphorylation of Ser-66 may also occur.
            {ECO:0000269|PubMed:16403478}.
            [MASS SPECTROMETRY] Mass=16645.6; Method=Electrospray;
            Evidence={ECO:0000269|PubMed:16403478}.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Dromaius novaehollandiae"
                     /db_xref="taxon:8790"
     Protein         1..142
                     /product="Dromaiocalcin-2"
                     /note="DCA-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..142
                     /region_name="Mature chain"
                     /note="Dromaiocalcin-2. /id=PRO_0000046717."
     Region          6..140
                     /region_name="CLECT_REG-1_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in Human REG-1 (lithostathine), REG-4, and avian
                     eggshell-specific proteins: ansocalcin,
                     structhiocalcin-1(SCA-1), and -2(SCA-2); cd03594"
                     /db_xref="CDD:153064"
     Bond            bond(6,17)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9PRS8,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          13..139
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(34,138)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9PRS8,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16403478."
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16403478."
     Site            order(111,126..127)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153064"
     Bond            bond(113,130)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9PRS8,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 eeeigctsgw vpfdgrcygf fpqelswrra esfcqrlgar thlvsihnee ehqaiismla
       61 ssqpysdsee qeangdvwig lrlslrrlwe wsdgtkldyg swyrdvlprr racaaledta
      121 dfaswdvelc sdrkpficay rt
//
LOCUS       PGCB_BOVIN               912 aa            linear   MAM 13-SEP-2023
DEFINITION  RecName: Full=Brevican core protein; Flags: Precursor.
ACCESSION   Q28062
VERSION     Q28062.1
DBSOURCE    UniProtKB: locus PGCB_BOVIN, accession Q28062;
            class: standard.
            created: Nov 1, 1997.
            sequence updated: Nov 1, 1997.
            annotation updated: Sep 13, 2023.
            xrefs: X75887.1, CAA53481.1, A54423
            xrefs (non-sequence databases): AlphaFoldDB:Q28062, SMR:Q28062,
            STRING:9913.ENSBTAP00000020965, GlyCosmos:Q28062, PaxDb:Q28062,
            eggNOG:KOG4297, InParanoid:Q28062, Proteomes:UP000009136,
            GO:0005615, GO:0072534, GO:0045202, GO:0030246, GO:0005540,
            GO:0007155, GO:0007417, GO:0010001, GO:0002052, GO:0001501,
            CDD:cd00033, CDD:cd00054, CDD:cd03517, CDD:cd03520,
            Gene3D:2.10.70.10, Gene3D:2.60.40.10, Gene3D:2.10.25.10,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR016187, InterPro:IPR000742,
            InterPro:IPR007110, InterPro:IPR036179, InterPro:IPR013783,
            InterPro:IPR003006, InterPro:IPR003599, InterPro:IPR013106,
            InterPro:IPR000538, InterPro:IPR035976, InterPro:IPR000436,
            PANTHER:PTHR22804, PANTHER:PTHR22804:SF41, Pfam:PF00008,
            Pfam:PF00059, Pfam:PF00084, Pfam:PF07686, Pfam:PF00193,
            PRINTS:PR01265, SMART:SM00032, SMART:SM00034, SMART:SM00181,
            SMART:SM00409, SMART:SM00406, SMART:SM00445, SUPFAM:SSF56436,
            SUPFAM:SSF57535, SUPFAM:SSF48726, PROSITE:PS00615, PROSITE:PS50041,
            PROSITE:PS00022, PROSITE:PS01186, PROSITE:PS50026, PROSITE:PS50835,
            PROSITE:PS00290, PROSITE:PS01241, PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Direct protein sequencing; Disulfide bond; EGF-like domain;
            Extracellular matrix; Glycoprotein; Hyaluronic acid; Immunoglobulin
            domain; Lectin; Phosphoprotein; Proteoglycan; Reference proteome;
            Repeat; Secreted; Signal; Sushi.
SOURCE      Bos taurus (cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Yamada,H., Watanabe,K., Shimonaka,M. and Yamaguchi,Y.
  TITLE     Molecular cloning of brevican, a novel brain proteoglycan of the
            aggrecan/versican family
  JOURNAL   J Biol Chem 269 (13), 10119-10126 (1994)
   PUBMED   8144512
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.;
            TISSUE=Brain
COMMENT     On Mar 15, 2005 this sequence version replaced gi:627722.
            [FUNCTION] May play a role in the terminally differentiating and
            the adult nervous system during postnatal development. Could
            stabilize interactions between hyaluronan (HA) and brain
            proteoglycans.
            [SUBUNIT] Interacts with TNR. {ECO:0000250}.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000250}. Secreted {ECO:0000250|UniProtKB:Q96GW7}.
            [TISSUE SPECIFICITY] Brain; expressed in cerebellar astrocytes but
            not in neurons.
            [PTM] O-glycosylated; contains chondroitin sulfate.
            {ECO:0000250|UniProtKB:Q96GW7}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
     gene            1..912
                     /gene="BCAN"
     Protein         1..912
                     /product="Brevican core protein"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          23..912
                     /region_name="Mature chain"
                     /note="Brevican core protein. /id=PRO_0000017509."
     Region          36..155
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          39..159
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:448366"
     Region          53..57
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Bond            bond(57,137)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          76..80
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..124
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          134..139
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..155
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          157..252
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          157..251
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            167..168
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(179,250)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(203,224)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          257..354
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          258..353
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            265..266
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(277,352)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(301,322)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          <356..595
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          408..427
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            418
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:Q96GW7."
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55068."
     Region          438..651
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          461..479
                     /region_name="Compositionally biased region"
                     /note="Acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          516..541
                     /region_name="Compositionally biased region"
                     /note="Pro residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          647..683
                     /region_name="Domain"
                     /note="EGF-like.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          651..680
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Bond            bond(651,662)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(656,671)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(673,682)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          683..811
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          689..812
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(689,700)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(717,809)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(783,787,789,795,797..800,803..805)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(785,801)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          814..874
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          816..873
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(816,859)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(826,846)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(845,872)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
ORIGIN
        1 maplflplla tlvlawipva ladalegdss edrafrvria gdaplqgvlg galtipchvh
       61 ylrpspsrra aqgsprvkwt flsggreaev lvarglrvkv seayrfrval paypasltdv
      121 slvlselrpn dsgiyrcevq hgiddssdav evkvkgvvfl yregsaryaf sfagaqeaca
      181 rigariatpe qlyaaylggy eqcdagwlsd qtvrypiqtp reacygdmdg fpgvrnygvv
      241 dpddlydvyc yaeelngelf lgappdkltl eeartycqer gakiattgql yaawdggldr
      301 cssgwlsdgs vrypivtpsq rcggglpgvk tlflfpnqtg fpnkhsrfnv ycfrdsaqps
      361 aipeaanpas hlasdaleai vtvtetleel klpqeavese srgaiysipi iedggggsst
      421 pedpaeaprt llefetqsiv pplgsseeeg kvleqeekyr geeekeeeee eeevedealw
      481 awpselssld peaplptepv peesltqasp pvraalqpgv spppydepea prpprvlgpp
      541 tktlptpreg nlaspppstl vgareieeet ggpelsgapr geseetgsse dapsllpatr
      601 apgdtrdlet pseensrrtv pagtsvraqp vlptdsasrg gvavapssgd cvpspchngg
      661 tcleeeegvr clclpgyggd lcdvglhfcs pgwdafqgac ykhfsarrsw eeaenkcrmy
      721 gahlasistp eeqdfinnry reyqwiglnd rtiegdflws dgvpllyenw npgqpdsyfl
      781 sgencvvmvw hdqgqwsdvp cnyhlsytck mglvscgppp elplaevfgr prlryevdtv
      841 lryrcreglt qrnlplircq engrwglpqi scvprrpara lrpveaqegr pwrlvghwka
      901 rlnpspnpap gp
//
LOCUS       PGCA_HUMAN              2530 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=Aggrecan core protein; AltName:
            Full=Cartilage-specific proteoglycan core protein; Short=CSPCP;
            AltName: Full=Chondroitin sulfate proteoglycan core protein 1;
            Short=Chondroitin sulfate proteoglycan 1; Contains: RecName:
            Full=Aggrecan core protein 2; Flags: Precursor.
ACCESSION   P16112
VERSION     P16112.3
DBSOURCE    UniProtKB: locus PGCA_HUMAN, accession P16112;
            class: standard.
            extra
            accessions:B9EK55,E7ENV9,E7EX88,H0YM81,Q13650,Q9UCD3,Q9UCP4,Q9UCP5,
            Q9UDE0
            created: Apr 1, 1990.
            sequence updated: Mar 28, 2018.
            annotation updated: Sep 13, 2023.
            xrefs: M55172.1, AAA62824.1, AC103982.10, BC150624.1, AAI50625.1,
            X80278.1, S74659.1, AAC60643.2, X17406.1, CAA35463.1, J05062.1,
            AAA35726.1, A39086, NP_001126.3, NP_037359.3, XP_011519616.1,
            4MD4_C, 7RDV_H
            xrefs (non-sequence databases): CCDS:CCDS53970.1, CCDS:CCDS53971.1,
            CCDS:CCDS92056.1, PDBsum:4MD4, PDBsum:7RDV, AlphaFoldDB:P16112,
            SMR:P16112, IntAct:P16112, MINT:P16112,
            STRING:9606.ENSP00000387356, DrugBank:DB02255, GlyConnect:2002,
            GlyCosmos:P16112, GlyGen:P16112, iPTMnet:P16112,
            PhosphoSitePlus:P16112, BioMuta:ACAN, DMDM:129886, jPOST:P16112,
            MassIVE:P16112, PaxDb:P16112, PeptideAtlas:P16112,
            ProteomicsDB:17235, ProteomicsDB:19009, ProteomicsDB:40179,
            ProteomicsDB:53288, ProteomicsDB:53289, ProteomicsDB:53290,
            Antibodypedia:4288, DNASU:176, Ensembl:ENST00000352105.11,
            Ensembl:ENSP00000341615.7, Ensembl:ENSG00000157766.19,
            Ensembl:ENST00000439576.7, Ensembl:ENSP00000387356.2,
            Ensembl:ENST00000559004.5, Ensembl:ENSP00000453499.1, GeneID:176,
            KEGG:hsa:176, UCSC:uc010upo.1, AGR:HGNC:319, CTD:176, DisGeNET:176,
            GeneCards:ACAN, HGNC:319, HPA:ENSG00000157766, MalaCards:ACAN,
            MIM:155760, MIM:165800, MIM:608361, MIM:612813, neXtProt:NX_P16112,
            OpenTargets:ENSG00000157766, Orphanet:251262, Orphanet:435804,
            Orphanet:171866, Orphanet:93283, PharmGKB:PA24616,
            VEuPathDB:HostDB:ENSG00000157766, eggNOG:ENOG502QUX8,
            GeneTree:ENSGT00940000155971, InParanoid:P16112,
            OrthoDB:5402504at2759, PhylomeDB:P16112, TreeFam:TF332134,
            PathwayCommons:P16112, Reactome:R-HSA-1474228,
            Reactome:R-HSA-2022854, Reactome:R-HSA-2022857,
            Reactome:R-HSA-3000178, Reactome:R-HSA-3656225,
            Reactome:R-HSA-3656243, Reactome:R-HSA-3656244, SignaLink:P16112,
            SIGNOR:P16112, BioGRID-ORCS:176, ChiTaRS:ACAN, GenomeRNAi:176,
            Pharos:P16112, PRO:PR:P16112, Proteomes:UP000005640, RNAct:P16112,
            Bgee:ENSG00000157766, ExpressionAtlas:P16112, GO:0062023,
            GO:0005576, GO:0005615, GO:0005796, GO:0043202, GO:0072534,
            GO:0045202, GO:0030246, GO:0005201, GO:0005540, GO:0046872,
            GO:0007155, GO:0007417, GO:0010001, GO:0002052, GO:0006508,
            GO:0001501, CDD:cd00033, CDD:cd03588, CDD:cd00054, CDD:cd05900,
            CDD:cd03517, CDD:cd03520, Gene3D:2.10.70.10, Gene3D:2.60.40.10,
            Gene3D:2.10.25.10, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033987,
            InterPro:IPR016187, InterPro:IPR000742, InterPro:IPR007110,
            InterPro:IPR036179, InterPro:IPR013783, InterPro:IPR003006,
            InterPro:IPR003599, InterPro:IPR013106, InterPro:IPR000538,
            InterPro:IPR035976, InterPro:IPR000436, PANTHER:PTHR22804:SF42,
            PANTHER:PTHR22804, Pfam:PF00059, Pfam:PF00084, Pfam:PF07686,
            Pfam:PF00193, PRINTS:PR01265, SMART:SM00032, SMART:SM00034,
            SMART:SM00181, SMART:SM00409, SMART:SM00406, SMART:SM00445,
            SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF48726, PROSITE:PS00615,
            PROSITE:PS50041, PROSITE:PS00022, PROSITE:PS01186, PROSITE:PS50026,
            PROSITE:PS50835, PROSITE:PS00290, PROSITE:PS01241, PROSITE:PS50963,
            PROSITE:PS50923
KEYWORDS    3D-structure; Alternative splicing; Calcium; Direct protein
            sequencing; Disease variant; Disulfide bond; Dwarfism; EGF-like
            domain; Extracellular matrix; Glycoprotein; Immunoglobulin domain;
            Lectin; Metal-binding; Proteoglycan; Reference proteome; Repeat;
            Secreted; Signal; Sushi.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2530)
  AUTHORS   Doege,K.J., Sasaki,M., Kimura,T. and Yamada,Y.
  TITLE     Complete coding sequence and deduced primary structure of the human
            cartilage large aggregating proteoglycan, aggrecan. Human-specific
            repeats, and additional alternatively spliced forms
  JOURNAL   J Biol Chem 266 (2), 894-902 (1991)
   PUBMED   1985970
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS THR-913 AND
            VAL-1765.;
            TISSUE=Chondrocyte
REFERENCE   2  (residues 1 to 2530)
  AUTHORS   Zody,M.C., Garber,M., Sharpe,T., Young,S.K., Rowen,L., O'Neill,K.,
            Whittaker,C.A., Kamal,M., Chang,J.L., Cuomo,C.A., Dewar,K.,
            FitzGerald,M.G., Kodira,C.D., Madan,A., Qin,S., Yang,X., Abbasi,N.,
            Abouelleil,A., Arachchi,H.M., Baradarani,L., Birditt,B., Bloom,S.,
            Bloom,T., Borowsky,M.L., Burke,J., Butler,J., Cook,A.,
            DeArellano,K., DeCaprio,D., Dorris,L. 3rd, Dors,M., Eichler,E.E.,
            Engels,R., Fahey,J., Fleetwood,P., Friedman,C., Gearin,G.,
            Hall,J.L., Hensley,G., Johnson,E., Jones,C., Kamat,A., Kaur,A.,
            Locke,D.P., Madan,A., Munson,G., Jaffe,D.B., Lui,A., Macdonald,P.,
            Mauceli,E., Naylor,J.W., Nesbitt,R., Nicol,R., O'Leary,S.B.,
            Ratcliffe,A., Rounsley,S., She,X., Sneddon,K.M., Stewart,S.,
            Sougnez,C., Stone,S.M., Topham,K., Vincent,D., Wang,S.,
            Zimmer,A.R., Birren,B.W., Hood,L., Lander,E.S. and Nusbaum,C.
  TITLE     Analysis of the DNA sequence and duplication history of human
            chromosome 15
  JOURNAL   Nature 440 (7084), 671-675 (2006)
   PUBMED   16572171
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   3  (residues 1 to 2530)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
            LEU-864; ILE-930; THR-939; ALA-1080; ALA-1403; ALA-1508; VAL-1765;
            VAL-2079 AND GLU-2373.
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   4  (residues 1 to 2530)
  AUTHORS   Ilic,M.Z., Mok,M.T., Williamson,O.D., Campbell,M.A., Hughes,C.E.
            and Handley,C.J.
  TITLE     Catabolism of aggrecan by explant cultures of human articular
            cartilage in the presence of retinoic acid
  JOURNAL   Arch Biochem Biophys 322 (1), 22-30 (1995)
   PUBMED   7574678
  REMARK    PROTEIN SEQUENCE OF 17-27 AND 393-403, AND PROTEOLYTIC PROCESSING
            BY AGGRECANASE.
REFERENCE   5  (residues 1 to 2530)
  AUTHORS   Sandy,J.D., Flannery,C.R., Neame,P.J. and Lohmander,L.S.
  TITLE     The structure of aggrecan fragments in human synovial fluid.
            Evidence for the involvement in osteoarthritis of a novel
            proteinase which cleaves the Glu 373-Ala 374 bond of the
            interglobular domain
  JOURNAL   J Clin Invest 89 (5), 1512-1516 (1992)
   PUBMED   1569188
  REMARK    PROTEIN SEQUENCE OF 361-373 AND 393-409, PROTEOLYTIC PROCESSING,
            AND GLYCOSYLATION AT THR-371 AND THR-376.
REFERENCE   6  (residues 1 to 2530)
  AUTHORS   Glumoff,V., Savontaus,M., Vehanen,J. and Vuorio,E.
  TITLE     Analysis of aggrecan and tenascin gene expression in mouse skeletal
            tissues by northern and in situ hybridization using species
            specific cDNA probes
  JOURNAL   Biochim Biophys Acta 1219 (3), 613-622 (1994)
   PUBMED   7524681
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 350-497, AND TISSUE SPECIFICITY.;
            TISSUE=Fetal cartilage
REFERENCE   7  (residues 1 to 2530)
  AUTHORS   Lohmander,L.S., Neame,P.J. and Sandy,J.D.
  TITLE     The structure of aggrecan fragments in human synovial fluid.
            Evidence that aggrecanase mediates cartilage degradation in
            inflammatory joint disease, joint injury, and osteoarthritis
  JOURNAL   Arthritis Rheum 36 (9), 1214-1222 (1993)
   PUBMED   8216415
  REMARK    PROTEIN SEQUENCE OF 393-409.;
            TISSUE=Synovial fluid
REFERENCE   8  (residues 1 to 2530)
  AUTHORS   Barry,F.P., Neame,P.J., Sasse,J. and Pearson,D.
  TITLE     Length variation in the keratan sulfate domain of mammalian
            aggrecan
  JOURNAL   Matrix Biol 14 (4), 323-328 (1994)
   PUBMED   7827755
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 765-866.;
            TISSUE=Blood
REFERENCE   9  (residues 1 to 2530)
  AUTHORS   Dudhia,J., Davidson,C.M., Wells,T.M., Vynios,D.H., Hardingham,T.E.
            and Bayliss,M.T.
  TITLE     Age-related changes in the content of the C-terminal region of
            aggrecan in human articular cartilage
  JOURNAL   Biochem J 313 (Pt 3), 933-940 (1996)
   PUBMED   8611178
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 1893-2530 (ISOFORM 2), AND VARIANTS
            VAL-2079 AND ARG-2500.;
            TISSUE=Chondrocyte
REFERENCE   10 (residues 1 to 2530)
  AUTHORS   Baldwin,C.T., Reginato,A.M. and Prockop,D.J.
  TITLE     A new epidermal growth factor-like domain in the human core protein
            for the large cartilage-specific proteoglycan. Evidence for
            alternative splicing of the domain
  JOURNAL   J Biol Chem 264 (27), 15747-15750 (1989)
   PUBMED   2789216
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 2051-2530 (ISOFORM 1), AND VARIANTS
            VAL-2079 AND ARG-2500.
REFERENCE   11 (residues 1 to 2530)
  AUTHORS   Gleghorn,L., Ramesar,R., Beighton,P. and Wallis,G.
  TITLE     A mutation in the variable repeat region of the aggrecan gene
            (AGC1) causes a form of spondyloepiphyseal dysplasia associated
            with severe, premature osteoarthritis
  JOURNAL   Am J Hum Genet 77 (3), 484-490 (2005)
   PUBMED   16080123
  REMARK    INVOLVEMENT IN SEDK.
REFERENCE   12 (residues 1 to 2530)
  AUTHORS   Liu,T., Qian,W.J., Gritsenko,M.A., Camp,D.G. 2nd, Monroe,M.E.,
            Moore,R.J. and Smith,R.D.
  TITLE     Human plasma N-glycoproteome analysis by immunoaffinity
            subtraction, hydrazide chemistry, and mass spectrometry
  JOURNAL   J Proteome Res 4 (6), 2070-2080 (2005)
   PUBMED   16335952
  REMARK    GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-658.;
            TISSUE=Plasma
REFERENCE   13 (residues 1 to 2530)
  AUTHORS   Chen,F.H., Herndon,M.E., Patel,N., Hecht,J.T., Tuan,R.S. and
            Lawler,J.
  TITLE     Interaction of cartilage oligomeric matrix protein/thrombospondin 5
            with aggrecan
  JOURNAL   J Biol Chem 282 (34), 24591-24598 (2007)
   PUBMED   17588949
  REMARK    INTERACTION WITH COMP.
REFERENCE   14 (residues 1 to 2530)
  AUTHORS   Toledo,A.G., Pihl,J., Spliid,C.B., Persson,A., Nilsson,J.,
            Pereira,M.A., Gustavsson,T., Choudhary,S., Oo,H.Z., Black,P.C.,
            Daugaard,M., Esko,J.D., Larson,G., Salanti,A. and Clausen,T.M.
  TITLE     An affinity chromatography and glycoproteomics workflow to profile
            the chondroitin sulfate proteoglycans that interact with malarial
            VAR2CSA in the placenta and in cancer
  JOURNAL   Glycobiology 30 (12), 989-1002 (2020)
   PUBMED   32337544
  REMARK    GLYCOSYLATION.
REFERENCE   15 (residues 1 to 2530)
  AUTHORS   Ramarajan,M.G., Saraswat,M., Budhraja,R., Garapati,K., Raymond,K.
            and Pandey,A.
  TITLE     Mass spectrometric analysis of chondroitin sulfate-linked peptides
  JOURNAL   J Proteins Proteom 13 (4), 187-203 (2022)
   PUBMED   36213313
  REMARK    TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-1530; SER-1567;
            SER-1601 AND SER-1703.
REFERENCE   16 (residues 1 to 2530)
  AUTHORS   Tompson,S.W., Merriman,B., Funari,V.A., Fresquet,M., Lachman,R.S.,
            Rimoin,D.L., Nelson,S.F., Briggs,M.D., Cohn,D.H. and Krakow,D.
  TITLE     A recessive skeletal dysplasia, SEMD aggrecan type, results from a
            missense mutation affecting the C-type lectin domain of aggrecan
  JOURNAL   Am J Hum Genet 84 (1), 72-79 (2009)
   PUBMED   19110214
  REMARK    VARIANT SEMDAG ASN-2381, AND CHARACTERIZATION OF VARIANT SEMDAG
            ASN-2381.
REFERENCE   17 (residues 1 to 2530)
  AUTHORS   Stattin,E.L., Wiklund,F., Lindblom,K., Onnerfjord,P., Jonsson,B.A.,
            Tegner,Y., Sasaki,T., Struglics,A., Lohmander,S., Dahl,N.,
            Heinegard,D. and Aspberg,A.
  TITLE     A missense mutation in the aggrecan C-type lectin domain disrupts
            extracellular matrix interactions and causes dominant familial
            osteochondritis dissecans
  JOURNAL   Am J Hum Genet 86 (2), 126-137 (2010)
   PUBMED   20137779
  REMARK    VARIANT SSOAOD MET-2418, AND DETECTION OF VARIANT SSOAOD MET-2418
            BY MASS SPECTROMETRY.
COMMENT     On Apr 6, 2018 this sequence version replaced P16112.2.
            [FUNCTION] This proteoglycan is a major component of extracellular
            matrix of cartilagenous tissues. A major function of this protein
            is to resist compression in cartilage. It binds avidly to
            hyaluronic acid via an N-terminal globular region.
            [SUBUNIT] Interacts with FBLN1 (By similarity). Interacts with
            COMP. {ECO:0000250, ECO:0000269|PubMed:17588949}.
            [INTERACTION] P16112; P05067: APP; NbExp=3; IntAct=EBI-9076211,
            EBI-77613.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000250}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=3; Name=1; IsoId=P16112-1; Sequence=Displayed; Name=2;
            IsoId=P16112-2; Sequence=VSP_003074; Name=3; IsoId=P16112-3;
            Sequence=VSP_003074, VSP_003075.
            [TISSUE SPECIFICITY] Detected in fibroblasts (at protein level)
            (PubMed:36213313). Restricted to cartilage (PubMed:7524681).
            {ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:7524681}.
            [DEVELOPMENTAL STAGE] Expression was detected in chondrocytes
            throughout the developing skeleton.
            [DOMAIN] Two globular domains, G1 and G2, comprise the N-terminus
            of the proteoglycan, while another globular region, G3, makes up
            the C-terminus. G1 contains Link domains and thus consists of three
            disulfide-bonded loop structures designated as the A, B, B' motifs.
            G2 is similar to G1. The keratan sulfate (KS) and the chondroitin
            sulfate (CS) attachment domains lie between G2 and G3.
            [PTM] Contains mostly chondroitin sulfate, but also keratan sulfate
            chains, N-linked and O-linked oligosaccharides. The release of
            aggrecan fragments from articular cartilage into the synovial fluid
            at all stages of human osteoarthritis is the result of cleavage by
            aggrecanase. {ECO:0000269|PubMed:1569188,
            ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:32337544,
            ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:7574678}.
            [DISEASE] Spondyloepiphyseal dysplasia type Kimberley (SEDK)
            [MIM:608361]: Spondyloepiphyseal dysplasias are a heterogeneous
            group of congenital chondrodysplasias that specifically affect
            epiphyses and vertebrae. The autosomal dominant SEDK is associated
            with premature degenerative arthropathy.
            {ECO:0000269|PubMed:16080123}. Note=The disease is caused by
            variants affecting the gene represented in this entry.
            [DISEASE] Spondyloepimetaphyseal dysplasia, aggrecan type (SEMDAG)
            [MIM:612813]: A bone disease characterized by severe short stature,
            macrocephaly, severe midface hypoplasia, short neck, barrel chest
            and brachydactyly. The radiological findings comprise long bones
            with generalized irregular epiphyses with widened metaphyses,
            especially at the knees, platyspondyly, and multiple
            cervical-vertebral clefts. {ECO:0000269|PubMed:19110214}. Note=The
            disease is caused by variants affecting the gene represented in
            this entry.
            [DISEASE] Short stature and advanced bone age, with or without
            early-onset osteoarthritis and/or osteochondritis dissecans
            (SSOAOD) [MIM:165800]: An autosomal dominant disease characterized
            by short stature, advanced bone maturation, early-onset
            osteoarthritis, and mild dysmorphic features consisting of midface
            hypoplasia, brachydactyly, broad great toes, and lumbar lordosis.
            Other features include intervertebral disk disease and
            osteochondritis dissecans. Osteochondritis dissecans is defined as
            a separation of cartilage and subchondral bone from the surrounding
            tissue. {ECO:0000269|PubMed:20137779}. Note=The disease is caused
            by variants affecting the gene represented in this entry.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Aggrecan;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_hum_Ctlect_351'.
FEATURES             Location/Qualifiers
     source          1..2530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..2530
                     /gene="ACAN"
                     /gene_synonym="AGC1"
                     /gene_synonym="CSPG1"
                     /gene_synonym="MSK16"
     Protein         1..2530
                     /product="Aggrecan core protein"
                     /note="Cartilage-specific proteoglycan core protein;
                     Chondroitin sulfate proteoglycan core protein 1; CSPCP;
                     Chondroitin sulfate proteoglycan 1"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..16
                     /region_name="Signal"
                     /note="/evidence=ECO:0000269|PubMed:7574678."
     Region          17..2530
                     /region_name="Mature chain"
                     /note="Aggrecan core protein. /id=PRO_0000017505."
     Region          33..155
                     /region_name="Ig_Aggrecan"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), aggrecan;
                     cd05900"
                     /db_xref="CDD:409481"
     Region          33..36
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409481"
     Region          34..147
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          39..41
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409481"
     Region          45..53
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409481"
     Region          48..141
                     /region_name="Region of interest in the sequence"
                     /note="G1-A."
     Bond            bond(51,133)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          72..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409481"
     Region          83..86
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409481"
     Region          102
                     /region_name="Variant"
                     /note="D -> E (in dbSNP:rs16942318). /id=VAR_056152."
     Region          104..109
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409481"
     Region          115..121
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409481"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          129..136
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409481"
     Region          146..155
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409481"
     Region          152..247
                     /region_name="Region of interest in the sequence"
                     /note="G1-B."
     Region          153..248
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          153..247
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            163..164
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(175,246)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(199,220)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          253..349
                     /region_name="Region of interest in the sequence"
                     /note="G1-B'."
     Region          254..350
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          254..349
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            261..262
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(273,348)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          275
                     /region_name="Variant"
                     /note="R -> Q (in dbSNP:rs34949187). /id=VAR_056153."
     Region          285..286
                     /region_name="Conflict"
                     /note="QL -> HV (in Ref. 1; AAA62824).
                     /evidence=ECO:0000305."
     Bond            bond(297,318)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            371
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (keratan sulfate) threonine.
                     /evidence=ECO:0000305|PubMed:1569188."
     Site            376
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (keratan sulfate) threonine.
                     /evidence=ECO:0000305|PubMed:1569188."
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            392..393
                     /site_type="cleavage"
                     /note="Cleavage; by aggrecanase."
     Region          393..2530
                     /region_name="Mature chain"
                     /note="Aggrecan core protein 2. /id=PRO_0000017506."
     Site            434
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          477..571
                     /region_name="Region of interest in the sequence"
                     /note="G2-B."
     Region          478..573
                     /region_name="Domain"
                     /note="Link 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          478..572
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            488..489
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(500,571)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          501..502
                     /region_name="Conflict"
                     /note="LR -> PG (in Ref. 1; AAA62824).
                     /evidence=ECO:0000305."
     Bond            bond(524,545)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          578..673
                     /region_name="Region of interest in the sequence"
                     /note="G2-B'."
     Region          579..675
                     /region_name="Domain"
                     /note="Link 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          579..674
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            586..587
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(598,673)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            602
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          605
                     /region_name="Conflict"
                     /note="Missing (in Ref. 1; AAA62824).
                     /evidence=ECO:0000305."
     Bond            bond(622,643)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            658
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952."
     Region          677..849
                     /region_name="Region of interest in the sequence"
                     /note="KS."
     Region          716..>975
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          734..979
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            738
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          765..785
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          767
                     /region_name="Conflict"
                     /note="A -> E (in Ref. 1; AAA62824).
                     /evidence=ECO:0000305."
     Region          773..844
                     /region_name="Region of interest in the sequence"
                     /note="12 X 6 AA approximate tandem repeats of
                     E-[GVE]-P-[SFY]-[APT]-[TSP]."
     Region          773..778
                     /region_name="Repetitive region"
                     /note="1-1."
     Region          779..784
                     /region_name="Repetitive region"
                     /note="1-2."
     Region          785..790
                     /region_name="Repetitive region"
                     /note="1-3."
     Region          791..796
                     /region_name="Repetitive region"
                     /note="1-4."
     Region          792..808
                     /region_name="Compositionally biased region"
                     /note="Pro residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          797..802
                     /region_name="Repetitive region"
                     /note="1-5."
     Region          803..808
                     /region_name="Repetitive region"
                     /note="1-6."
     Region          809..814
                     /region_name="Repetitive region"
                     /note="1-7; approximate."
     Region          815..820
                     /region_name="Repetitive region"
                     /note="1-8; approximate."
     Region          821..826
                     /region_name="Repetitive region"
                     /note="1-9."
     Region          827..832
                     /region_name="Repetitive region"
                     /note="1-10; approximate."
     Region          833..838
                     /region_name="Repetitive region"
                     /note="1-11."
     Region          839..844
                     /region_name="Repetitive region"
                     /note="1-12."
     Region          848
                     /region_name="Conflict"
                     /note="V -> E (in Ref. 1; AAA62824).
                     /evidence=ECO:0000305."
     Region          852..1612
                     /region_name="Region of interest in the sequence"
                     /note="CS-1."
     Region          864
                     /region_name="Variant"
                     /note="P -> L (in dbSNP:rs3743398).
                     /evidence=ECO:0000269|PubMed:15489334. /id=VAR_080159."
     Region          898..913
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          913
                     /region_name="Variant"
                     /note="P -> T (in dbSNP:rs35430524).
                     /evidence=ECO:0000269|PubMed:1985970. /id=VAR_080160."
     Region          930
                     /region_name="Variant"
                     /note="S -> I (in dbSNP:rs938608).
                     /evidence=ECO:0000269|PubMed:15489334. /id=VAR_080161."
     Region          939
                     /region_name="Variant"
                     /note="S -> T (in dbSNP:rs938609).
                     /evidence=ECO:0000269|PubMed:15489334. /id=VAR_080162."
     Region          942..1612
                     /region_name="Region of interest in the sequence"
                     /note="35 X 19 AA approximate tandem repeats of
                     E-[IVDG]-[LV]-[EV]-[GTI]-[STA]-[ATV]-[SP]-[GA]-[VIFAD]-
                     [GEDL]-[DE]-[LVI]-[SG]-[GERK]-[LV]-P-S-G."
     Region          942..960
                     /region_name="Repetitive region"
                     /note="2-1."
     Region          961..979
                     /region_name="Repetitive region"
                     /note="2-2."
     Region          980..998
                     /region_name="Repetitive region"
                     /note="2-3."
     Region          999..1017
                     /region_name="Repetitive region"
                     /note="2-4."
     Region          999..1017
                     /region_name="Conflict"
                     /note="Missing (in Ref. 3; AAI50625).
                     /evidence=ECO:0000305."
     Region          1018..1036
                     /region_name="Repetitive region"
                     /note="2-5."
     Region          1037..1055
                     /region_name="Repetitive region"
                     /note="2-6."
     Region          1056..1074
                     /region_name="Repetitive region"
                     /note="2-7."
     Region          1075..1188
                     /region_name="Conflict"
                     /note="Missing (in Ref. 1; AAA62824).
                     /evidence=ECO:0000305."
     Region          1075..1093
                     /region_name="Repetitive region"
                     /note="2-8."
     Region          1080
                     /region_name="Variant"
                     /note="T -> A (in dbSNP:rs373544100).
                     /evidence=ECO:0000269|PubMed:15489334. /id=VAR_080163."
     Region          1094..1112
                     /region_name="Repetitive region"
                     /note="2-9."
     Region          1113..1131
                     /region_name="Repetitive region"
                     /note="2-10."
     Region          1132..1150
                     /region_name="Repetitive region"
                     /note="2-11."
     Region          1151..1169
                     /region_name="Repetitive region"
                     /note="2-12."
     Region          1170..1188
                     /region_name="Repetitive region"
                     /note="2-13."
     Region          1189..1207
                     /region_name="Repetitive region"
                     /note="2-14."
     Region          1208..1226
                     /region_name="Repetitive region"
                     /note="2-15."
     Region          1227..1245
                     /region_name="Repetitive region"
                     /note="2-16."
     Region          1246..1264
                     /region_name="Repetitive region"
                     /note="2-17."
     Region          1265..1283
                     /region_name="Repetitive region"
                     /note="2-18."
     Region          1284..1302
                     /region_name="Repetitive region"
                     /note="2-19."
     Region          1303..1321
                     /region_name="Repetitive region"
                     /note="2-20."
     Region          1322..1340
                     /region_name="Repetitive region"
                     /note="2-21."
     Region          1341..1359
                     /region_name="Repetitive region"
                     /note="2-22."
     Region          1360..1378
                     /region_name="Repetitive region"
                     /note="2-23."
     Region          1379..1397
                     /region_name="Repetitive region"
                     /note="2-24."
     Region          1398..1416
                     /region_name="Repetitive region"
                     /note="2-25."
     Region          1403
                     /region_name="Variant"
                     /note="T -> A (in dbSNP:rs12899191).
                     /evidence=ECO:0000269|PubMed:15489334. /id=VAR_080164."
     Region          1417..1435
                     /region_name="Repetitive region"
                     /note="2-26."
     Region          <1433..>1614
                     /region_name="PRK15387"
                     /note="type III secretion system effector E3 ubiquitin
                     transferase SspH2"
                     /db_xref="CDD:185285"
     Region          1436..1454
                     /region_name="Repetitive region"
                     /note="2-27."
     Region          1455..1473
                     /region_name="Repetitive region"
                     /note="2-28."
     Region          1475..1493
                     /region_name="Repetitive region"
                     /note="2-29."
     Region          1494..1512
                     /region_name="Repetitive region"
                     /note="2-30."
     Region          1499..1526
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1508
                     /region_name="Variant"
                     /note="E -> A (in dbSNP:rs2882676).
                     /evidence=ECO:0000269|PubMed:15489334. /id=VAR_080165."
     Region          1513..1531
                     /region_name="Repetitive region"
                     /note="2-31."
     Site            1530
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:36213313."
     Region          1533..1551
                     /region_name="Repetitive region"
                     /note="2-32."
     Region          1543..1649
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1548
                     /region_name="Conflict"
                     /note="L -> V (in Ref. 1; AAA62824).
                     /evidence=ECO:0000305."
     Region          1553..1572
                     /region_name="Repetitive region"
                     /note="2-33; approximate."
     Site            1567
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:36213313."
     Region          1574..1592
                     /region_name="Repetitive region"
                     /note="2-34."
     Site            1581
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            1587
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            1591
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Region          1594..1612
                     /region_name="Repetitive region"
                     /note="2-35."
     Site            1601
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:36213313."
     Region          1613..2277
                     /region_name="Region of interest in the sequence"
                     /note="CS-2."
     Region          1615..1629
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1687..1772
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1703
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:36213313."
     Region          1709..1723
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1739..1772
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1765
                     /region_name="Variant"
                     /note="I -> V (in dbSNP:rs4932439).
                     /evidence=ECO:0000269|PubMed:15489334,
                     ECO:0000269|PubMed:1985970. /id=VAR_080166."
     Region          1784..1827
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1812..1827
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1883..1902
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1948..1977
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2013
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2043
                     /region_name="Conflict"
                     /note="E -> A (in Ref. 9; CAA35463).
                     /evidence=ECO:0000305."
     Region          2048..2204
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2048..2077
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2058
                     /region_name="Variant"
                     /note="P -> L (in dbSNP:rs35061438). /id=VAR_056154."
     Region          2079
                     /region_name="Variant"
                     /note="I -> V (in dbSNP:rs1042630).
                     /evidence=ECO:0000269|PubMed:15489334,
                     ECO:0000269|PubMed:2789216, ECO:0000269|PubMed:8611178.
                     /id=VAR_080167."
     Region          2093..2107
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2120
                     /region_name="Variant"
                     /note="S -> R (in dbSNP:rs34153007). /id=VAR_056155."
     Region          2126..2159
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2166..2204
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2185
                     /region_name="Conflict"
                     /note="P -> A (in Ref. 10; AAA35726).
                     /evidence=ECO:0000305."
     Region          2249..2281
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2278..2530
                     /region_name="Region of interest in the sequence"
                     /note="G3."
     Region          2278..2315
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2 and isoform 3).
                     /evidence=ECO:0000303|PubMed:1985970,
                     ECO:0000303|PubMed:8611178. /id=VSP_003074."
     Region          2279..2314
                     /region_name="Domain"
                     /note="EGF-like.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          2283..2313
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Bond            bond(2283,2293)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(2288,2302)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(2304,2313)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2320..2443
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Bond            bond(2320,2331)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2327..2441
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(2338,2370..2373,2402,2412,2420,2422,2428,2431,
                     2433..2435)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Bond            bond(2348,2440)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2373
                     /region_name="Variant"
                     /note="D -> E (in dbSNP:rs3817428).
                     /evidence=ECO:0000269|PubMed:15489334. /id=VAR_080168."
     Site            order(2381,2385,2408,2414..2415)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Region          2381
                     /region_name="Variant"
                     /note="D -> N (in SEMDAG; creates a functional
                     N-glycosylation site; does not adversely affect protein
                     trafficking and secretion; dbSNP:rs121913568).
                     /evidence=ECO:0000269|PubMed:19110214. /id=VAR_063053."
     Site            order(2385,2415)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(2405,2407,2414,2428..2429)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Bond            bond(2416,2432)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2418
                     /region_name="Variant"
                     /note="V -> M (in SSOAOD; dbSNP:rs779794758).
                     /evidence=ECO:0000269|PubMed:20137779. /id=VAR_063765."
     Region          2445..2506
                     /region_name="Splicing variant"
                     /note="VACGEPPVVEHARTFGQKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGH
                     WEEPQITCTDP -> A (in isoform 3).
                     /evidence=ECO:0000303|PubMed:1985970. /id=VSP_003075."
     Region          2445..2505
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          2447..2503
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(2447,2490)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(2457,2477)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(2476,2503)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2500
                     /region_name="Variant"
                     /note="Q -> R (in dbSNP:rs1126823).
                     /evidence=ECO:0000269|PubMed:2789216,
                     ECO:0000269|PubMed:8611178. /id=VAR_080169."
     Region          2510..2530
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2513..2530
                     /region_name="Compositionally biased region"
                     /note="Basic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
        1 mttllwvfvt lrvitaavtv etsdhdnsls vsipqpsplr vllgtsltip cyfidpmhpv
       61 ttapstapla prikwsrvsk ekevvllvat egrvrvnsay qdkvslpnyp aipsdatlev
      121 qslrsndsgv yrcevmhgie dseatlevvv kgivfhyrai strytldfdr aqraclqnsa
      181 iiatpeqlqa ayedgfhqcd agwladqtvr ypihtpregc ygdkdefpgv rtygirdtne
      241 tydvycfaee megevfyats pekftfqeaa necrrlgarl attgqlylaw qagmdmcsag
      301 wladrsvryp iskarpncgg nllgvrtvyv hanqtgypdp ssrydaicyt gedfvdipen
      361 ffgvggeedi tvqtvtwpdm elplprnite geargsvilt vkpifevsps plepeepftf
      421 apeigatafa evenetgeat rpwgfptpgl gpataftsed lvvqvtavpg qphlpggvvf
      481 hyrpgptrys ltfeeaqqac lrtgaviasp eqlqaayeag yeqcdagwlr dqtvrypivs
      541 prtpcvgdkd sspgvrtygv rpstetydvy cfvdrlegev ffatrleqft fqealefces
      601 hnatlattgq lyaawsrgld kcyagwladg slrypivtpr pacggdkpgv rtvylypnqt
      661 glpdplsrhh afcfrgisav pspgeeeggt ptspsgveew ivtqvvpgva avpveeetta
      721 vpsgettail efttepenqt ewepaytpvg tsplpgilpt wpptgaatee stegpsatev
      781 psaseepsps evpfpseeps pseepfpsvr pfpsvelfps eepfpskeps pseepsasee
      841 pytpsppvps wtelpssgee sgapdvsgdf tgsgdvsghl dfsgqlsgdr asglpsgdld
      901 ssgltstvgs glpvesglps gdeeriewps tptvgelpsg aeilegsasg vgdlsglpsg
      961 evletsasgv gdlsglpsge vlettapgve disglpsgev lettapgved isglpsgevl
     1021 ettapgvedi sglpsgevle ttapgvedis glpsgevlet tapgvedisg lpsgevlett
     1081 apgvedisgl psgevletaa pgvedisglp sgevletaap gvedisglps gevletaapg
     1141 vedisglpsg evletaapgv edisglpsge vletaapgve disglpsgev letaapgved
     1201 isglpsgevl etaapgvedi sglpsgevle taapgvedis glpsgevlet aapgvedisg
     1261 lpsgevleta apgvedisgl psgevletaa pgvedisglp sgevletaap gvedisglps
     1321 gevletaapg vedisglpsg evletaapgv edisglpsge vletaapgve disglpsgev
     1381 letaapgved isglpsgevl ettapgveei sglpsgevle ttapgvdeis glpsgevlet
     1441 tapgveeisg lpsgevlets tsavgdlsgl psggevleis vsgvedisgl psgevvetsa
     1501 sgiedvselp sgegletsas gvedlsrlps geevleisas gfgdlsglps ggegletsas
     1561 evgtdlsglp sgregletsa sgaedlsglp sgkedlvgsa sgdldlgklp sgtlgsgqap
     1621 etsglpsgfs geysgvdlgs gppsglpdfs glpsgfptvs lvdstlvevv tastaseleg
     1681 rgtigisgag eisglpssel disgrasglp sgtelsgqas gspdvsgeip glfgvsgqps
     1741 gfpdtsgets gvtelsglss gqpgisgeas gvlygtsqpf gitdlsgets gvpdlsgqps
     1801 glpgfsgats gvpdlvsgtt sgsgessgit fvdtslveva pttfkeeegl gsvelsglps
     1861 geadlsgksg mvdvsgqfsg tvdssgftsq tpefsglpsg iaevsgessr aeigsslpsg
     1921 ayygsgtpss fptvslvdrt lvesvtqapt aqeagegpsg ilelsgahsg apdmsgehsg
     1981 fldlsglqsg liepsgeppg tpyfsgdfas ttnvsgessv amgtsgeasg lpevtlitse
     2041 fvegvtepti sqelgqrppv thtpqlfess gkvstagdis gatpvlpgsg vevssvpess
     2101 setsaypeag fgasaapeas redsgspdls ettsafhean lerssglgvs gstltfqege
     2161 asaapevsge stttsdvgte apglpsatpt asgdrteisg dlsghtsqlg vvistsipes
     2221 ewtqqtqrpa ethleiesss llysgeetht vetatsptda sipaspewkr esestaaapa
     2281 rscaeepcga gtcketeghv iclcppgytg ehcnidqevc eegwnkyqgh cyrhfpdret
     2341 wvdaerrcre qqshlssivt peeqefvnnn aqdyqwigln drtiegdfrw sdghpmqfen
     2401 wrpnqpdnff aagedcvvmi whekgewndv pcnyhlpftc kkgtvacgep pvvehartfg
     2461 qkkdryeins lvryqctegf vqrhmptirc qpsghweepq itctdpttyk rrlqkrssrh
     2521 prrsrpstah
//
LOCUS       CLC4K_HUMAN              328 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 4 member K; AltName:
            Full=Langerin; AltName: CD_antigen=CD207.
ACCESSION   Q9UJ71
VERSION     Q9UJ71.2
DBSOURCE    UniProtKB: locus CLC4K_HUMAN, accession Q9UJ71;
            class: standard.
            created: Feb 21, 2006.
            sequence updated: Mar 24, 2009.
            annotation updated: Sep 13, 2023.
            xrefs: AJ242859.1, CAB62403.1, AC007395.4, BC022278.1, AAH22278.1,
            NP_056532.4, XP_011531176.1, 3C22_A, 3C22_B, 3C22_C, 3C22_D,
            3KQG_A, 3KQG_B, 3KQG_C, 3KQG_D, 3KQG_E, 3KQG_F, 3P5D_A, 3P5D_B,
            3P5D_C, 3P5D_D, 3P5E_A, 3P5E_B, 3P5E_C, 3P5E_D, 3P5F_A, 3P5F_B,
            3P5F_C, 3P5F_D, 3P5G_A, 3P5G_B, 3P5G_C, 3P5G_D, 3P5H_A, 3P5H_B,
            3P5H_C, 3P5H_D, 3P5I_A, 3P5I_B, 3P5I_C, 3P5I_D, 3P7F_A, 3P7F_B,
            3P7F_C, 3P7F_D, 3P7G_A, 3P7G_B, 3P7G_C, 3P7G_D, 3P7H_A, 3P7H_B,
            3P7H_C, 3P7H_D, 4AK8_A, 4AK8_B, 4AK8_C, 4AK8_D, 4N32_A, 4N32_B,
            4N32_C, 4N32_D, 4N33_A, 4N33_B, 4N33_C, 4N33_D, 4N34_A, 4N34_B,
            4N34_C, 4N34_D, 4N35_A, 4N35_B, 4N35_C, 4N35_D, 4N36_A, 4N36_B,
            4N36_C, 4N36_D, 4N37_A, 4N37_B, 4N37_C, 4N37_D, 4N38_A, 4N38_B,
            4N38_C, 4N38_D, 5G6U_A, 5G6U_B, 5G6U_C, 5G6U_D, 7WZ8_A, 7WZ8_B,
            7WZ8_C, 7WZ8_D, 7WZ8_E, 7WZ8_F, 7YTQ_A, 7YTQ_B, 7YTQ_C, 7YTQ_D
            xrefs (non-sequence databases): CCDS:CCDS74520.1, PDBsum:3C22,
            PDBsum:3KQG, PDBsum:3P5D, PDBsum:3P5E, PDBsum:3P5F, PDBsum:3P5G,
            PDBsum:3P5H, PDBsum:3P5I, PDBsum:3P7F, PDBsum:3P7G, PDBsum:3P7H,
            PDBsum:4AK8, PDBsum:4N32, PDBsum:4N33, PDBsum:4N34, PDBsum:4N35,
            PDBsum:4N36, PDBsum:4N37, PDBsum:4N38, PDBsum:5G6U, PDBsum:7WZ8,
            PDBsum:7YTQ, AlphaFoldDB:Q9UJ71, SMR:Q9UJ71, BioGRID:119076,
            IntAct:Q9UJ71, STRING:9606.ENSP00000386378, BindingDB:Q9UJ71,
            ChEMBL:CHEMBL2176853, UniLectin:Q9UJ71, GlyCosmos:Q9UJ71,
            GlyGen:Q9UJ71, iPTMnet:Q9UJ71, PhosphoSitePlus:Q9UJ71,
            BioMuta:CD207, DMDM:229784129, jPOST:Q9UJ71, MassIVE:Q9UJ71,
            PaxDb:Q9UJ71, PeptideAtlas:Q9UJ71, ProteomicsDB:84594,
            Antibodypedia:2366, DNASU:50489, Ensembl:ENST00000410009.5,
            Ensembl:ENSP00000386378.3, Ensembl:ENSG00000116031.9, GeneID:50489,
            KEGG:hsa:50489, MANE-Select:ENST00000410009.5, UCSC:uc002shg.4,
            AGR:HGNC:17935, CTD:50489, DisGeNET:50489, GeneCards:CD207,
            HGNC:17935, HPA:ENSG00000116031, MalaCards:CD207, MIM:604862,
            MIM:613393, neXtProt:NX_Q9UJ71, OpenTargets:ENSG00000116031,
            PharmGKB:PA134986203, VEuPathDB:HostDB:ENSG00000116031,
            eggNOG:KOG4297, GeneTree:ENSGT00940000161863,
            HOGENOM:CLU_081746_0_0_1, InParanoid:Q9UJ71, OMA:QFCVSRN,
            OrthoDB:5257739at2759, PhylomeDB:Q9UJ71, TreeFam:TF333341,
            PathwayCommons:Q9UJ71, Reactome:R-HSA-1236978, SignaLink:Q9UJ71,
            BioGRID-ORCS:50489, EvolutionaryTrace:Q9UJ71, GeneWiki:Langerin,
            GenomeRNAi:50489, Pharos:Q9UJ71, PRO:PR:Q9UJ71,
            Proteomes:UP000005640, RNAct:Q9UJ71, Bgee:ENSG00000116031,
            Genevisible:Q9UJ71, GO:0030669, GO:0031901, GO:0030139, GO:0009897,
            GO:0005886, GO:0030246, GO:0005537, GO:0051607, CDD:cd03590,
            Gene3D:1.20.5.170, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033989,
            InterPro:IPR016187, PANTHER:PTHR22801, PANTHER:PTHR22801:SF61,
            Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    3D-structure; Coiled coil; Disulfide bond; Glycoprotein; Lectin;
            Membrane; Reference proteome; Signal-anchor; Transmembrane;
            Transmembrane helix.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Valladeau,J., Ravel,O., Dezutter-Dambuyant,C., Moore,K.,
            Kleijmeer,M., Liu,Y., Duvert-Frances,V., Vincent,C., Schmitt,D.,
            Davoust,J., Caux,C., Lebecque,S. and Saeland,S.
  TITLE     Langerin, a novel C-type lectin specific to Langerhans cells, is an
            endocytic receptor that induces the formation of Birbeck granules
  JOURNAL   Immunity 12 (1), 71-81 (2000)
   PUBMED   10661407
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
            SPECIFICITY, AND VARIANT ALA-278.
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Hillier,L.W., Graves,T.A., Fulton,R.S., Fulton,L.A., Pepin,K.H.,
            Minx,P., Wagner-McPherson,C., Layman,D., Wylie,K., Sekhon,M.,
            Becker,M.C., Fewell,G.A., Delehaunty,K.D., Miner,T.L., Nash,W.E.,
            Kremitzki,C., Oddy,L., Du,H., Sun,H., Bradshaw-Cordum,H., Ali,J.,
            Carter,J., Cordes,M., Harris,A., Isak,A., van Brunt,A., Nguyen,C.,
            Du,F., Courtney,L., Kalicki,J., Ozersky,P., Abbott,S.,
            Armstrong,J., Belter,E.A., Caruso,L., Cedroni,M., Cotton,M.,
            Davidson,T., Desai,A., Elliott,G., Erb,T., Fronick,C., Gaige,T.,
            Haakenson,W., Haglund,K., Holmes,A., Harkins,R., Kim,K.,
            Kruchowski,S.S., Strong,C.M., Grewal,N., Goyea,E., Hou,S., Levy,A.,
            Martinka,S., Mead,K., McLellan,M.D., Meyer,R., Randall-Maher,J.,
            Tomlinson,C., Dauphin-Kohlberg,S., Kozlowicz-Reilly,A., Shah,N.,
            Swearengen-Shahid,S., Snider,J., Strong,J.T., Thompson,J.,
            Yoakum,M., Leonard,S., Pearman,C., Trani,L., Radionenko,M.,
            Waligorski,J.E., Wang,C., Rock,S.M., Tin-Wollam,A.M., Maupin,R.,
            Latreille,P., Wendl,M.C., Yang,S.P., Pohl,C., Wallis,J.W.,
            Spieth,J., Bieri,T.A., Berkowicz,N., Nelson,J.O., Osborne,J.,
            Ding,L., Meyer,R., Sabo,A., Shotland,Y., Sinha,P., Wohldmann,P.E.,
            Cook,L.L., Hickenbotham,M.T., Eldred,J., Williams,D., Jones,T.A.,
            She,X., Ciccarelli,F.D., Izaurralde,E., Taylor,J., Schmutz,J.,
            Myers,R.M., Cox,D.R., Huang,X., McPherson,J.D., Mardis,E.R.,
            Clifton,S.W., Warren,W.C., Chinwalla,A.T., Eddy,S.R., Marra,M.A.,
            Ovcharenko,I., Furey,T.S., Miller,W., Eichler,E.E., Bork,P.,
            Suyama,M., Torrents,D., Waterston,R.H. and Wilson,R.K.
  TITLE     Generation and annotation of the DNA sequences of human chromosomes
            2 and 4
  JOURNAL   Nature 434 (7034), 724-731 (2005)
   PUBMED   15815621
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Lung
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Stambach,N.S. and Taylor,M.E.
  TITLE     Characterization of carbohydrate recognition by langerin, a C-type
            lectin of Langerhans cells
  JOURNAL   Glycobiology 13 (5), 401-410 (2003)
   PUBMED   12626394
  REMARK    SUBUNIT.
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Valladeau,J., Dezutter-Dambuyant,C. and Saeland,S.
  TITLE     Langerin/CD207 sheds light on formation of birbeck granules and
            their possible function in Langerhans cells
  JOURNAL   Immunol Res 28 (2), 93-107 (2003)
   PUBMED   14610287
  REMARK    REVIEW.
REFERENCE   6  (residues 1 to 328)
  AUTHORS   de Witte,L., Nabatov,A., Pion,M., Fluitsma,D., de Jong,M.A., de
            Gruijl,T., Piguet,V., van Kooyk,Y. and Geijtenbeek,T.B.
  TITLE     Langerin is a natural barrier to HIV-1 transmission by Langerhans
            cells
  JOURNAL   Nat Med 13 (3), 367-371 (2007)
   PUBMED   17334373
  REMARK    FUNCTION.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Mayya,V., Lundgren,D.H., Hwang,S.I., Rezaul,K., Wu,L., Eng,J.K.,
            Rodionov,V. and Han,D.K.
  TITLE     Quantitative phosphoproteomic analysis of T cell receptor signaling
            reveals system-wide modulation of protein-protein interactions
  JOURNAL   Sci Signal 2 (84), ra46 (2009)
   PUBMED   19690332
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Leukemic T-cell
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Tateno,H., Ohnishi,K., Yabe,R., Hayatsu,N., Sato,T., Takeya,M.,
            Narimatsu,H. and Hirabayashi,J.
  TITLE     Dual specificity of Langerin to sulfated and mannosylated glycans
            via a single C-type carbohydrate recognition domain
  JOURNAL   J Biol Chem 285 (9), 6390-6400 (2010)
   PUBMED   20026605
  REMARK    FUNCTION, TISSUE SPECIFICITY, DOMAIN C-TYPE LECTIN, AND MUTAGENESIS
            OF GLU-285; ASN-287; LYS-299 AND LYS-313.
REFERENCE   9  (residues 1 to 328)
  AUTHORS   de Jong,M.A., Vriend,L.E., Theelen,B., Taylor,M.E., Fluitsma,D.,
            Boekhout,T. and Geijtenbeek,T.B.
  TITLE     C-type lectin Langerin is a beta-glucan receptor on human
            Langerhans cells that recognizes opportunistic and pathogenic fungi
  JOURNAL   Mol Immunol 47 (6), 1216-1225 (2010)
   PUBMED   20097424
  REMARK    FUNCTION.
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Thepaut,M., Valladeau,J., Nurisso,A., Kahn,R., Arnou,B., Vives,C.,
            Saeland,S., Ebel,C., Monnier,C., Dezutter-Dambuyant,C., Imberty,A.
            and Fieschi,F.
  TITLE     Structural studies of langerin and Birbeck granule: a
            macromolecular organization model
  JOURNAL   Biochemistry 48 (12), 2684-2698 (2009)
   PUBMED   19175323
  REMARK    X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 188-328, AND DISULFIDE
            BONDS.
REFERENCE   11 (residues 1 to 328)
  AUTHORS   Verdijk,P., Dijkman,R., Plasmeijer,E.I., Mulder,A.A., Zoutman,W.H.,
            Mieke Mommaas,A. and Tensen,C.P.
  TITLE     A lack of Birbeck granules in Langerhans cells is associated with a
            naturally occurring point mutation in the human Langerin gene
  JOURNAL   J Invest Dermatol 124 (4), 714-717 (2005)
   PUBMED   15816828
  REMARK    VARIANT BIRGD ARG-264.
REFERENCE   12 (residues 1 to 328)
  AUTHORS   Ward,E.M., Stambach,N.S., Drickamer,K. and Taylor,M.E.
  TITLE     Polymorphisms in human langerin affect stability and sugar binding
            activity
  JOURNAL   J Biol Chem 281 (22), 15450-15456 (2006)
   PUBMED   16567809
  REMARK    VARIANTS ALA-278; ASP-288 AND PRO-300, CHARACTERIZATION OF VARIANT
            BIRGD ARG-264, AND CHARACTERIZATION OF VARIANTS ALA-278; ASP-288
            AND PRO-300.
COMMENT     On May 8, 2009 this sequence version replaced Q9UJ71.1.
            [FUNCTION] Calcium-dependent lectin displaying mannose-binding
            specificity. Induces the formation of Birbeck granules (BGs); is a
            potent regulator of membrane superimposition and zippering. Binds
            to sulfated as well as mannosylated glycans, keratan sulfate (KS)
            and beta-glucans. Facilitates uptake of antigens and is involved in
            the routing and/or processing of antigen for presentation to T
            cells. Major receptor on primary Langerhans cells for Candida
            species, Saccharomyces species, and Malassezia furfur. Protects
            against human immunodeficiency virus-1 (HIV-1) infection. Binds to
            high-mannose structures present on the envelope glycoprotein which
            is followed by subsequent targeting of the virus to the Birbeck
            granules leading to its rapid degradation.
            {ECO:0000269|PubMed:10661407, ECO:0000269|PubMed:17334373,
            ECO:0000269|PubMed:20026605, ECO:0000269|PubMed:20097424}.
            [SUBUNIT] Homotrimer. {ECO:0000269|PubMed:12626394}.
            [INTERACTION] Q9UJ71; O43889-2: CREB3; NbExp=3; IntAct=EBI-2873235,
            EBI-625022; Q9UJ71; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2873235,
            EBI-781551; Q9UJ71; Q96HH9: GRAMD2B; NbExp=6; IntAct=EBI-2873235,
            EBI-2832937; Q9UJ71; O00767: SCD; NbExp=3; IntAct=EBI-2873235,
            EBI-2684237; Q9UJ71; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2873235,
            EBI-8652744; Q9UJ71; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-2873235,
            EBI-748373.
            [SUBCELLULAR LOCATION] Membrane {ECO:0000269|PubMed:10661407};
            Single-pass type II membrane protein {ECO:0000269|PubMed:10661407}.
            Note=Found in Birbeck granules (BGs), which are organelles
            consisting of superimposed and zippered membranes.
            [TISSUE SPECIFICITY] Exclusively expressed by Langerhans cells.
            Expressed in astrocytoma and malignant ependymoma, but not in
            normal brain tissues. {ECO:0000269|PubMed:10661407,
            ECO:0000269|PubMed:20026605}.
            [DOMAIN] The C-type lectin domain mediates dual recognition of both
            sulfated and mannosylated glycans. {ECO:0000269|PubMed:20026605}.
            [DISEASE] Birbeck granule deficiency (BIRGD) [MIM:613393]: A
            condition characterized by the absence of Birbeck granules in
            epidermal Langerhans cells. Despite the lack of Birbeck granules,
            Langerhans cells are present in normal numbers and have normal
            morphologic characteristics and antigen-presenting capacity.
            {ECO:0000269|PubMed:15816828, ECO:0000269|PubMed:16567809}.
            Note=The disease is caused by variants affecting the gene
            represented in this entry.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Langerin;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_hum_Ctlect_00126'.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..328
                     /gene="CD207"
                     /gene_synonym="CLEC4K"
     Protein         1..328
                     /product="C-type lectin domain family 4 member K"
                     /note="Langerin"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..328
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 4 member K.
                     /id=PRO_0000223693."
     Region          1..43
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          44..64
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          55
                     /region_name="Variant"
                     /note="A -> V (in dbSNP:rs10489990). /id=VAR_054781."
     Region          65..328
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          <71..183
                     /region_name="PRK01156"
                     /note="chromosome segregation protein; Provisional"
                     /db_xref="CDD:100796"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          136
                     /region_name="Variant"
                     /note="Q -> E (in dbSNP:rs17718987). /id=VAR_056151."
     Region          145..190
                     /region_name="Coiled-coil region"
                     /note="/evidence=ECO:0000255."
     Region          160..195
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:3KQG."
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          196..321
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Region          196..198
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:3KQG."
     Region          200..202
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Region          202..320
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          205..209
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Region          213
                     /region_name="Variant"
                     /note="P -> S (in dbSNP:rs17006436). /id=VAR_054782."
     Region          216..225
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Bond            bond(223,319)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:19175323."
     Region          236..246
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Site            order(250,285,287,293,299..300,307..310)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Region          251..258
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Site            order(257,261,288,293..294)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Region          259..262
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Site            order(261,294)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Region          263..266
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Region          264
                     /region_name="Variant"
                     /note="W -> R (in BIRGD; abolishes mannose-binding
                     ability; dbSNP:rs200837270).
                     /evidence=ECO:0000269|PubMed:15816828,
                     ECO:0000269|PubMed:16567809. /id=VAR_063828."
     Region          274..277
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Region          278..280
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Region          278
                     /region_name="Variant"
                     /note="V -> A (no effect on mannose-binding ability;
                     dbSNP:rs741326). /evidence=ECO:0000269|PubMed:10661407,
                     ECO:0000269|PubMed:16567809. /id=VAR_054783."
     Site            285
                     /site_type="mutagenized"
                     /note="E->A: Loss of binding to 6'-sulfo-LacNAc and
                     invertase. /evidence=ECO:0000269|PubMed:20026605."
     Site            287
                     /site_type="mutagenized"
                     /note="N->A: Loss of binding to 6'-sulfo-LacNAc and
                     invertase. /evidence=ECO:0000269|PubMed:20026605."
     Region          288
                     /region_name="Variant"
                     /note="N -> D (significant reduction in mannose-binding
                     ability; dbSNP:rs13383830).
                     /evidence=ECO:0000269|PubMed:16567809. /id=VAR_054784."
     Region          289..291
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Bond            bond(295,311)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:19175323."
     Region          295..298
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Site            299
                     /site_type="mutagenized"
                     /note="K->A: Loss of binding to 6'-sulfo-LacNAc.
                     /evidence=ECO:0000269|PubMed:20026605."
     Region          300..304
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Region          300
                     /region_name="Variant"
                     /note="A -> P (significant reduction in mannose-binding
                     ability; significant decrease in thermal stability;
                     increased sensitivity of sugar binding to pH change;
                     dbSNP:rs2080391). /evidence=ECO:0000269|PubMed:16567809.
                     /id=VAR_059448."
     Region          306..309
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
     Site            313
                     /site_type="mutagenized"
                     /note="K->A: Loss of binding to 6'-sulfo-LacNAc and
                     6-sulfo-GlcNAc. /evidence=ECO:0000269|PubMed:20026605."
     Region          315..322
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:4AK8."
ORIGIN
        1 mtvekeapda hftvdkqnis lwprepppks gpslvpgktp tvraaliclt lvlvasvllq
       61 avlyprfmgt isdvktnvql lkgrvdnist ldseikknsd gmeaagvqiq mvneslgyvr
      121 sqflklktsv ekanaqiqil trsweevstl naqipelksd lekasalntk iralqgslen
      181 mskllkrqnd ilqvvsqgwk yfkgnfyyfs lipktwysae qfcvsrnshl tsvtseseqe
      241 flyktaggli ywigltkagm egdwswvddt pfnkvqsvrf wipgepnnag nnehcgnika
      301 pslqawndap cdktflfick rpyvpsep
//
LOCUS       FCER2_MOUSE              331 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Low affinity immunoglobulin epsilon Fc receptor;
            AltName: Full=Fc-epsilon-RII; AltName: Full=Lymphocyte IgE
            receptor; AltName: CD_antigen=CD23.
ACCESSION   P20693
VERSION     P20693.1
DBSOURCE    UniProtKB: locus FCER2_MOUSE, accession P20693;
            class: standard.
            extra accessions:Q61556,Q61557
            created: Feb 1, 1991.
            sequence updated: Feb 1, 1991.
            annotation updated: Sep 13, 2023.
            xrefs: M99371.1, AAA74898.1, M34163.1, AAA37603.1, X64223.1,
            CAA45532.1, X64224.1, CAA45533.1, LNMSER, NP_001240666.1,
            NP_001240668.1, NP_001240672.1, NP_001240674.1, NP_001240675.1,
            NP_001240676.1, NP_038545.1
            xrefs (non-sequence databases): CCDS:CCDS22071.1, CCDS:CCDS85491.1,
            CCDS:CCDS85494.1, AlphaFoldDB:P20693, SMR:P20693,
            STRING:10090.ENSMUSP00000005678, GlyCosmos:P20693, GlyGen:P20693,
            iPTMnet:P20693, PhosphoSitePlus:P20693, EPD:P20693, PaxDb:P20693,
            ProteomicsDB:271728, ProteomicsDB:271730, Antibodypedia:2294,
            DNASU:14128, Ensembl:ENSMUST00000005678,
            Ensembl:ENSMUSP00000005678, Ensembl:ENSMUSG00000005540,
            Ensembl:ENSMUST00000208145, Ensembl:ENSMUSP00000146647,
            Ensembl:ENSMUST00000208492, Ensembl:ENSMUSP00000146568,
            GeneID:14128, KEGG:mmu:14128, UCSC:uc009ksl.1, UCSC:uc009ksm.1,
            UCSC:uc009ksn.1, AGR:MGI:95497, CTD:14128, MGI:95497,
            VEuPathDB:HostDB:ENSMUSG00000005540, eggNOG:KOG4297,
            GeneTree:ENSGT00940000162574, HOGENOM:CLU_049894_7_2_1,
            InParanoid:P20693, OMA:PRKRCCG, OrthoDB:4735139at2759,
            PhylomeDB:P20693, TreeFam:TF333341, BioGRID-ORCS:14128,
            PRO:PR:P20693, Proteomes:UP000000589, RNAct:P20693,
            Bgee:ENSMUSG00000005540, ExpressionAtlas:P20693,
            Genevisible:P20693, GO:0009897, GO:0005886, GO:0030246, GO:0019863,
            GO:0019769, GO:0046872, GO:0002450, GO:0160006, GO:0006955,
            GO:0042116, GO:0002925, GO:0051712, GO:0051000, GO:0051770,
            CDD:cd03590, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033989,
            InterPro:IPR016187, PANTHER:PTHR22801, PANTHER:PTHR22801:SF61,
            Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    Alternative splicing; Calcium; Cell membrane; Disulfide bond;
            Glycoprotein; IgE-binding protein; Lectin; Lipoprotein; Membrane;
            Metal-binding; Palmitate; Receptor; Reference proteome; Repeat;
            Signal-anchor; Transmembrane; Transmembrane helix.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Bettler,B., Hofstetter,H., Rao,M., Yokoyama,W.M., Kilchherr,F. and
            Conrad,D.H.
  TITLE     Molecular structure and expression of the murine lymphocyte
            low-affinity receptor for IgE (Fc epsilon RII)
  JOURNAL   Proc Natl Acad Sci U S A 86 (19), 7566-7570 (1989)
   PUBMED   2529542
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Gollnick,S.O., Trounstine,M.L., Yamashita,L.C., Kehry,M.R. and
            Moore,K.W.
  TITLE     Isolation, characterization, and expression of cDNA clones encoding
            the mouse Fc receptor for IgE (Fc epsilon RII)1
  JOURNAL   J Immunol 144 (5), 1974-1982 (1990)
   PUBMED   2137845
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Kondo,H., Ichikawa,Y., Nakamura,K. and Tsuchiya,S.
  TITLE     Cloning of cDNAs for new subtypes of murine low-affinity Fc
            receptor for IgE (Fc epsilon RII/CD23)
  JOURNAL   Int Arch Allergy Immunol 105 (1), 38-48 (1994)
   PUBMED   8086828
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).;
            STRAIN=DBA/2J
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Spleen
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Padlan,E.A. and Helm,B.A.
  TITLE     Modeling of the lectin-homology domains of the human and murine
            low-affinity Fc epsilon receptor (Fc epsilon RII/CD23)
  JOURNAL   Receptor 3 (4), 325-341 (1993)
   PUBMED   8142907
  REMARK    3D-STRUCTURE MODELING OF LECTIN DOMAIN.
COMMENT     On Oct 25, 2005 this sequence version replaced gi:625319.
            [FUNCTION] Low-affinity receptor for immunoglobulin E (IgE) and
            CR2/CD21. Has essential roles in the regulation of IgE production
            and in the differentiation of B cells. On B cells, initiates
            IgE-dependent antigen uptake and presentation to T cells. On
            macrophages, upon IgE binding and antigen cross-linking induces
            intracellular killing of parasites through activation of
            L-Arginine-nitric oxide pathway. {ECO:0000250|UniProtKB:P06734}.
            [SUBUNIT] Homotrimer. Interacts (via C-type lectin domain) with
            IGHE (via CH3 region); this interaction regulates IgE homeostasis.
            Interacts (via C-terminus) with CR2/CD21 (via Sushi domain 1 and
            2). {ECO:0000250|UniProtKB:P06734}.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000250}; Single-pass
            type II membrane protein {ECO:0000250}. Cell membrane
            {ECO:0000250}; Lipid-anchor {ECO:0000250}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=3; Name=1; Synonyms=A; IsoId=P20693-1; Sequence=Displayed;
            Name=2; Synonyms=B; IsoId=P20693-2; Sequence=VSP_003058; Name=3;
            Synonyms=C; IsoId=P20693-3; Sequence=VSP_003059.
            [PTM] N- and O-glycosylated. {ECO:0000250}.
            [MISCELLANEOUS] There are two kinds of Fc receptors for IgE, which
            differ in both structure and function: high affinity receptors on
            basophils and mast cells and low affinity receptors on lymphocytes
            and monocytes.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=CD23;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_222'.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..331
                     /gene="Fcer2"
                     /gene_synonym="Fcer2a"
     Protein         1..331
                     /product="Low affinity immunoglobulin epsilon Fc receptor"
                     /note="Fc-epsilon-RII; Lymphocyte IgE receptor"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..331
                     /region_name="Mature chain"
                     /note="Low affinity immunoglobulin epsilon Fc receptor.
                     /id=PRO_0000046640."
     Region          1..23
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          1..7
                     /region_name="Splicing variant"
                     /note="MEENEYS -> MDTHHT (in isoform 3).
                     /evidence=ECO:0000303|PubMed:8086828. /id=VSP_003059."
     Region          1..7
                     /region_name="Splicing variant"
                     /note="MEENEYS -> MNSQNQ (in isoform 2).
                     /evidence=ECO:0000303|PubMed:8086828. /id=VSP_003058."
     Site            17
                     /site_type="lipid-binding"
                     /note="S-palmitoyl cysteine. /evidence=ECO:0000250."
     Site            18
                     /site_type="lipid-binding"
                     /note="S-palmitoyl cysteine. /evidence=ECO:0000250."
     Region          24..49
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          50..331
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          63..>174
                     /region_name="CCDC158"
                     /note="Coiled-coil domain-containing protein 158;
                     pfam15921"
                     /db_xref="CDD:435022"
     Site            65
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          71..91
                     /region_name="Repetitive region"
     Region          92..112
                     /region_name="Repetitive region"
     Region          113..133
                     /region_name="Repetitive region"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(183,311)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          185..298
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          186..306
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(186,197)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(214,305)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(242,272,274,280,286..287,292..295)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(248,252,275,280..281)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(252,281)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Bond            bond(282,296)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 meeneysgyw epprkrccca rrgtqlmlvg llstamwagl lallllwhwe teknlkqlgd
       61 taiqnvshvt kdlqkfqsnq laqksqvvqm sqnlqelqae qkqmkaqdsr lsqnltglqe
      121 dlrnaqsqns klsqnlnrlq ddlvnikslg lnekrtasds leklqeevak lwieiliskg
      181 tacnicpknw lhfqqkcyyf gkgskqwiqa rfacsdlqgr lvsihsqkeq dflmqhinkk
      241 dswiglqdln megefvwsdg spvgysnwnp gepnnggqge dcvmmrgsgq wndafcrsyl
      301 dawvceqlat ceisaplasv tptrptpkse p
//
LOCUS       CSPG2_MOUSE             3357 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Versican core protein; AltName: Full=Chondroitin
            sulfate proteoglycan core protein 2; Short=Chondroitin sulfate
            proteoglycan 2; AltName: Full=Large fibroblast proteoglycan;
            AltName: Full=PG-M; Flags: Precursor.
ACCESSION   Q62059
VERSION     Q62059.2
DBSOURCE    UniProtKB: locus CSPG2_MOUSE, accession Q62059;
            class: standard.
            extra accessions:Q62058,Q9CUU0
            created: Nov 1, 1997.
            sequence updated: Jun 13, 2006.
            annotation updated: Sep 13, 2023.
            xrefs: D16263.1, BAA03796.1, D28599.1, D32040.1, BAA06802.1,
            AK014525.1, BAB29411.3, A55535
            xrefs (non-sequence databases): SMR:Q62059, IntAct:Q62059,
            MINT:Q62059, STRING:10090.ENSMUSP00000105173, GlyConnect:2818,
            GlyCosmos:Q62059, GlyGen:Q62059, iPTMnet:Q62059,
            PhosphoSitePlus:Q62059, SwissPalm:Q62059, jPOST:Q62059,
            MaxQB:Q62059, PaxDb:Q62059, PeptideAtlas:Q62059,
            ProteomicsDB:284036, ProteomicsDB:284037, ProteomicsDB:284038,
            ProteomicsDB:284039, ABCD:Q62059, AGR:MGI:102889, MGI:102889,
            eggNOG:ENOG502QRBE, InParanoid:Q62059, PhylomeDB:Q62059,
            Reactome:R-MMU-1971475, Reactome:R-MMU-2022870,
            Reactome:R-MMU-2022923, Reactome:R-MMU-2024101,
            Reactome:R-MMU-3000178, Reactome:R-MMU-381426,
            Reactome:R-MMU-8957275, ChiTaRS:Vcan, PRO:PR:Q62059,
            Proteomes:UP000000589, RNAct:Q62059, GO:0009986, GO:0062023,
            GO:0031012, GO:0005576, GO:0005615, GO:0033165, GO:0072534,
            GO:0001750, GO:0045202, GO:0005509, GO:0030246, GO:0005540,
            GO:0019903, GO:0007155, GO:0007417, GO:0010001, GO:0008347,
            GO:0007507, GO:0002052, GO:0043666, GO:0001501, GO:0001657,
            CDD:cd00033, CDD:cd03588, CDD:cd00054, CDD:cd05901, CDD:cd03517,
            CDD:cd03520, Gene3D:2.10.70.10, Gene3D:2.60.40.10,
            Gene3D:2.10.25.10, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033987,
            InterPro:IPR016187, InterPro:IPR001881, InterPro:IPR000742,
            InterPro:IPR000152, InterPro:IPR018097, InterPro:IPR007110,
            InterPro:IPR036179, InterPro:IPR013783, InterPro:IPR003599,
            InterPro:IPR013106, InterPro:IPR000538, InterPro:IPR035976,
            InterPro:IPR000436, PANTHER:PTHR22804, PANTHER:PTHR22804:SF6,
            Pfam:PF00008, Pfam:PF00059, Pfam:PF00084, Pfam:PF07686,
            Pfam:PF00193, PRINTS:PR01265, SMART:SM00032, SMART:SM00034,
            SMART:SM00181, SMART:SM00179, SMART:SM00409, SMART:SM00406,
            SMART:SM00445, SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF57196,
            SUPFAM:SSF48726, PROSITE:PS00010, PROSITE:PS00615, PROSITE:PS50041,
            PROSITE:PS00022, PROSITE:PS01186, PROSITE:PS50026, PROSITE:PS01187,
            PROSITE:PS50835, PROSITE:PS01241, PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Alternative splicing; Calcium; Cell projection; Direct protein
            sequencing; Disulfide bond; EGF-like domain; Extracellular matrix;
            Glycoprotein; Hyaluronic acid; Immunoglobulin domain; Lectin;
            Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted;
            Signal; Sushi.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 3357)
  AUTHORS   Ito,K., Shinomura,T., Zako,M., Ujita,M. and Kimata,K.
  TITLE     Multiple forms of mouse PG-M, a large chondroitin sulfate
            proteoglycan generated by alternative splicing
  JOURNAL   J Biol Chem 270 (2), 958-965 (1995)
   PUBMED   7822336
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0; V1 AND V2), AND TISSUE
            SPECIFICITY.;
            STRAIN=C57BL/6J, and Swiss Webster; TISSUE=Brain, and Endothelial
            cell
REFERENCE   2  (residues 1 to 3357)
  AUTHORS   Zako,M., Shinomura,T., Ujita,M., Ito,K. and Kimata,K.
  TITLE     Expression of PG-M(V3), an alternatively spliced form of PG-M
            without a chondroitin sulfate attachment in region in mouse and
            human tissues
  JOURNAL   J Biol Chem 270 (8), 3914-3918 (1995)
   PUBMED   7876137
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).;
            STRAIN=C57BL/6J; TISSUE=Endothelial cell
REFERENCE   3  (residues 1 to 3357)
  AUTHORS   Carninci,P., Kasukawa,T., Katayama,S., Gough,J., Frith,M.C.,
            Maeda,N., Oyama,R., Ravasi,T., Lenhard,B., Wells,C., Kodzius,R.,
            Shimokawa,K., Bajic,V.B., Brenner,S.E., Batalov,S., Forrest,A.R.,
            Zavolan,M., Davis,M.J., Wilming,L.G., Aidinis,V., Allen,J.E.,
            Ambesi-Impiombato,A., Apweiler,R., Aturaliya,R.N., Bailey,T.L.,
            Bansal,M., Baxter,L., Beisel,K.W., Bersano,T., Bono,H., Chalk,A.M.,
            Chiu,K.P., Choudhary,V., Christoffels,A., Clutterbuck,D.R.,
            Crowe,M.L., Dalla,E., Dalrymple,B.P., de Bono,B., Della Gatta,G.,
            di Bernardo,D., Down,T., Engstrom,P., Fagiolini,M., Faulkner,G.,
            Fletcher,C.F., Fukushima,T., Furuno,M., Futaki,S., Gariboldi,M.,
            Georgii-Hemming,P., Gingeras,T.R., Gojobori,T., Green,R.E.,
            Gustincich,S., Harbers,M., Hayashi,Y., Hensch,T.K., Hirokawa,N.,
            Hill,D., Huminiecki,L., Iacono,M., Ikeo,K., Iwama,A., Ishikawa,T.,
            Jakt,M., Kanapin,A., Katoh,M., Kawasawa,Y., Kelso,J., Kitamura,H.,
            Kitano,H., Kollias,G., Krishnan,S.P., Kruger,A., Kummerfeld,S.K.,
            Kurochkin,I.V., Lareau,L.F., Lazarevic,D., Lipovich,L., Liu,J.,
            Liuni,S., McWilliam,S., Madan Babu,M., Madera,M., Marchionni,L.,
            Matsuda,H., Matsuzawa,S., Miki,H., Mignone,F., Miyake,S.,
            Morris,K., Mottagui-Tabar,S., Mulder,N., Nakano,N., Nakauchi,H.,
            Ng,P., Nilsson,R., Nishiguchi,S., Nishikawa,S., Nori,F., Ohara,O.,
            Okazaki,Y., Orlando,V., Pang,K.C., Pavan,W.J., Pavesi,G.,
            Pesole,G., Petrovsky,N., Piazza,S., Reed,J., Reid,J.F., Ring,B.Z.,
            Ringwald,M., Rost,B., Ruan,Y., Salzberg,S.L., Sandelin,A.,
            Schneider,C., Schonbach,C., Sekiguchi,K., Semple,C.A., Seno,S.,
            Sessa,L., Sheng,Y., Shibata,Y., Shimada,H., Shimada,K., Silva,D.,
            Sinclair,B., Sperling,S., Stupka,E., Sugiura,K., Sultana,R.,
            Takenaka,Y., Taki,K., Tammoja,K., Tan,S.L., Tang,S., Taylor,M.S.,
            Tegner,J., Teichmann,S.A., Ueda,H.R., van Nimwegen,E., Verardo,R.,
            Wei,C.L., Yagi,K., Yamanishi,H., Zabarovsky,E., Zhu,S., Zimmer,A.,
            Hide,W., Bult,C., Grimmond,S.M., Teasdale,R.D., Liu,E.T.,
            Brusic,V., Quackenbush,J., Wahlestedt,C., Mattick,J.S., Hume,D.A.,
            Kai,C., Sasaki,D., Tomaru,Y., Fukuda,S., Kanamori-Katayama,M.,
            Suzuki,M., Aoki,J., Arakawa,T., Iida,J., Imamura,K., Itoh,M.,
            Kato,T., Kawaji,H., Kawagashira,N., Kawashima,T., Kojima,M.,
            Kondo,S., Konno,H., Nakano,K., Ninomiya,N., Nishio,T., Okada,M.,
            Plessy,C., Shibata,K., Shiraki,T., Suzuki,S., Tagami,M., Waki,K.,
            Watahiki,A., Okamura-Oho,Y., Suzuki,H., Kawai,J. and Hayashizaki,Y.
  CONSRTM   FANTOM Consortium; RIKEN Genome Exploration Research Group and
            Genome Science Group (Genome Network Project Core Group)
  TITLE     The transcriptional landscape of the mammalian genome
  JOURNAL   Science 309 (5740), 1559-1563 (2005)
   PUBMED   16141072
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1691 (ISOFORM V1).;
            STRAIN=C57BL/6J; TISSUE=Skin
            Erratum:[Science. 2006 Mar 24;311(5768):1713]
REFERENCE   4  (residues 1 to 3357)
  AUTHORS   Lubec,G., Sunyer,B. and Chen,W.-Q.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-JAN-2009) to UniProtKB
  REMARK    PROTEIN SEQUENCE OF 277-288, AND IDENTIFICATION BY MASS
            SPECTROMETRY.;
            STRAIN=OF1; TISSUE=Hippocampus
REFERENCE   5  (residues 1 to 3357)
  AUTHORS   Aspberg,A., Adam,S., Kostka,G., Timpl,R. and Heinegard,D.
  TITLE     Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
            versican
  JOURNAL   J Biol Chem 274 (29), 20444-20449 (1999)
   PUBMED   10400671
  REMARK    INTERACTION WITH FBLN1.
REFERENCE   6  (residues 1 to 3357)
  AUTHORS   Villen,J., Beausoleil,S.A., Gerber,S.A. and Gygi,S.P.
  TITLE     Large-scale phosphorylation analysis of mouse liver
  JOURNAL   Proc Natl Acad Sci U S A 104 (5), 1488-1493 (2007)
   PUBMED   17242355
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver
REFERENCE   7  (residues 1 to 3357)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2585 AND SER-2586,
            AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen
REFERENCE   8  (residues 1 to 3357)
  AUTHORS   Stupka,N., Kintakas,C., White,J.D., Fraser,F.W., Hanciu,M.,
            Aramaki-Hattori,N., Martin,S., Coles,C., Collier,F., Ward,A.C.,
            Apte,S.S. and McCulloch,D.R.
  TITLE     Versican processing by a disintegrin-like and metalloproteinase
            domain with thrombospondin-1 repeats proteinases-5 and -15
            facilitates myoblast fusion
  JOURNAL   J Biol Chem 288 (3), 1907-1917 (2013)
   PUBMED   23233679
  REMARK    DEVELOPMENTAL STAGE, AND CLEAVAGE BY ADAMTS5.
REFERENCE   9  (residues 1 to 3357)
  AUTHORS   Dancevic,C.M., Fraser,F.W., Smith,A.D., Stupka,N., Ward,A.C. and
            McCulloch,D.R.
  TITLE     Biosynthesis and expression of a disintegrin-like and
            metalloproteinase domain with thrombospondin-1 repeats-15: a novel
            versican-cleaving proteoglycanase
  JOURNAL   J Biol Chem 288 (52), 37267-37276 (2013)
   PUBMED   24220035
  REMARK    CLEAVAGE BY ADAMTS15.
REFERENCE   10 (residues 1 to 3357)
  AUTHORS   Felemban,M., Dorgau,B., Hunt,N.C., Hallam,D., Zerti,D., Bauer,R.,
            Ding,Y., Collin,J., Steel,D., Krasnogor,N., Al-Aama,J., Lindsay,S.,
            Mellough,C. and Lako,M.
  TITLE     Extracellular matrix component expression in human pluripotent stem
            cell-derived retinal organoids recapitulates retinogenesis in vivo
            and reveals an important role for IMPG1 and CD44 in the development
            of photoreceptors and interphotoreceptor matrix
  JOURNAL   Acta Biomater 74, 207-221 (2018)
   PUBMED   29777959
  REMARK    SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
COMMENT     On or before Jul 17, 2007 this sequence version replaced
            gi:2137709, gi:2497660.
            [FUNCTION] May play a role in intercellular signaling and in
            connecting cells with the extracellular matrix. May take part in
            the regulation of cell motility, growth and differentiation. Binds
            hyaluronic acid.
            [SUBUNIT] Interacts with FBLN1. {ECO:0000269|PubMed:10400671}.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000250|UniProtKB:P13611}. Cell projection, cilium,
            photoreceptor outer segment {ECO:0000269|PubMed:29777959}.
            Secreted, extracellular space, extracellular matrix,
            interphotoreceptor matrix {ECO:0000269|PubMed:29777959}. Secreted
            {ECO:0000250|UniProtKB:P13611}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=4; Comment=Additional isoforms seem to exist.; Name=V0;
            IsoId=Q62059-1; Sequence=Displayed; Name=V1; IsoId=Q62059-2;
            Sequence=VSP_003087, VSP_003088; Name=V2; IsoId=Q62059-3;
            Sequence=VSP_003089; Name=V3; IsoId=Q62059-4; Sequence=VSP_003087,
            VSP_003090.
            [TISSUE SPECIFICITY] Expressed in the retina (at protein level)
            (PubMed:29777959). Isoform V2: Only expressed in brain
            (PubMed:7822336). {ECO:0000269|PubMed:29777959,
            ECO:0000269|PubMed:7822336}.
            [DEVELOPMENTAL STAGE] In embryonic skeletal muscle, significantly
            up-regulated from 12.5 dpc to 15.5 dpc (PubMed:23233679). Decreased
            levels in postnatal skeletal muscle (PubMed:23233679). In
            myoblasts, dramatically up-regulated when myoblasts reach
            confluence and contact inhibition, remaining high throughout the
            differentiation process (PubMed:23233679). Disappears after the
            cartilage development. {ECO:0000269|PubMed:23233679}.
            [PTM] Phosphorylated by FAM20C in the extracellular medium.
            {ECO:0000250|UniProtKB:P13611}.
            [PTM] Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the
            pericellular matrix surrounding myoblasts, facilitating myoblast
            contact and fusion which is required for skeletal muscle
            development and regeneration. {ECO:0000269|PubMed:23233679,
            ECO:0000269|PubMed:24220035}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Versican;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_157'.
FEATURES             Location/Qualifiers
     source          1..3357
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..3357
                     /gene="Vcan"
                     /gene_synonym="Cspg2"
     Protein         1..3357
                     /product="Versican core protein"
                     /note="Chondroitin sulfate proteoglycan core protein 2;
                     Large fibroblast proteoglycan; PG-M; Chondroitin sulfate
                     proteoglycan 2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..23
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          24..3357
                     /region_name="Mature chain"
                     /note="Versican core protein. /id=PRO_0000017523."
     Region          24..146
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          26..152
                     /region_name="Ig_Versican"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), versican;
                     cd05901"
                     /db_xref="CDD:409482"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409482"
     Region          32..34
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409482"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409482"
     Bond            bond(44,130)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          63..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409482"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409482"
     Region          101..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409482"
     Region          112..118
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409482"
     Region          126..133
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409482"
     Region          126
                     /region_name="Conflict"
                     /note="A -> G (in Ref. 3). /evidence=ECO:0000305."
     Region          143..152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409482"
     Region          150..245
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          150..244
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            160..161
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(172,243)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(196,217)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          251..347
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          251..346
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            258..259
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(270,333)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(294,315)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          348..1308
                     /region_name="Region of interest in the sequence"
                     /note="GAG-alpha (glucosaminoglycan attachment domain)."
     Region          348
                     /region_name="Splicing variant"
                     /note="P -> R (in isoform V1 and isoform V3).
                     /evidence=ECO:0000303|PubMed:16141072,
                     ECO:0000303|PubMed:7822336, ECO:0000303|PubMed:7876137.
                     /id=VSP_003087."
     Region          349..3051
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V3).
                     /evidence=ECO:0000303|PubMed:7876137. /id=VSP_003090."
     Region          349..1308
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V1).
                     /evidence=ECO:0000303|PubMed:16141072,
                     ECO:0000303|PubMed:7822336. /id=VSP_003088."
     Site            351
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            441
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          625..646
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            660
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          801..863
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          801..816
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            807
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          881..908
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            914
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            951
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1010..1088
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1010..1046
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1252..1288
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1254..1288
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1305
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1309..3051
                     /region_name="Region of interest in the sequence"
                     /note="GAG-beta."
     Region          1309..3051
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V2).
                     /evidence=ECO:0000303|PubMed:7822336. /id=VSP_003089."
     Site            1371
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1396..1421
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1401..1402
                     /site_type="cleavage"
                     /note="Cleavage; by ADAMTS15.
                     /evidence=ECO:0000269|PubMed:24220035."
     Region          1458..1524
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1472..1501
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1517
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            1599
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          1657
                     /region_name="Conflict"
                     /note="I -> T (in Ref. 3). /evidence=ECO:0000305."
     Region          1664..1705
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1669..1685
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1673..1679
                     /region_name="Conflict"
                     /note="TVWNSNS -> QFGIQTA (in Ref. 3).
                     /evidence=ECO:0000305."
     Site            1678
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1686..1705
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1907
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          1926..1965
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1931
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          1940..1954
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2053
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2219
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            2226
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            2243
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2308..2374
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2330..2344
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2351..2374
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2361
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2475..2494
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079."
     Site            2586
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079."
     Site            2626
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2696
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            2697
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            2741
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          2853..2908
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2870..2888
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            3029
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          3051..3087
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          3053..3087
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Bond            bond(3055,3066)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3060,3075)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3077,3086)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3089..3125
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          3089..3125
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(3089,3092,3106)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(3093,3104)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3098,3113)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3115,3124)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3131..3254
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Bond            bond(3131,3142)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3138..3252
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(3149,3181..3184,3213,3223,3231,3233,3239,3242,
                     3244..3246)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Bond            bond(3159,3251)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(3192,3196,3219,3225..3226)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3196,3226)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3216,3218,3225,3239..3240)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Bond            bond(3227,3243)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3256..3316
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          3258..3314
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(3258,3301)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(3268,3288)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(3287,3314)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3331..3357
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            3331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          3340..3357
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            3341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
ORIGIN
        1 mlinmkgilw mcstllltha lhqakmetsp pvkgslsgkv vlpchfstlp tlppnyntse
       61 flrikwskme vdkngkdike ttvlvaqngn ikigqdykgr vsvpthpddv gdasltmvkl
      121 rasdaavyrc dvmygiedtq dtmslavdgv vfhyraatsr ytlnfaaaqq acldigavia
      181 speqlfaaye dgfeqcdagw lsdqtvrypi rapregcygd mmgkegvrty gfrspqetyd
      241 vycyvdhldg dvfhitapsk ftfeeaeaec tsrdarlatv gelqaawrng fdqcdygwls
      301 dasvrhpvtv araqcgggll gvrtlyrfen qtcfplpdsr fdaycfkpkq niseattiem
      361 nilaetssps lskephmvpd ratpviplat elpiftthfp pagnivnseq ksvvysqait
      421 grlatesptt trntinswdl ndslasgsgp lgmpdiseik eeelrsttvi sqhatgsqav
      481 itedtqthes vsqieqievg plvtsmeitn hislkelpek nktpyestev tlehttempt
      541 vsaspelatt shygftlred dredrtltvr sdqstrvfsq ipevitvskt sedttysqlg
      601 dlesiststi tmlgtdrsli dkekepktng kvtedefgqs qptttfpsqh ltevellpys
      661 gdttsvegis tviypslqtd vtqgrertet prpelkkdpy tvdeipekvt kdpfigktee
      721 vfsgmplsts ssessverte svspaltiek ltgkpteard veemttltrl etdvtksdkd
      781 vtrvhlthst lnvevvtvsk wpgdednsts kplpstehag ftklppvpls tigingkdke
      841 ipsftdggge ytlfpdgtpk plekvseedl asgeltvtfh tstsigsaek sasgepttgd
      901 rflpttsted qvinataegs algedteask plftgppfvh tsdveelafv nysstqeptt
      961 yvdishtspl siipktewsv letsvplede ilgksdqdil eqthleatms pgalrttgvs
     1021 qgetqeepqt pgspfptfss tavmaketta feegegstyt psegrlmtgs ervpglettp
     1081 vgtsyppgai tdqevemdtm vtlmstirpt vvsstesevi yeaegsspte fastlrpfqt
     1141 hvtqlmeett eegkkasldy tdlgsglfep ratelpkfps tpsdisvfta idslhrtppl
     1201 spsssfteeq rvfeeessek ttgdilpges vtqhpvttli divamktesd idhmtskppv
     1261 tqptrpsvve rkttsktqel ststpaagtk fhpdinvyii evrenktgrl sdmivsghpi
     1321 dseskeeepc seetdplhdl faeilpelpd sfeidiyhse ededgeedcv natdvtttps
     1381 vqyingkqlv ttvpkdpeaa earrgqyesv apsqnfpdss atdthqfila etessttmqf
     1441 kkskegtell eitwkpetyp etpdhvssge pdvfptlssh dgkttrwses itesspnlen
     1501 pvhkqpkpvp lfpeessgeg aieqasqeti lsratevalg ketdqsptls tssilsssvs
     1561 vnvleeeplt ltgisqtdes mstieswvei tpsqtvkfse sssapiiegs geveenknki
     1621 fnmvtdlpqr dptdtlspld mskimitnhh iyipatiapl dsklpspdar pttvwnsnst
     1681 sewvsdksfe grkkkenede egavnaahqg evraatersd hllltpeles snvdassdla
     1741 twegfilett ptesekeman stpvfretig vanveaqpfe hsssshprvq eelttlsgnp
     1801 pslftdlgsg dastgmelit aslftldles etkvkkelps tpspsveiss sfeptgltps
     1861 tvldieiagv msqtsqktli seisgkptsq sgvrdlytgf pmgedfsgdf seyptvsypt
     1921 mkeetvgmgg sddervrdtq tsssipttsd niypvpdskg pdstvastta fpweevmssa
     1981 egsgeqlasv rssvgpvlpl avdifsgtes pyfdeefeev aavteanerp tvlptaasgn
     2041 tvdltengyi evnstmsldf pqtmepsklw skpevnldkq eigretvtke kaqgqktfes
     2101 lhssfapeqt iletqsliet efqtsdysml ttlktyitnk eveeegmsia hmstpgpgik
     2161 dlesytthpe apgkshsfsa talvtesgaa rsvlmdsstq eeesiklfqk gvkltnkesn
     2221 adlsfsglgs ggalpplptt svnltdmkqi istlyaetsh meslgtsilg dkmedherme
     2281 dvssnevrml iskigsisqd stealdttls htgteeptts tlpfvklmdl erspkqdpsg
     2341 gkrkpkthrp qtmsglisne nssaseaeeg atsptaflpq tysvemtkhf apsesqpsdl
     2401 fnvnsgegsg evdtldlvyt sgttqassqg dsmlashgfl ekhpevskte agatdvspta
     2461 samflhhsey ksslyptstl pstepyksps egiedglqdn iqfegstlkp srrkttesii
     2521 idldkedskd lgltitesai vkslpeltsd kniiididht kpvyeyipgi qtdldpeikl
     2581 eshgsseesl qvqekyegav tlspteesfe gsgdallagy tqaiynesvt pndgkqaedi
     2641 sfsfatgipv sstetelhtf fptastlhip sklttaspei dkpnieaisl ddifesstls
     2701 dgqaiadqse vistlghlek tqeeyeekky ggpsfqpeff sgvgevltdp payvsigsty
     2761 liaqtltelp nvvrpsdsth yteatpevss laelspqips spfpvyvdng vskfpevpht
     2821 saqpvstvts sqksiespfk evhanieeti kplggnvhrt eppsmsrdpa ldvsedeskh
     2881 klleeletsp tkpetsqdfp nkakdhipge tvgmlagirt tesepvitad dmelggatqq
     2941 phsasaafrv etgmvpqpiq qeperptfps leinhethts lfgesilats ekqvsqkild
     3001 nsnqatvsst ldlhtahals pfsildnsne tafligisee svegtavylp gpdlcktnpc
     3061 lnggtcypte tsyvctcapg ysgdqceldf dechsnpcrn gatcvdgfnt frclclpsyv
     3121 galceqdtet cdygwhkfqg qcykyfahrr twdaaerecr lqgahltsil sheeqmfvnr
     3181 vghdyqwigl ndkmfehdfr wtdgsalqye nwrpnqpdsf fsagedcvvi iwhengqwnd
     3241 vpcnyhltyt ckkgtvacgq ppvvenaktf gkmkpryein sliryhckdg fiqrhlptir
     3301 clgngrwamp kitcmnpsay qrtyskkylk nsssakdnsi ntskhehrws rrqetrr
//
LOCUS       CSPG2_HUMAN             3396 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=Versican core protein; AltName: Full=Chondroitin
            sulfate proteoglycan core protein 2; Short=Chondroitin sulfate
            proteoglycan 2; AltName: Full=Glial hyaluronate-binding protein;
            Short=GHAP; AltName: Full=Large fibroblast proteoglycan; AltName:
            Full=PG-M; Flags: Precursor.
ACCESSION   P13611
VERSION     P13611.3
DBSOURCE    UniProtKB: locus CSPG2_HUMAN, accession P13611;
            class: standard.
            extra accessions:P20754,Q13010,Q13189,Q15123,Q9UCL9,Q9UNW5
            created: Jan 1, 1990.
            sequence updated: Nov 1, 1997.
            annotation updated: Sep 13, 2023.
            xrefs: X15998.1, CAA34128.1, U16306.1, AAA65018.1, U26555.1,
            AAA67565.1, D32039.1, BAA06801.1, S52488.1, AAB24878.1, J02814.1,
            AAA36437.1, AF084545.1, AAD48545.1, A60979, NP_001119808.1,
            NP_001157569.1, NP_001157570.1, NP_004376.2
            xrefs (non-sequence databases): CCDS:CCDS4060.1, CCDS:CCDS47242.1,
            CCDS:CCDS54875.1, CCDS:CCDS54876.1, SMR:P13611, BioGRID:107844,
            IntAct:P13611, MINT:P13611, STRING:9606.ENSP00000265077,
            DrugBank:DB08818, CarbonylDB:P13611, GlyConnect:1890,
            GlyCosmos:P13611, GlyGen:P13611, iPTMnet:P13611,
            PhosphoSitePlus:P13611, SwissPalm:P13611, BioMuta:VCAN,
            DMDM:2506816, CPTAC:CPTAC-5841, CPTAC:CPTAC-5866, EPD:P13611,
            jPOST:P13611, MassIVE:P13611, MaxQB:P13611, PaxDb:P13611,
            PeptideAtlas:P13611, ProteomicsDB:52938, ProteomicsDB:52939,
            ProteomicsDB:52940, ProteomicsDB:52941, ProteomicsDB:52942,
            Antibodypedia:1346, DNASU:1462, Ensembl:ENST00000265077.8,
            Ensembl:ENSP00000265077.3, Ensembl:ENSG00000038427.16,
            Ensembl:ENST00000342785.8, Ensembl:ENSP00000342768.4,
            Ensembl:ENST00000343200.9, Ensembl:ENSP00000340062.5,
            Ensembl:ENST00000502527.2, Ensembl:ENSP00000421362.2, GeneID:1462,
            KEGG:hsa:1462, MANE-Select:ENST00000265077.8, UCSC:uc003kii.4,
            AGR:HGNC:2464, CTD:1462, DisGeNET:1462, GeneCards:VCAN,
            GeneReviews:VCAN, HGNC:2464, HPA:ENSG00000038427, MalaCards:VCAN,
            MIM:118661, MIM:143200, neXtProt:NX_P13611,
            OpenTargets:ENSG00000038427, Orphanet:898, PharmGKB:PA162408788,
            VEuPathDB:HostDB:ENSG00000038427, eggNOG:ENOG502QRBE,
            GeneTree:ENSGT00940000156102, HOGENOM:CLU_000303_1_1_1,
            InParanoid:P13611, OMA:ELTWKPE, OrthoDB:5323609at2759,
            PhylomeDB:P13611, TreeFam:TF332134, PathwayCommons:P13611,
            Reactome:R-HSA-1971475, Reactome:R-HSA-2022870,
            Reactome:R-HSA-2022923, Reactome:R-HSA-2024101,
            Reactome:R-HSA-3000178, Reactome:R-HSA-3560783,
            Reactome:R-HSA-3560801, Reactome:R-HSA-3595172,
            Reactome:R-HSA-3595174, Reactome:R-HSA-3595177,
            Reactome:R-HSA-381426, Reactome:R-HSA-4420332,
            Reactome:R-HSA-8957275, SignaLink:P13611, SIGNOR:P13611,
            BioGRID-ORCS:1462, ChiTaRS:VCAN, GeneWiki:Versican,
            GenomeRNAi:1462, Pharos:P13611, PRO:PR:P13611,
            Proteomes:UP000005640, RNAct:P13611, Bgee:ENSG00000038427,
            ExpressionAtlas:P13611, Genevisible:P13611, GO:0062023, GO:0005788,
            GO:0031012, GO:0005576, GO:0005615, GO:0005796, GO:0033165,
            GO:0043202, GO:0016020, GO:0072534, GO:0001750, GO:0045202,
            GO:0005509, GO:0030246, GO:0030021, GO:0005539, GO:0005540,
            GO:0007155, GO:0008037, GO:0007417, GO:0010001, GO:0008347,
            GO:0001649, GO:0002052, GO:0001501, CDD:cd00033, CDD:cd03588,
            CDD:cd00054, CDD:cd05901, CDD:cd03517, CDD:cd03520,
            Gene3D:2.10.70.10, Gene3D:2.60.40.10, Gene3D:2.10.25.10,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033987, InterPro:IPR016187,
            InterPro:IPR001881, InterPro:IPR000742, InterPro:IPR000152,
            InterPro:IPR018097, InterPro:IPR007110, InterPro:IPR036179,
            InterPro:IPR013783, InterPro:IPR003599, InterPro:IPR013106,
            InterPro:IPR000538, InterPro:IPR035976, InterPro:IPR000436,
            PANTHER:PTHR22804, Pfam:PF00008, Pfam:PF00059, Pfam:PF00084,
            Pfam:PF07686, Pfam:PF00193, PRINTS:PR01265, SMART:SM00032,
            SMART:SM00034, SMART:SM00181, SMART:SM00179, SMART:SM00409,
            SMART:SM00445, SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF57196,
            SUPFAM:SSF48726, PROSITE:PS00010, PROSITE:PS00615, PROSITE:PS50041,
            PROSITE:PS00022, PROSITE:PS01186, PROSITE:PS50026, PROSITE:PS01187,
            PROSITE:PS50835, PROSITE:PS01241, PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Alternative splicing; Calcium; Cataract; Cell projection; Direct
            protein sequencing; Disulfide bond; EGF-like domain; Extracellular
            matrix; Glycoprotein; Hyaluronic acid; Immunoglobulin domain;
            Lectin; Phosphoprotein; Proteoglycan; Reference proteome; Repeat;
            Secreted; Signal; Sushi.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3396)
  AUTHORS   Zimmermann,D.R. and Ruoslahti,E.
  TITLE     Multiple domains of the large fibroblast proteoglycan, versican
  JOURNAL   EMBO J 8 (10), 2975-2981 (1989)
   PUBMED   2583089
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V1), AND SUBCELLULAR LOCATION.;
            TISSUE=Placenta
REFERENCE   2  (residues 1 to 3396)
  AUTHORS   Dours-Zimmermann,M.T. and Zimmermann,D.R.
  TITLE     A novel glycosaminoglycan attachment domain identified in two
            alternative splice variants of human versican
  JOURNAL   J Biol Chem 269 (52), 32992-32998 (1994)
   PUBMED   7806529
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V2).;
            TISSUE=Glial tumor
REFERENCE   3  (residues 1 to 3396)
  AUTHORS   Naso,M.F., Zimmermann,D.R. and Iozzo,R.V.
  TITLE     Characterization of the complete genomic structure of the human
            versican gene and functional analysis of its promoter
  JOURNAL   J Biol Chem 269 (52), 32999-33008 (1994)
   PUBMED   7528742
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM V0).
REFERENCE   4  (residues 1 to 3396)
  AUTHORS   Zako,M., Shinomura,T., Ujita,M., Ito,K. and Kimata,K.
  TITLE     Expression of PG-M(V3), an alternatively spliced form of PG-M
            without a chondroitin sulfate attachment in region in mouse and
            human tissues
  JOURNAL   J Biol Chem 270 (8), 3914-3918 (1995)
   PUBMED   7876137
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).;
            TISSUE=Brain
REFERENCE   5  (residues 1 to 3396)
  AUTHORS   Yao,L.Y., Moody,C., Schonherr,E., Wight,T.N. and Sandell,L.J.
  TITLE     Identification of the proteoglycan versican in aorta and smooth
            muscle cells by DNA sequence analysis, in situ hybridization and
            immunohistochemistry
  JOURNAL   Matrix Biol 14 (3), 213-225 (1994)
   PUBMED   7921538
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 208-1427; 2081-2372 AND 2897-3233
            (ISOFORM V1), AND DEVELOPMENTAL STAGE.
REFERENCE   6  (residues 1 to 3396)
  AUTHORS   Iozzo,R.V., Naso,M.F., Cannizzaro,L.A., Wasmuth,J.J. and
            McPherson,J.D.
  TITLE     Mapping of the versican proteoglycan gene (CSPG2) to the long arm
            of human chromosome 5 (5q12-5q14)
  JOURNAL   Genomics 14 (4), 845-851 (1992)
   PUBMED   1478664
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-347.
REFERENCE   7  (residues 1 to 3396)
  AUTHORS   Krusius,T., Gehlsen,K.R. and Ruoslahti,E.
  TITLE     A fibroblast chondroitin sulfate proteoglycan core protein contains
            lectin-like and growth factor-like sequences
  JOURNAL   J Biol Chem 262 (27), 13120-13125 (1987)
   PUBMED   2820964
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 2709-3396.;
            TISSUE=Lung fibroblast
REFERENCE   8  (residues 1 to 3396)
  AUTHORS   Lemire,J.M., Braun,K.R., Maurel,P., Kaplan,E.D., Schwartz,S.M. and
            Wight,T.N.
  TITLE     Versican/PG-M isoforms in vascular smooth muscle cells
  JOURNAL   Arterioscler Thromb Vasc Biol 19 (7), 1630-1639 (1999)
   PUBMED   10397680
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 3333-3396 (ISOFORM VINT).;
            TISSUE=Aortic smooth muscle
REFERENCE   9  (residues 1 to 3396)
  AUTHORS   Perides,G., Rahemtulla,F., Lane,W.S., Asher,R.A. and Bignami,A.
  TITLE     Isolation of a large aggregating proteoglycan from human brain
  JOURNAL   J Biol Chem 267 (33), 23883-23887 (1992)
   PUBMED   1429726
  REMARK    PROTEIN SEQUENCE OF 21-37.
REFERENCE   10 (residues 1 to 3396)
  AUTHORS   Perides,G., Lane,W.S., Andrews,D., Dahl,D. and Bignami,A.
  TITLE     Isolation and partial characterization of a glial
            hyaluronate-binding protein
  JOURNAL   J Biol Chem 264 (10), 5981-5987 (1989)
   PUBMED   2466833
  REMARK    PROTEIN SEQUENCE OF 24-50; 80-119; 128-155; 167-218; 229-268 AND
            277-290.;
            TISSUE=Brain
REFERENCE   11 (residues 1 to 3396)
  AUTHORS   Bignami,A., Lane,W.S., Andrews,D. and Dahl,D.
  TITLE     Structural similarity of hyaluronate binding proteins in brain and
            cartilage
  JOURNAL   Brain Res Bull 22 (1), 67-70 (1989)
   PUBMED   2469524
  REMARK    PROTEIN SEQUENCE OF 171-210 AND 289-303, AND TISSUE SPECIFICITY.
REFERENCE   12 (residues 1 to 3396)
  AUTHORS   Paulus,W., Baur,I., Dours-Zimmermann,M.T. and Zimmermann,D.R.
  TITLE     Differential expression of versican isoforms in brain tumors
  JOURNAL   J Neuropathol Exp Neurol 55 (5), 528-533 (1996)
   PUBMED   8627343
  REMARK    TISSUE SPECIFICITY (ISOFORMS V0; V1; V2 AND V3).
REFERENCE   13 (residues 1 to 3396)
  AUTHORS   Miyamoto,T., Inoue,H., Sakamoto,Y., Kudo,E., Naito,T., Mikawa,T.,
            Mikawa,Y., Isashiki,Y., Osabe,D., Shinohara,S., Shiota,H. and
            Itakura,M.
  TITLE     Identification of a novel splice site mutation of the CSPG2 gene in
            a Japanese family with Wagner syndrome
  JOURNAL   Invest Ophthalmol Vis Sci 46 (8), 2726-2735 (2005)
   PUBMED   16043844
  REMARK    INVOLVEMENT IN WGVRP.
REFERENCE   14 (residues 1 to 3396)
  AUTHORS   Burkard,T.R., Planyavsky,M., Kaupe,I., Breitwieser,F.P.,
            Burckstummer,T., Bennett,K.L., Superti-Furga,G. and Colinge,J.
  TITLE     Initial characterization of the human central proteome
  JOURNAL   BMC Syst Biol 5, 17 (2011)
   PUBMED   21269460
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
            Publication Status: Online-Only
REFERENCE   15 (residues 1 to 3396)
  AUTHORS   Kloeckener-Gruissem,B., Neidhardt,J., Magyar,I., Plauchu,H.,
            Zech,J.C., Morle,L., Palmer-Smith,S.M., Macdonald,M.J., Nas,V.,
            Fry,A.E. and Berger,W.
  TITLE     Novel VCAN mutations and evidence for unbalanced alternative
            splicing in the pathogenesis of Wagner syndrome
  JOURNAL   Eur J Hum Genet 21 (3), 352-356 (2013)
   PUBMED   22739342
  REMARK    INVOLVEMENT IN WGVRP, AND PATHOLOGICAL MECHANISM.
REFERENCE   16 (residues 1 to 3396)
  AUTHORS   Bian,Y., Song,C., Cheng,K., Dong,M., Wang,F., Huang,J., Sun,D.,
            Wang,L., Ye,M. and Zou,H.
  TITLE     An enzyme assisted RP-RPLC approach for in-depth analysis of human
            liver phosphoproteome
  JOURNAL   J Proteomics 96, 253-262 (2014)
   PUBMED   24275569
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2116 AND THR-2617,
            AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver
REFERENCE   17 (residues 1 to 3396)
  AUTHORS   Tagliabracci,V.S., Wiley,S.E., Guo,X., Kinch,L.N., Durrant,E.,
            Wen,J., Xiao,J., Cui,J., Nguyen,K.B., Engel,J.L., Coon,J.J.,
            Grishin,N., Pinna,L.A., Pagliarini,D.J. and Dixon,J.E.
  TITLE     A Single Kinase Generates the Majority of the Secreted
            Phosphoproteome
  JOURNAL   Cell 161 (7), 1619-1632 (2015)
   PUBMED   26091039
  REMARK    PHOSPHORYLATION AT SER-2116.
REFERENCE   18 (residues 1 to 3396)
  AUTHORS   Noborn,F., Gomez Toledo,A., Sihlbom,C., Lengqvist,J., Fries,E.,
            Kjellen,L., Nilsson,J. and Larson,G.
  TITLE     Identification of chondroitin sulfate linkage region glycopeptides
            reveals prohormones as a novel class of proteoglycans
  JOURNAL   Mol Cell Proteomics 14 (1), 41-49 (2015)
   PUBMED   25326458
  REMARK    SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT
            SER-1548.
REFERENCE   19 (residues 1 to 3396)
  AUTHORS   Felemban,M., Dorgau,B., Hunt,N.C., Hallam,D., Zerti,D., Bauer,R.,
            Ding,Y., Collin,J., Steel,D., Krasnogor,N., Al-Aama,J., Lindsay,S.,
            Mellough,C. and Lako,M.
  TITLE     Extracellular matrix component expression in human pluripotent stem
            cell-derived retinal organoids recapitulates retinogenesis in vivo
            and reveals an important role for IMPG1 and CD44 in the development
            of photoreceptors and interphotoreceptor matrix
  JOURNAL   Acta Biomater 74, 207-221 (2018)
   PUBMED   29777959
  REMARK    SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
REFERENCE   20 (residues 1 to 3396)
  AUTHORS   Toledo,A.G., Pihl,J., Spliid,C.B., Persson,A., Nilsson,J.,
            Pereira,M.A., Gustavsson,T., Choudhary,S., Oo,H.Z., Black,P.C.,
            Daugaard,M., Esko,J.D., Larson,G., Salanti,A. and Clausen,T.M.
  TITLE     An affinity chromatography and glycoproteomics workflow to profile
            the chondroitin sulfate proteoglycans that interact with malarial
            VAR2CSA in the placenta and in cancer
  JOURNAL   Glycobiology 30 (12), 989-1002 (2020)
   PUBMED   32337544
  REMARK    TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-659; SER-1548;
            SER-1631; SER-1959; SER-2247 AND SER-2767.
REFERENCE   21 (residues 1 to 3396)
  AUTHORS   Ramarajan,M.G., Saraswat,M., Budhraja,R., Garapati,K., Raymond,K.
            and Pandey,A.
  TITLE     Mass spectrometric analysis of chondroitin sulfate-linked peptides
  JOURNAL   J Proteins Proteom 13 (4), 187-203 (2022)
   PUBMED   36213313
  REMARK    TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-1548; SER-1631;
            SER-1935; SER-1959; SER-2254; SER-2723 AND SER-2941.
COMMENT     On or before Jul 28, 2006 this sequence version replaced
            gi:74720244, gi:482656, gi:129888.
            [FUNCTION] May play a role in intercellular signaling and in
            connecting cells with the extracellular matrix. May take part in
            the regulation of cell motility, growth and differentiation. Binds
            hyaluronic acid.
            [SUBUNIT] Interacts with FBLN1. {ECO:0000250}.
            [INTERACTION] P13611; P14780: MMP9; NbExp=3; IntAct=EBI-8515977,
            EBI-1382326.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000305|PubMed:2583089}. Cell projection, cilium,
            photoreceptor outer segment {ECO:0000269|PubMed:29777959}.
            Secreted, extracellular space, extracellular matrix,
            interphotoreceptor matrix {ECO:0000269|PubMed:29777959}. Secreted
            {ECO:0000269|PubMed:25326458}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=5; Comment=Additional isoforms seem to exist.; Name=V0;
            IsoId=P13611-1; Sequence=Displayed; Name=V1; IsoId=P13611-2;
            Sequence=VSP_003082, VSP_003083; Name=V2; IsoId=P13611-3;
            Sequence=VSP_003084; Name=V3; IsoId=P13611-4; Sequence=VSP_003082,
            VSP_003085; Name=Vint; IsoId=P13611-5; Sequence=VSP_003086.
            [TISSUE SPECIFICITY] Detected in placenta (at protein level)
            (PubMed:32337544). Detected in cerebrospinal fluid, fibroblasts and
            urine (at protein level) (PubMed:25326458, PubMed:36213313).
            Expressed in the retina (at protein level) (PubMed:29777959).
            Cerebral white matter and plasma (PubMed:2469524). Isoform V0:
            Expressed in normal brain, gliomas, medulloblastomas, schwannomas,
            neurofibromas, and meningiomas (PubMed:8627343). Isoform V1:
            Expressed in normal brain, gliomas, medulloblastomas, schwannomas,
            neurofibromas, and meningiomas (PubMed:8627343). Isoform V2:
            Restricted to normal brain and gliomas (PubMed:8627343). Isoform
            V3: Found in all these tissues except medulloblastomas
            (PubMed:8627343). {ECO:0000269|PubMed:2469524,
            ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:29777959,
            ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313,
            ECO:0000269|PubMed:8627343}.
            [DEVELOPMENTAL STAGE] Expressed in developing photoreceptors and
            the interphotoreceptor matrix between 12 and 17 weeks post
            conception (at protein level) (PubMed:29777959). Disappears in
            aorta after the cartilage development (PubMed:7921538).
            {ECO:0000269|PubMed:29777959, ECO:0000269|PubMed:7921538}.
            [PTM] Phosphorylated by FAM20C in the extracellular medium.
            {ECO:0000269|PubMed:26091039}.
            [PTM] Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the
            pericellular matrix surrounding myoblasts, facilitating myoblast
            contact and fusion which is required for skeletal muscle
            development and regeneration. {ECO:0000250|UniProtKB:Q62059}.
            [DISEASE] Wagner vitreoretinopathy (WGVRP) [MIM:143200]: A rare
            vitreoretinopathy characterized by an optically empty vitreous
            cavity with fibrillary condensations and a preretinal avascular
            membrane. Other optical features include progressive chorioretinal
            atrophy, perivascular sheating, subcapsular cataract and myopia.
            {ECO:0000269|PubMed:16043844, ECO:0000269|PubMed:22739342}.
            Note=The disease is caused by variants affecting the gene
            represented in this entry. The pathological mechanism involves a
            quantitative imbalance of the normally occurring splice variants
            (PubMed:22739342). {ECO:0000269|PubMed:22739342}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Versican;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_hum_Ctlect_214'.
            [WEB RESOURCE] Name=Atlas of Genetics and Cytogenetics in Oncology
            and Haematology;
            URL='https://atlasgeneticsoncology.org/gene/40173/VCAN'.
FEATURES             Location/Qualifiers
     source          1..3396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..3396
                     /gene="VCAN"
                     /gene_synonym="CSPG2"
     Protein         1..3396
                     /product="Versican core protein"
                     /note="Chondroitin sulfate proteoglycan core protein 2;
                     Glial hyaluronate-binding protein; Large fibroblast
                     proteoglycan; PG-M; Chondroitin sulfate proteoglycan 2;
                     GHAP"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..20
                     /region_name="Signal"
                     /note="/evidence=ECO:0000269|PubMed:1429726."
     Region          21..3396
                     /region_name="Mature chain"
                     /note="Versican core protein. /id=PRO_0000017522."
     Region          21..146
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          26..152
                     /region_name="Ig_Versican"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), versican;
                     cd05901"
                     /db_xref="CDD:409482"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409482"
     Region          32..34
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409482"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409482"
     Bond            bond(44,130)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          63..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409482"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409482"
     Region          88
                     /region_name="Conflict"
                     /note="N -> D (in Ref. 10; AA sequence).
                     /evidence=ECO:0000305."
     Region          101..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409482"
     Region          112..118
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409482"
     Region          126..133
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409482"
     Region          143..152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409482"
     Region          150..245
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          150..244
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            160..161
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(172,243)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(196,217)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          251..347
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          251..346
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            258..259
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Region          260
                     /region_name="Conflict"
                     /note="K -> I (in Ref. 10; AA sequence).
                     /evidence=ECO:0000305."
     Bond            bond(270,345)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          274
                     /region_name="Conflict"
                     /note="D -> A (in Ref. 4; BAA06801).
                     /evidence=ECO:0000305."
     Region          284
                     /region_name="Conflict"
                     /note="Q -> G (in Ref. 10; AA sequence).
                     /evidence=ECO:0000305."
     Bond            bond(294,315)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          300
                     /region_name="Variant"
                     /note="S -> L (in dbSNP:rs2652098). /id=VAR_021958."
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          348..1335
                     /region_name="Region of interest in the sequence"
                     /note="GAG-alpha (glucosaminoglycan attachment domain)."
     Region          348
                     /region_name="Splicing variant"
                     /note="P -> R (in isoform V1 and isoform V3).
                     /evidence=ECO:0000303|PubMed:2583089,
                     ECO:0000303|PubMed:7876137, ECO:0000303|PubMed:7921538.
                     /id=VSP_003082."
     Region          349..3089
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V3).
                     /evidence=ECO:0000303|PubMed:7876137. /id=VSP_003085."
     Region          349..1335
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V1).
                     /evidence=ECO:0000303|PubMed:2583089,
                     ECO:0000303|PubMed:7921538. /id=VSP_003083."
     Region          420..439
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          428
                     /region_name="Variant"
                     /note="G -> D (in dbSNP:rs2287926). /id=VAR_020214."
     Region          603..622
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            615
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            659
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:32337544."
     Site            782
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          807..829
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            809
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1126..1154
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1138..1154
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1277..1316
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1332
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1336..3089
                     /region_name="Region of interest in the sequence"
                     /note="GAG-beta."
     Region          1336..3089
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V2).
                     /evidence=ECO:0000303|PubMed:7806529. /id=VSP_003084."
     Site            1398
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1420..1497
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1428..1429
                     /site_type="cleavage"
                     /note="Cleavage; by ADAMTS15.
                     /evidence=ECO:0000250|UniProtKB:Q62059."
     Region          1435..1453
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1442
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1461..1480
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1468
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1510..1539
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1516
                     /region_name="Variant"
                     /note="K -> R (in dbSNP:rs309559). /id=VAR_021959."
     Site            1548
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:25326458,
                     ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313."
     Site            1631
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:32337544,
                     ECO:0000269|PubMed:36213313."
     Site            1663
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1717..1737
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1717..1732
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1759..1789
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1826
                     /region_name="Variant"
                     /note="R -> H (in dbSNP:rs188703). /id=VAR_031632."
     Site            1898
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1935
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:36213313."
     Site            1959
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:32337544,
                     ECO:0000269|PubMed:36213313."
     Region          1962..1994
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1963..1994
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2107..2134
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2116
                     /site_type="phosphorylation"
                     /note="Phosphoserine; by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:24275569."
     Region          2168..2188
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2179
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2247
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:32337544."
     Site            2254
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:36213313."
     Site            2272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2301
                     /region_name="Variant"
                     /note="F -> Y (in dbSNP:rs160278). /id=VAR_020215."
     Region          2315
                     /region_name="Variant"
                     /note="V -> L (in dbSNP:rs3734094). /id=VAR_020216."
     Site            2360
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2371..2396
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2385
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2392
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2445..2473
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2445..2463
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2493..2518
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2493..2517
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2598..2617
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62059."
     Site            2617
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569."
     Site            2628
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2709..2713
                     /region_name="Conflict"
                     /note="IKAEA -> EFREV (in Ref. 7; AAA36437).
                     /evidence=ECO:0000305."
     Site            2722
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            2723
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:36213313."
     Site            2767
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:32337544."
     Region          2834..2856
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2881..2905
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2934
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2937
                     /region_name="Variant"
                     /note="D -> Y (in dbSNP:rs160277). /id=VAR_021960."
     Site            2941
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:36213313."
     Region          3011
                     /region_name="Variant"
                     /note="N -> K (in dbSNP:rs16900532). /id=VAR_031633."
     Site            3067
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          3089..3125
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          3091..3125
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Bond            bond(3093,3104)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3098,3113)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3115,3124)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3127..3163
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          3127..3163
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(3127,3130,3144)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(3131,3142)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3136,3151)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3153,3162)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3169..3292
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Bond            bond(3169,3180)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3176..3290
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(3187,3219..3222,3251,3261,3269,3271,3277,3280,
                     3282..3284)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Bond            bond(3197,3289)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(3230,3234,3257,3263..3264)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3234,3264)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3254,3256,3263,3277..3278)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Bond            bond(3265,3281)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3294..3354
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          3296..3352
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(3296,3339)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(3306,3326)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(3325,3352)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3355..3396
                     /region_name="Splicing variant"
                     /note="PSAYQRTYSMKYFKNSSSAKDNSINTSKHDHRWSRRWQESRR ->
                     RKWSFRKNGLPCYNNY (in isoform Vint).
                     /evidence=ECO:0000303|PubMed:10397680. /id=VSP_003086."
     Site            3369
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          3371..3396
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          3378..3396
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            3379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
ORIGIN
        1 mfiniksilw mcstlivtha lhkvkvgksp pvrgslsgkv slpchfstmp tlppsyntse
       61 flrikwskie vdkngkdlke ttvlvaqngn ikigqdykgr vsvpthpeav gdasltvvkl
      121 lasdaglyrc dvmygiedtq dtvsltvdgv vfhyraatsr ytlnfeaaqk acldvgavia
      181 tpeqlfaaye dgfeqcdagw ladqtvrypi raprvgcygd kmgkagvrty gfrspqetyd
      241 vycyvdhldg dvfhltvpsk ftfeeaakec enqdarlatv gelqaawrng fdqcdygwls
      301 dasvrhpvtv araqcgggll gvrtlyrfen qtgfpppdsr fdaycfkpke attidlsila
      361 etaspslske pqmvsdrttp iiplvdelpv iptefppvgn ivsfeqkatv qpqaitdsla
      421 tklptptgst kkpwdmddys psasgplgkl diseikeevl qsttgvshya tdswdgvved
      481 kqtqesvtqi eqievgplvt smeilkhips kefpvtetpl vtarmilesk tekkmvstvs
      541 elvttghygf tlgeeddedr tltvgsdest lifdqipevi tvsktsedti hthledlesv
      601 sasttvspli mpdnngssmd dweerqtsgr iteeflgkyl sttpfpsqhr teielfpysg
      661 dkilvegist viypslqtem thrrertetl ipemrtdtyt deiqeeitks pfmgkteeev
      721 fsgmklstsl sepihvtess vemtksfdfp tlitklsaep tevrdmeedf tatpgttkyd
      781 enittvllah gtlsveaatv skwswdednt tskplestep sassklppal lttvgmngkd
      841 kdipsftedg adeftlipds tqkqleevtd ediaahgkft irfqpttstg iaekstlrds
      901 tteekvppit stegqvyatm egsalgeved vdlskpvstv pqfahtseve glafvsysst
      961 qepttyvdss htiplsvipk tdwgvlvpsv psedevlgep sqdilvidqt rleatispet
     1021 mrttkitegt tqeefpwkeq taekpvpals stawtpkeav tpldeqegdg saytvsedel
     1081 ltgservpvl ettpvgkidh svsyppgavt ehkvktdevv tltprigpkv slspgpeqky
     1141 etegssttgf tsslspfsth itqlmeettt ektsledidl gsglfekpka teliefstik
     1201 vtvpsditta fssvdrlhtt safkpssait kkpplidrep geettsdmvi igestshvpp
     1261 ttledivake tetdidreyf ttssppatqp trpptvedke afgpqalstp qppastkfhp
     1321 dinvyiievr enktgrmsdl svighpidse skedepcsee tdpvhdlmae ilpefpdiie
     1381 idlyhseene eeeeecanat dvtttpsvqy ingkhlvttv pkdpeaaear rgqfesvaps
     1441 qnfsdssesd thpfviakte lstavqpnes tetteslevt wkpetypets ehfsggepdv
     1501 fptvpfheef esgtakkgae svterdtevg hqahehtepv slfpeessge iaidqesqki
     1561 afaratevtf geevekstsv tytptivpss asayvseeea vtlignpwpd dllstkeswv
     1621 eatprqvvel sgsssipite gsgeaeeded tmftmvtdls qrnttdtlit ldtsriites
     1681 ffevpattiy pvseqpsakv vptkfvsetd tsewissttv eekkrkeeeg ttgtastfev
     1741 ysstqrsdql ilpfelespn vatssdsgtr ksfmslttpt qseremtdst pvftetntle
     1801 nlgaqttehs sihqpgvqeg lttlprspas vfmeqgsgea aadpetttvs sfslnveyai
     1861 qaekevagtl sphvettfst eptglvlstv mdrvvaenit qtsreivise rlgepnygae
     1921 irgfstgfpl eedfsgdfre ystvshpiak eetvmmegsg daafrdtqts pstvptsvhi
     1981 shisdsegps stmvstsafp weeftssaeg sgeqlvtvss svvpvlpsav qkfsgtassi
     2041 ideglgevgt vneidrrsti lptaevegtk apvekeevkv sgtvstnfpq tiepaklwsr
     2101 qevnpvrqei esettseeqi qeeksfespq nspateqtif dsqtftetel kttdysvltt
     2161 kktysddkem keedtslvnm stpdpdangl esyttlpeat ekshfflata lvtesipaeh
     2221 vvtdspikke estkhfpkgm rptiqesdte llfsglgsge evlptlptes vnfteveqin
     2281 ntlyphtsqv estssdkied fnrmenvake vgplvsqtdi fegsgsvtst tlieilsdtg
     2341 aegptvaplp fstdighpqn qtvrwaeeiq tsrpqtiteq dsnknsstae inetttsstd
     2401 flaraygfem akefvtsapk psdlyyepsg egsgevdivd sfhtsattqa trqessttfv
     2461 sdgslekhpe vpsakavtad gfptvsvmlp lhseqnkssp dptstlsntv syerstdgsf
     2521 qdrfrefeds tlkpnrkkpt eniiidldke dkdliltite stileilpel tsdkntiidi
     2581 dhtkpvyedi lgmqtdidte vpsephdsnd esnddstqvq eiyeaavnls lteetfegsa
     2641 dvlasytqat hdesmtyedr sqldhmgfhf ttgipapste teldvllpta tslpiprksa
     2701 tvipeiegik aeakalddmf esstlsdgqa iadqseiipt lgqfertqee yedkkhagps
     2761 fqpefssgae ealvdhtpyl siatthlmdq svtevpdvme gsnppyytdt tlavstfakl
     2821 ssqtpssplt iysgseasgh teipqpsalp gidvgssvms pqdsfkeihv nieatfkpss
     2881 eeylhitepp slspdtklep seddgkpell eemeasptel iavegteilq dfqnktdgqv
     2941 sgeaikmfpt iktpeagtvi ttadeieleg atqwphstsa satygveagv vpwlspqtse
     3001 rptlssspei npetqaalir gqdstiaase qqvaarilds ndqatvnpve fntevatppf
     3061 slletsnetd fligineesv egtaiylpgp drckmnpcln ggtcyptets yvctcvpgys
     3121 gdqceldfde chsnpcrnga tcvdgfntfr clclpsyvga lceqdtetcd ygwhkfqgqc
     3181 ykyfahrrtw daaerecrlq gahltsilsh eeqmfvnrvg hdyqwiglnd kmfehdfrwt
     3241 dgstlqyenw rpnqpdsffs agedcvviiw hengqwndvp cnyhltytck kgtvacgqpp
     3301 vvenaktfgk mkpryeinsl iryhckdgfi qrhlptircl gngrwaipki tcmnpsayqr
     3361 tysmkyfkns ssakdnsint skhdhrwsrr wqesrr
//
LOCUS       CLC4E_RAT                215 aa            linear   ROD 22-FEB-2023
DEFINITION  RecName: Full=C-type lectin domain family 4 member E; AltName:
            Full=C-type lectin superfamily member 9; AltName:
            Full=Macrophage-inducible C-type lectin; Short=Mincle.
ACCESSION   Q67EQ1
VERSION     Q67EQ1.1
DBSOURCE    UniProtKB: locus CLC4E_RAT, accession Q67EQ1;
            class: standard.
            extra accessions:Q56TZ4
            created: Feb 15, 2005.
            sequence updated: Oct 11, 2004.
            annotation updated: Feb 22, 2023.
            xrefs: AY363175.1, AAR18685.1, AY581049.1, AAT92025.1,
            NP_001005897.1
            xrefs (non-sequence databases): AlphaFoldDB:Q67EQ1, SMR:Q67EQ1,
            STRING:10116.ENSRNOP00000013562, GlyCosmos:Q67EQ1, GlyGen:Q67EQ1,
            iPTMnet:Q67EQ1, PhosphoSitePlus:Q67EQ1, PaxDb:Q67EQ1,
            GeneID:450223, KEGG:rno:450223, UCSC:RGD:1359298, AGR:RGD:1359298,
            CTD:26253, RGD:1359298, eggNOG:KOG4297, InParanoid:Q67EQ1,
            OrthoDB:2881452at2759, PhylomeDB:Q67EQ1, Reactome:R-RNO-5621480,
            PRO:PR:Q67EQ1, Proteomes:UP000002494, GO:0042995, GO:0009897,
            GO:0016020, GO:0001891, GO:0030670, GO:0005886, GO:0005509,
            GO:0030246, GO:0051861, GO:0038187, GO:0038023, GO:0061760,
            GO:0042742, GO:0038094, GO:0006955, GO:0045087, GO:0002221,
            GO:0001819, GO:0002292, CDD:cd03590, Gene3D:3.10.100.10,
            InterPro:IPR001304, InterPro:IPR016186, InterPro:IPR018378,
            InterPro:IPR033989, InterPro:IPR016187, PANTHER:PTHR46784,
            PANTHER:PTHR46784:SF1, Pfam:PF00059, SMART:SM00034,
            SUPFAM:SSF56436, PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Calcium; Cell membrane; Cell projection; Disulfide bond;
            Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
            Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
            Transmembrane helix.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Flornes,L.M., Bryceson,Y.T., Spurkland,A., Lorentzen,J.C.,
            Dissen,E. and Fossum,S.
  TITLE     Identification of lectin-like receptors expressed by antigen
            presenting cells and neutrophils and their mapping to a novel gene
            complex
  JOURNAL   Immunogenetics 56 (7), 506-517 (2004)
   PUBMED   15368084
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.;
            STRAIN=PVG
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Lorentzen,J.C., Flornes,L.M., Dissen,E. and Fossum,S.R.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-MAR-2004) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=Lewis
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Lobato-Pascual,A., Saether,P.C., Fossum,S., Dissen,E. and Daws,M.R.
  TITLE     Mincle, the receptor for mycobacterial cord factor, forms a
            functional receptor complex with MCL and FcepsilonRI-gamma
  JOURNAL   Eur J Immunol 43 (12), 3167-3174 (2013)
   PUBMED   23921530
  REMARK    SUBUNIT, IDENTIFICATION IN COMPLEX WITH CLEC4D AND FCER1G,
            SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
COMMENT     On May 9, 2007 this sequence version replaced gi:81870201.
            [FUNCTION] Calcium-dependent lectin that acts as a pattern
            recognition receptor (PRR) of the innate immune system: recognizes
            damage-associated molecular patterns (DAMPs) of abnormal self and
            pathogen-associated molecular patterns (PAMPs) of bacteria and
            fungi. The PAMPs notably include mycobacterial trehalose
            6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant
            immunomodulatory functions. Interacts with signaling adapter Fc
            receptor gamma chain/FCER1G to form a functional complex in myeloid
            cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to
            this receptor complex leads to phosphorylation of the
            immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G,
            triggering activation of SYK, CARD9 and NF-kappa-B, consequently
            driving maturation of antigen-presenting cells and shaping
            antigen-specific priming of T-cells toward effector T-helper 1
            (Th1) and T-helper 17 (Th17) cell subtypes. Also recognizes
            alpha-mannose residues on pathogenic fungi of the genus Malassezia
            and mediates macrophage activation. Through recognition of DAMPs
            released upon nonhomeostatic cell death, enables immune sensing of
            damaged self and promotes inflammatory cell infiltration into the
            damaged tissue. {ECO:0000250|UniProtKB:Q9R0Q8}.
            [SUBUNIT] Monomer and homodimer (By similarity). Interacts with
            signaling adapter Fc receptor gamma chain/FCER1G to form a
            functional complex; the interaction is direct (By similarity).
            Alternatively, acts as a bridge for interaction between CLEC4D and
            FCER1G. A heterodimer of CLEC4E and CLEC4D associates with
            signaling adapter Fc receptor gamma chain/FCER1G to form a
            functional complex (PubMed:23921530). Interacts with SAP130 nuclear
            protein that is released from necrotic cells; the interaction is
            direct (By similarity). {ECO:0000250|UniProtKB:Q9R0Q8,
            ECO:0000250|UniProtKB:Q9ULY5, ECO:0000269|PubMed:23921530}.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000305|PubMed:23921530};
            Single-pass type II membrane protein
            {ECO:0000250|UniProtKB:Q9R0Q8}. Cell projection, phagocytic cup
            {ECO:0000250|UniProtKB:Q9R0Q8}.
            [TISSUE SPECIFICITY] Expressed in dendritic cells, macrophages,
            neutrophils and in B-cells. {ECO:0000269|PubMed:15368084,
            ECO:0000269|PubMed:23921530}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Mincle;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_167'.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..215
                     /gene="Clec4e"
                     /gene_synonym="Clecsf9"
                     /gene_synonym="Mincle"
     Protein         1..215
                     /product="C-type lectin domain family 4 member E"
                     /note="C-type lectin superfamily member 9;
                     Macrophage-inducible C-type lectin; Mincle"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..215
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 4 member E.
                     /id=PRO_0000046621."
     Region          1..23
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          24..46
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          47..215
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          81..208
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(81,92)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          88..207
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(109,206)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(137,170,172,178,184..185,194..197)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(144,148,173,178..179)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(148,179)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Region          170..172
                     /region_name="Short sequence motif of biological interest"
                     /note="Confers specificity for glucose/mannose-type
                     carbohydrates. /evidence=ECO:0000250|UniProtKB:Q9ULY5."
     Bond            bond(180,198)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mnstkspash hterecfkns qvlswtmaga silflsvcfi trcvvtyhsf qiygqkklqp
       61 hktikelscy leasgsvknc cplnwkhfqs scyffstttl swlsslkncs dmgahlvvin
      121 tweeqeflfr tkprkkefyi gltdqvvegq wrwvddtpft eslsfwdage pnnivfvedc
      181 atmrdssnpr knwndvscff smpwicempe ispld
//
LOCUS       CSPG2_RAT               2738 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Versican core protein; AltName: Full=Chondroitin
            sulfate proteoglycan core protein 2; Short=Chondroitin sulfate
            proteoglycan 2; AltName: Full=Glial hyaluronate-binding protein;
            Short=GHAP; AltName: Full=Large fibroblast proteoglycan; AltName:
            Full=PG-M; Flags: Precursor.
ACCESSION   Q9ERB4
VERSION     Q9ERB4.2
DBSOURCE    UniProtKB: locus CSPG2_RAT, accession Q9ERB4;
            class: standard.
            extra accessions:O08592,O88564,Q9R1K4
            created: Sep 26, 2001.
            sequence updated: Sep 26, 2001.
            annotation updated: Sep 13, 2023.
            xrefs: AF062402.1, AAC40166.1, U75306.1, AAB51125.1, AF084544.1,
            AAD48544.1, AF072892.1, AAC26116.1, AY007691.1, AAG16631.1,
            NP_001164029.1, NP_001164030.1, NP_001164031.1
            xrefs (non-sequence databases): SMR:Q9ERB4, BioGRID:250300,
            IntAct:Q9ERB4, MINT:Q9ERB4, GlyCosmos:Q9ERB4, GlyGen:Q9ERB4,
            PhosphoSitePlus:Q9ERB4, ABCD:Q9ERB4, Ensembl:ENSRNOT00000063821,
            Ensembl:ENSRNOP00000062961, Ensembl:ENSRNOG00000029212,
            GeneID:114122, KEGG:rno:114122, UCSC:RGD:619940, AGR:RGD:619940,
            CTD:1462, RGD:619940, eggNOG:ENOG502QRBE,
            GeneTree:ENSGT00940000156102, InParanoid:Q9ERB4,
            OrthoDB:5323609at2759, PhylomeDB:Q9ERB4, Reactome:R-RNO-1971475,
            Reactome:R-RNO-2022870, Reactome:R-RNO-2022923,
            Reactome:R-RNO-2024101, Reactome:R-RNO-3000178,
            Reactome:R-RNO-381426, Reactome:R-RNO-8957275,
            Proteomes:UP000002494, GO:0009986, GO:0062023, GO:0031012,
            GO:0005576, GO:0005615, GO:0033165, GO:0072534, GO:0001750,
            GO:0045202, GO:0005509, GO:0030246, GO:0005540, GO:0030169,
            GO:0019903, GO:0031103, GO:0007155, GO:0007417, GO:0010001,
            GO:0008347, GO:0007507, GO:0002052, GO:0001501, GO:0001657,
            CDD:cd00033, CDD:cd03588, CDD:cd00054, CDD:cd05901, CDD:cd03517,
            CDD:cd03520, Gene3D:2.10.70.10, Gene3D:2.60.40.10,
            Gene3D:2.10.25.10, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033987,
            InterPro:IPR016187, InterPro:IPR001881, InterPro:IPR000742,
            InterPro:IPR000152, InterPro:IPR018097, InterPro:IPR007110,
            InterPro:IPR036179, InterPro:IPR013783, InterPro:IPR003599,
            InterPro:IPR013106, InterPro:IPR000538, InterPro:IPR035976,
            InterPro:IPR000436, PANTHER:PTHR22804, PANTHER:PTHR22804:SF6,
            Pfam:PF00008, Pfam:PF00059, Pfam:PF00084, Pfam:PF07686,
            Pfam:PF00193, PRINTS:PR01265, SMART:SM00032, SMART:SM00034,
            SMART:SM00181, SMART:SM00179, SMART:SM00409, SMART:SM00406,
            SMART:SM00445, SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF57196,
            SUPFAM:SSF48726, PROSITE:PS00010, PROSITE:PS00615, PROSITE:PS50041,
            PROSITE:PS00022, PROSITE:PS01186, PROSITE:PS50026, PROSITE:PS01187,
            PROSITE:PS50835, PROSITE:PS01241, PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Alternative splicing; Calcium; Cell projection; Disulfide bond;
            EGF-like domain; Extracellular matrix; Glycoprotein; Hyaluronic
            acid; Immunoglobulin domain; Lectin; Phosphoprotein; Proteoglycan;
            Reference proteome; Repeat; Secreted; Signal; Sushi.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2738)
  AUTHORS   Lemire,J.M., Braun,K.R., Maurel,P., Kaplan,E.D., Schwartz,S.M. and
            Wight,T.N.
  TITLE     Versican/PG-M isoforms in vascular smooth muscle cells
  JOURNAL   Arterioscler Thromb Vasc Biol 19 (7), 1630-1639 (1999)
   PUBMED   10397680
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 349-2738 (ISOFORM V0), NUCLEOTIDE
            SEQUENCE [MRNA] (ISOFORM V3), AND NUCLEOTIDE SEQUENCE [MRNA] OF
            2657-2738 (ISOFORM VINT).;
            STRAIN=Wistar Kyoto
REFERENCE   2  (residues 1 to 2738)
  AUTHORS   Milev,P., Maurel,P., Chiba,A., Mevissen,M., Popp,S., Yamaguchi,Y.,
            Margolis,R.K. and Margolis,R.U.
  TITLE     Differential regulation of expression of hyaluronan-binding
            proteoglycans in developing brain: aggrecan, versican, neurocan,
            and brevican
  JOURNAL   Biochem Biophys Res Commun 247 (2), 207-212 (1998)
   PUBMED   9642104
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 349-2738 (ISOFORM V0).;
            STRAIN=Wistar Kyoto
REFERENCE   3  (residues 1 to 2738)
  AUTHORS   Pyke,C., Kristensen,P., Ostergaard,P.B., Oturai,P.S. and Romer,J.
  TITLE     Proteoglycan expression in the normal rat kidney
  JOURNAL   Nephron 77 (4), 461-470 (1997)
   PUBMED   9434070
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 2421-2463 (ISOFORM V0).;
            TISSUE=Kidney
REFERENCE   4  (residues 1 to 2738)
  AUTHORS   Blomberg,L.A., Chan,W.-Y., Clerch,L. and Massaro,D.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-SEP-2000) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 2535-2738.;
            STRAIN=Sprague-Dawley; TISSUE=Lung
COMMENT     On Jun 17, 2002 this sequence version replaced gi:17380156.
            [FUNCTION] May play a role in intercellular signaling and in
            connecting cells with the extracellular matrix. May take part in
            the regulation of cell motility, growth and differentiation. Binds
            hyaluronic acid.
            [SUBUNIT] Interacts with FBLN1. {ECO:0000250}.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000250|UniProtKB:P13611}. Cell projection, cilium,
            photoreceptor outer segment {ECO:0000250|UniProtKB:P13611}.
            Secreted, extracellular space, extracellular matrix,
            interphotoreceptor matrix {ECO:0000250|UniProtKB:P13611}. Secreted
            {ECO:0000250|UniProtKB:P13611}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=3; Comment=Additional isoforms seem to exist.; Name=V0;
            IsoId=Q9ERB4-1; Sequence=Displayed; Name=V3; IsoId=Q9ERB4-2;
            Sequence=VSP_003091; Name=Vint; IsoId=Q9ERB4-3;
            Sequence=VSP_003092.
            [TISSUE SPECIFICITY] In kidney is expressed in the papillary area,
            but not in glomeruli.
            [DEVELOPMENTAL STAGE] Disappears after the cartilage development.
            [PTM] Phosphorylated by FAM20C in the extracellular medium.
            {ECO:0000250|UniProtKB:P13611}.
            [PTM] Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the
            pericellular matrix surrounding myoblasts, facilitating myoblast
            contact and fusion which is required for skeletal muscle
            development and regeneration. {ECO:0000250|UniProtKB:Q62059}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..2738
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..2738
                     /gene="Vcan"
                     /gene_synonym="Cspg2"
     Protein         1..2738
                     /product="Versican core protein"
                     /note="Chondroitin sulfate proteoglycan core protein 2;
                     Glial hyaluronate-binding protein; Large fibroblast
                     proteoglycan; PG-M; Chondroitin sulfate proteoglycan 2;
                     GHAP"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..20
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          21..2738
                     /region_name="Mature chain"
                     /note="Versican core protein. /id=PRO_0000017524."
     Region          21..146
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          26..152
                     /region_name="Ig_Versican"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), versican;
                     cd05901"
                     /db_xref="CDD:409482"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409482"
     Region          32..34
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409482"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409482"
     Bond            bond(44,130)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          63..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409482"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409482"
     Region          101..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409482"
     Region          112..118
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409482"
     Region          126..133
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409482"
     Region          143..152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409482"
     Region          150..245
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          150..244
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            160..161
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(172,243)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(196,217)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          251..347
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          251..346
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            258..259
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(270,345)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(294,315)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          349..2431
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V3).
                     /evidence=ECO:0000303|PubMed:10397680. /id=VSP_003091."
     Region          <349..695
                     /region_name="Region of interest in the sequence"
                     /note="GAG-alpha (glucosaminoglycan attachment domain)."
     gap             348..349
                     /note="Non-consecutive residues"
                     /estimated_length=unknown
     Region          641..679
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          654..672
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          696..2431
                     /region_name="Region of interest in the sequence"
                     /note="GAG-beta."
     Site            758
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            788..789
                     /site_type="cleavage"
                     /note="Cleavage; by ADAMTS15.
                     /evidence=ECO:0000250|UniProtKB:Q62059."
     Site            802
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            805
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            904
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            986
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          1064..1104
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1076..1092
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1284..1315
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1290
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          1293..1309
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1314
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            1435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1453..1478
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1463..1478
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1601
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            1608
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            1633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1660
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1671..1698
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1684
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1738
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1848
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1963
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62059."
     Site            1964
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62059."
     Site            2004
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2074
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            2075
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            2119
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          2166..2187
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2166..2186
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2229..2287
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2233..2249
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2252..2266
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2267..2284
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2409
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2431..2467
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          2433..2467
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Bond            bond(2435,2446)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(2440,2455)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(2457,2466)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2469..2505
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          2469..2505
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(2469,2472,2486)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(2473,2484)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(2478,2493)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(2495,2504)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2511..2634
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Bond            bond(2511,2522)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2518..2632
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(2529,2561..2564,2593,2603,2611,2613,2619,2622,
                     2624..2626)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Region          2535..2539
                     /region_name="Conflict"
                     /note="AEREC -> NSARG (in Ref. 4). /evidence=ECO:0000305."
     Bond            bond(2539,2631)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(2572,2576,2599,2605..2606)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(2576,2606)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(2596,2598,2605,2619..2620)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Bond            bond(2607,2623)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2636..2696
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          2638..2694
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(2638,2681)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(2648,2668)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(2667,2694)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2697..2738
                     /region_name="Splicing variant"
                     /note="PSAYQRTYSKKYLKNSSSVKDNSINTSKHEHRWSRRWQETRR ->
                     RKWSFRKNGQPCFNKY (in isoform Vint).
                     /evidence=ECO:0000303|PubMed:10397680. /id=VSP_003092."
     Site            2711
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2714..2738
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2720..2738
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
ORIGIN
        1 mlinmngilw mcstllltha lhkakmeenp pvkgslsgkv ilpchfstlp tlppdyntse
       61 flrikwskie vdkngkdike ttvlvaqdgn ikigqdykgr vsvpthpddv gdasltmvkl
      121 rasdagvyrc dvmygiedtq ntmslavdgv vfhyraatsr ytlnfesaqq acldigavia
      181 tpeqlfaaye dgfeqcdagw lsdqtvrypi rapregcygd mmgkegvrty gfrspqetyd
      241 vycyvdhldg dvfhitapsk ftfeeaeaec anrdarlatv gelhaawrng fdqcdygwls
      301 dasvrhpvtv araqcgggll gvrtlyrfen qtcfplpdsr fdaycfkrsp lsiipktews
      361 vsetsvpled evlgksdqdt leqthleatm spealstiev tqgetqeepq tpgipfpals
      421 stavmtkett afeeegegst ytlsedrlmt dseivpslet tpvgtsypgg amtqqevemd
      481 tmvtqmssir ptvvlstepe vsyeaegssp mefastlkpf gtqvtqlvee tteegkktpl
      541 dytdlgsglf eqprvtelpd fsmtpsdisv ftaidslhrt tplrppspft eephifekep
      601 sekttgdiil presvtqhpl ttlmdiiakk tesdidheyh mtskppvmqp trpsvverkt
      661 tskpqelsts pppagtkfhp dinvyiievr enktgrmsdm vvnghpidse skeeepcsee
      721 tdplhdlfae ilpelpdsfe idiyhseede dgeedcvnat dvtttpsvqy itgkphvttv
      781 pknpeaaear rglyesvaps qnfsntsatd thqfipaete lsttmqftks keatelleit
      841 wkpetypetp ehfssgepdv fptlpshdgk ttkwsefite snpntenpeh kqpkpiplfp
      901 eefsgegaid qasqqtifsr atevalgket dqsptistss irsgsvsvha leedpialtg
      961 isqtdesmst veswvemtps qtvefsgsss aptiegsgev eeytnkifnt vtdlpqrept
     1021 dtlipldmsn imitdhhiyt pattapldsq lpstdarptq fgiqtttsew vsstsfegrk
     1081 teedkerdtn aahtgevqpa tersdrlllt selessnvaa sspldtwegf vpettstvse
     1141 kemanttpvf tetsdvanle tqsfehssss qprvqeeltt lsgkpplifm dlgsgdastd
     1201 mefitassft ldlesdtkvk kelpstlsps vetssssepi glapstvldi eivevmnqts
     1261 kktliselsg kptsqaevrd lypglgedfs gdsseyptvs sttmkeetvg mggsenervk
     1321 dtqtlssipp tsdninpvpd skgfgstvas ttafpweefm tsaegsgeel ssvrssvslv
     1381 lplgvdilpt tespyfdqef eeaaavteag kqsalpiavs gntvdltenr dievnstmsv
     1441 dlpqtmepak lwskpevnpe kqeigsetvt qdkaqgqksf eslhsslape qttlesqsli
     1501 etevqtsyys mlttmktynt neeveeegts iahmstpgpg ikglesypth peatgksysf
     1561 sasalvtesg parsvvmdss tqeeesiklf qkdmilthke snsdlsfsgl gsgealpplp
     1621 ttsvsltdmg kinstlypet shmeslgtsi lgdnhermkn vsnevrtlis etgsisqdst
     1681 eapnttlsdt rteesttspl pfmklmdteh spkqtlrwee eiqthrpqtm tgqmtndnss
     1741 vseaeaaats apaflpetys vemtkafats psqtsdlfda nsgegsgevd gldlvytsrt
     1801 tqassqgdsm fashgfiekh pevsrtetga tdgsptasam flhqseynes slyptstlps
     1861 tvtyespseg iadglqdhir fevstlkpsr rkatesviid ldkedskdlg laitesaive
     1921 ilpeltsdrn iiididhtkp vyeyipgiqt dldsdiplgs hgsseeslev qekyeatinl
     1981 spteeafdgs gdalpaghtq aiynesvtps dgkqpedisf sfatgipvss tetelntffp
     2041 tvstlhipsk lttaspeidk pnieaisldd ifesstlsdg qaiadqsevi stlghlektq
     2101 eeyeekkygg psfqpeffsg vgevftdapa yvsigrtysv aqpltefpnv vgqsdsthyt
     2161 eatsavssvt elspqtpssp spvyidsgvs eftevphksa qpaptaassq kliegsfkkv
     2221 ranieatiks lgendhgtes psmspspald iseddskpkl ledletsptk tetsqdspnk
     2281 andqipgkta gilagiktte sgpvvtaadd melgdatqrp hsasapaafr vetsmvpqpi
     2341 pqeperptfp sleinhetht slfeesilat sekqvsqril dysnqatvst ldlntehsip
     2401 pfsildnsne tafligisee tvegtavylp gpdlcktnpc lnggtcypte tsyvctcapg
     2461 ysgdqceldf dechsnpcrn gatcvdglnt frclclpsyv galceqdtet cdygwhkfqg
     2521 qcykyfahrr twdaaerecr lqgahltsil sheeqmfvnr vghdyqwigl ndkmfehdfr
     2581 wtdgsalqye nwrpnqpdsf fsagedcvvi iwhengqwnd vpcnyhltyt ckkgtvacgq
     2641 ppvvenaktf gkmkpryein sliryhckdg fiqrhlptir clgngrwamp kitcmnpsay
     2701 qrtyskkylk nsssvkdnsi ntskhehrws rrwqetrr
//
LOCUS       CLC6A_HUMAN              209 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 6 member A; AltName:
            Full=C-type lectin superfamily member 10; AltName: Full=Dendritic
            cell-associated C-type lectin 2; Short=DC-associated C-type lectin
            2; Short=Dectin-2.
ACCESSION   Q6EIG7
VERSION     Q6EIG7.1
DBSOURCE    UniProtKB: locus CLC6A_HUMAN, accession Q6EIG7;
            class: standard.
            extra accessions:A2RUK3
            created: Feb 15, 2005.
            sequence updated: Aug 16, 2004.
            annotation updated: Sep 13, 2023.
            xrefs: AY365135.1, AAR13071.1, AY321309.1, AAQ83725.1, AC092746.9,
            AC092865.10, BC132933.1, AAI32934.1, BC132935.1, AAI32936.1,
            NP_001007034.1, NP_001304928.1, 5VYB_A
            xrefs (non-sequence databases): CCDS:CCDS31739.1, PDBsum:5VYB,
            AlphaFoldDB:Q6EIG7, SMR:Q6EIG7, STRING:9606.ENSP00000371505,
            ChEMBL:CHEMBL2176856, UniLectin:Q6EIG7, GlyCosmos:Q6EIG7,
            GlyGen:Q6EIG7, iPTMnet:Q6EIG7, PhosphoSitePlus:Q6EIG7,
            BioMuta:CLEC6A, DMDM:59797926, PaxDb:Q6EIG7, PeptideAtlas:Q6EIG7,
            Antibodypedia:23055, DNASU:93978, Ensembl:ENST00000382073.4,
            Ensembl:ENSP00000371505.3, Ensembl:ENSG00000205846.4, GeneID:93978,
            KEGG:hsa:93978, MANE-Select:ENST00000382073.4, UCSC:uc001qum.2,
            AGR:HGNC:14556, CTD:93978, DisGeNET:93978, GeneCards:CLEC6A,
            HGNC:14556, HPA:ENSG00000205846, MIM:613579, neXtProt:NX_Q6EIG7,
            OpenTargets:ENSG00000205846, PharmGKB:PA26579,
            VEuPathDB:HostDB:ENSG00000205846, eggNOG:KOG4297,
            GeneTree:ENSGT00940000162938, HOGENOM:CLU_049894_7_5_1,
            InParanoid:Q6EIG7, OMA:TYHFTYG, OrthoDB:2881452at2759,
            PhylomeDB:Q6EIG7, TreeFam:TF333341, PathwayCommons:Q6EIG7,
            Reactome:R-HSA-5621480, SignaLink:Q6EIG7, BioGRID-ORCS:93978,
            ChiTaRS:CLEC6A, GenomeRNAi:93978, Pharos:Q6EIG7, PRO:PR:Q6EIG7,
            Proteomes:UP000005640, RNAct:Q6EIG7, Bgee:ENSG00000205846,
            GO:0009897, GO:0005886, GO:0005509, GO:0030246, GO:0005537,
            GO:0038187, GO:0043274, GO:0002250, GO:0061760, GO:0050832,
            GO:0001879, GO:0045087, GO:0001819, GO:0043123, GO:1902533,
            GO:0050731, GO:2000318, GO:0001878, GO:0002223, CDD:cd03590,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR033989, InterPro:IPR016187, PANTHER:PTHR46784,
            PANTHER:PTHR46784:SF1, Pfam:PF00059, SMART:SM00034,
            SUPFAM:SSF56436, PROSITE:PS50041
KEYWORDS    3D-structure; Adaptive immunity; Alternative splicing; Calcium;
            Cell membrane; Disulfide bond; Glycoprotein; Immunity; Innate
            immunity; Lectin; Membrane; Metal-binding; Reference proteome;
            Signal-anchor; Transmembrane; Transmembrane helix.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Flornes,L.M., Bryceson,Y.T., Spurkland,A., Lorentzen,J.C.,
            Dissen,E. and Fossum,S.
  TITLE     Identification of lectin-like receptors expressed by antigen
            presenting cells and neutrophils and their mapping to a novel gene
            complex
  JOURNAL   Immunogenetics 56 (7), 506-517 (2004)
   PUBMED   15368084
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Kanazawa,N., Tashiro,K., Inaba,K., Lutz,M.B. and Miyachi,Y.
  TITLE     Molecular cloning of human dectin-2
  JOURNAL   J Invest Dermatol 122 (6), 1522-1524 (2004)
   PUBMED   15175046
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.;
            TISSUE=Spleen
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Scherer,S.E., Muzny,D.M., Buhay,C.J., Chen,R., Cree,A., Ding,Y.,
            Dugan-Rocha,S., Gill,R., Gunaratne,P., Harris,R.A., Hawes,A.C.,
            Hernandez,J., Hodgson,A.V., Hume,J., Jackson,A., Khan,Z.M.,
            Kovar-Smith,C., Lewis,L.R., Lozado,R.J., Metzker,M.L.,
            Milosavljevic,A., Miner,G.R., Montgomery,K.T., Morgan,M.B.,
            Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z., Steffen,D.,
            Lovering,R.C., Wheeler,D.A., Worley,K.C., Yuan,Y., Zhang,Z.,
            Adams,C.Q., Ansari-Lari,M.A., Ayele,M., Brown,M.J., Chen,G.,
            Chen,Z., Clerc-Blankenburg,K.P., Davis,C., Delgado,O., Dinh,H.H.,
            Draper,H., Gonzalez-Garay,M.L., Havlak,P., Jackson,L.R.,
            Jacob,L.S., Kelly,S.H., Li,L., Li,Z., Liu,J., Liu,W., Lu,J.,
            Maheshwari,M., Nguyen,B.V., Okwuonu,G.O., Pasternak,S., Perez,L.M.,
            Plopper,F.J., Santibanez,J., Shen,H., Tabor,P.E., Verduzco,D.,
            Waldron,L., Wang,Q., Williams,G.A., Zhang,J., Zhou,J., Allen,C.C.,
            Amin,A.G., Anyalebechi,V., Bailey,M., Barbaria,J.A., Bimage,K.E.,
            Bryant,N.P., Burch,P.E., Burkett,C.E., Burrell,K.L., Calderon,E.,
            Cardenas,V., Carter,K., Casias,K., Cavazos,I., Cavazos,S.R.,
            Ceasar,H., Chacko,J., Chan,S.N., Chavez,D., Christopoulos,C.,
            Chu,J., Cockrell,R., Cox,C.D., Dang,M., Dathorne,S.R., David,R.,
            Davis,C.M., Davy-Carroll,L., Deshazo,D.R., Donlin,J.E., D'Souza,L.,
            Eaves,K.A., Egan,A., Emery-Cohen,A.J., Escotto,M., Flagg,N.,
            Forbes,L.D., Gabisi,A.M., Garza,M., Hamilton,C., Henderson,N.,
            Hernandez,O., Hines,S., Hogues,M.E., Huang,M., Idlebird,D.G.,
            Johnson,R., Jolivet,A., Jones,S., Kagan,R., King,L.M., Leal,B.,
            Lebow,H., Lee,S., LeVan,J.M., Lewis,L.C., London,P.,
            Lorensuhewa,L.M., Loulseged,H., Lovett,D.A., Lucier,A.,
            Lucier,R.L., Ma,J., Madu,R.C., Mapua,P., Martindale,A.D.,
            Martinez,E., Massey,E., Mawhiney,S., Meador,M.G., Mendez,S.,
            Mercado,C., Mercado,I.C., Merritt,C.E., Miner,Z.L., Minja,E.,
            Mitchell,T., Mohabbat,F., Mohabbat,K., Montgomery,B., Moore,N.,
            Morris,S., Munidasa,M., Ngo,R.N., Nguyen,N.B., Nickerson,E.,
            Nwaokelemeh,O.O., Nwokenkwo,S., Obregon,M., Oguh,M., Oragunye,N.,
            Oviedo,R.J., Parish,B.J., Parker,D.N., Parrish,J., Parks,K.L.,
            Paul,H.A., Payton,B.A., Perez,A., Perrin,W., Pickens,A.,
            Primus,E.L., Pu,L.L., Puazo,M., Quiles,M.M., Quiroz,J.B.,
            Rabata,D., Reeves,K., Ruiz,S.J., Shao,H., Sisson,I., Sonaike,T.,
            Sorelle,R.P., Sutton,A.E., Svatek,A.F., Svetz,L.A., Tamerisa,K.S.,
            Taylor,T.R., Teague,B., Thomas,N., Thorn,R.D., Trejos,Z.Y.,
            Trevino,B.K., Ukegbu,O.N., Urban,J.B., Vasquez,L.I., Vera,V.A.,
            Villasana,D.M., Wang,L., Ward-Moore,S., Warren,J.T., Wei,X.,
            White,F., Williamson,A.L., Wleczyk,R., Wooden,H.S., Wooden,S.H.,
            Yen,J., Yoon,L., Yoon,V., Zorrilla,S.E., Nelson,D.,
            Kucherlapati,R., Weinstock,G. and Gibbs,R.A.
  CONSRTM   Baylor College of Medicine Human Genome Sequencing Center Sequence
            Production Team
  TITLE     The finished DNA sequence of human chromosome 12
  JOURNAL   Nature 440 (7082), 346-351 (2006)
   PUBMED   16541075
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Gavino,A.C., Chung,J.S., Sato,K., Ariizumi,K. and Cruz,P.D. Jr.
  TITLE     Identification and expression profiling of a human C-type lectin,
            structurally homologous to mouse dectin-2
  JOURNAL   Exp Dermatol 14 (4), 281-288 (2005)
   PUBMED   15810886
  REMARK    TISSUE SPECIFICITY, INDUCTION, AND ALTERNATIVE SPLICING (ISOFORM
            2).
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Zhu,L.L., Zhao,X.Q., Jiang,C., You,Y., Chen,X.P., Jiang,Y.Y.,
            Jia,X.M. and Lin,X.
  TITLE     C-type lectin receptors Dectin-3 and Dectin-2 form a heterodimeric
            pattern-recognition receptor for host defense against fungal
            infection
  JOURNAL   Immunity 39 (2), 324-334 (2013)
   PUBMED   23911656
  REMARK    FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLEC6A.
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Feinberg,H., Jegouzo,S.A.F., Rex,M.J., Drickamer,K., Weis,W.I. and
            Taylor,M.E.
  TITLE     Mechanism of pathogen recognition by human dectin-2
  JOURNAL   J Biol Chem 292 (32), 13402-13414 (2017)
   PUBMED   28652405
  REMARK    X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 64-209 IN COMPLEX WITH
            HIGH-MANNOSE CARBOHYDRATE AND CALCIUM, DISULFIDE BOND, AND
            FUNCTION.
COMMENT     [FUNCTION] Calcium-dependent lectin that acts as a pattern
            recognition receptor (PRR) of the innate immune system:
            specifically recognizes and binds alpha-mannans on C.albicans
            hypheas (PubMed:23911656, PubMed:28652405). Binding of C.albicans
            alpha-mannans to this receptor complex leads to phosphorylation of
            the immunoreceptor tyrosine-based activation motif (ITAM) of
            FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B,
            consequently driving maturation of antigen-presenting cells and
            shaping antigen-specific priming of T-cells toward effector
            T-helper 1 and T-helper 17 cell subtypes (By similarity).
            Recognizes also, in a mannose-dependent manner, allergens from
            house dust mite and fungi, by promoting cysteinyl leukotriene
            production (By similarity). Recognizes soluble elements from the
            eggs of Shistosoma mansoni altering adaptive immune responses (By
            similarity). {ECO:0000250|UniProtKB:Q9JKF4,
            ECO:0000269|PubMed:23911656, ECO:0000269|PubMed:28652405}.
            [SUBUNIT] Associated with FCER1G (By similarity). Heterodimer with
            CLEC4D; this heterodimer forms a pattern recognition receptor (PRR)
            against fungal infection (PubMed:23911656).
            {ECO:0000250|UniProtKB:Q9JKF4, ECO:0000269|PubMed:23911656}.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000269|PubMed:23911656};
            Single-pass type II membrane protein {ECO:0000305}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1; IsoId=Q6EIG7-1; Sequence=Displayed; Name=2;
            IsoId=Q6EIG7-2; Sequence=VSP_041514.
            [TISSUE SPECIFICITY] Expressed in lung, spleen, lymph node,
            leukocytes, bone marrow, tonsils and dendritic cells. Strongly
            expressed in purified monocytes and weakly in B-cells. In
            peripheral blood cells, preferentially expressed in plasmacytoids
            rather than myeloids. {ECO:0000269|PubMed:15175046,
            ECO:0000269|PubMed:15368084, ECO:0000269|PubMed:15810886}.
            [INDUCTION] Up-regulated by granulocyte-macrophage
            colony-stimulating factor (GM-CSF), TGF-beta 1, TNF-alpha and
            down-regulated by IL-4, IL-10 or UVB in CD14+ monocytes.
            {ECO:0000269|PubMed:15810886}.
            [DOMAIN] A short stretch of the intracellular domain (AA 8-14)
            proximal to the transmembrane domain is required for association
            with Fc receptor gamma chain. {ECO:0000250|UniProtKB:Q9JKF4}.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..209
                     /gene="CLEC6A"
                     /gene_synonym="CLECSF10"
                     /gene_synonym="DECTIN2"
     Protein         1..209
                     /product="C-type lectin domain family 6 member A"
                     /note="C-type lectin superfamily member 10; Dendritic
                     cell-associated C-type lectin 2; DC-associated C-type
                     lectin 2; Dectin-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..209
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 6 member A.
                     /id=PRO_0000046635."
     Region          1..20
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          11..40
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2). /evidence=ECO:0000305.
                     /id=VSP_041514."
     Region          21..41
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          42..209
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          64..68
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Bond            bond(66,78)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000269|PubMed:28652405,
                     ECO:0007744|PDB:5VYB."
     Region          76..80
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Region          79..204
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(79,90)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:28652405, ECO:0007744|PDB:5VYB."
     Region          83..86
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Region          86..203
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          89..98
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Region          100..109
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Bond            bond(107,202)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:28652405, ECO:0007744|PDB:5VYB."
     Region          120..127
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(135,168,170,174,180..181,190..193)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Region          136..141
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Site            order(142,146,174..175)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Region          145..147
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Site            order(146,175)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Site            170
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(176,194)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040,
                     ECO:0000269|PubMed:28652405, ECO:0007744|PDB:5VYB."
     Region          176..182
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Region          183..185
                     /region_name="Hydrogen bonded turn"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Region          186..192
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Region          198..205
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
     Region          207..209
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:5VYB."
ORIGIN
        1 mmqeqqpqst ekrgwlslrl wsvagisial lsacfivscv vtyhftyget gkrlselhsy
       61 hssltcfseg tkvpawgccp aswksfgssc yfisseekvw skseqncvem gahlvvfnte
      121 aeqnfivqql nesfsyflgl sdpqgnnnwq widktpyekn vrfwhlgepn hsaeqcasiv
      181 fwkptgwgwn dvicetrrns icemnkiyl
//
LOCUS       PLCL_MYTGA               156 aa            linear   INV 22-FEB-2023
DEFINITION  RecName: Full=Perlucin-like protein; Flags: Precursor.
ACCESSION   P86854
VERSION     P86854.1
DBSOURCE    UniProtKB: locus PLCL_MYTGA, accession P86854;
            class: standard.
            created: Feb 8, 2011.
            sequence updated: Feb 8, 2011.
            annotation updated: Feb 22, 2023.
            xrefs: AJ624413.1
            xrefs (non-sequence databases): AlphaFoldDB:P86854, SMR:P86854,
            GO:0005576, GO:0030246, CDD:cd03590, Gene3D:3.10.100.10,
            InterPro:IPR001304, InterPro:IPR016186, InterPro:IPR018378,
            InterPro:IPR033989, InterPro:IPR016187, PANTHER:PTHR22803:SF124,
            PANTHER:PTHR22803, Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Direct protein sequencing; Disulfide bond; Lectin; Secreted;
            Signal.
SOURCE      Mytilus galloprovincialis (Mediterranean mussel)
  ORGANISM  Mytilus galloprovincialis
            Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
            Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae;
            Mytilinae; Mytilus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Venier,P., De Pitta,C., Pallavicini,A., Marsano,F., Varotto,L.,
            Romualdi,C., Dondero,F., Viarengo,A. and Lanfranchi,G.
  TITLE     Development of mussel mRNA profiling: Can gene expression trends
            reveal coastal water pollution?
  JOURNAL   Mutat Res 602 (1-2), 121-134 (2006)
   PUBMED   17010391
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Marie,B., Le Roy,N., Zanella-Cleon,I., Becchi,M. and Marin,F.
  TITLE     Molecular evolution of mollusc shell proteins: insights from
            proteomic analysis of the edible mussel Mytilus
  JOURNAL   J Mol Evol 72 (5-6), 531-546 (2011)
   PUBMED   21643827
  REMARK    PROTEIN SEQUENCE OF 57-67 AND 89-99, SUBCELLULAR LOCATION, AND
            TISSUE SPECIFICITY.;
            TISSUE=Shell {ECO:0000269|PubMed:21643827}
COMMENT     [SUBCELLULAR LOCATION] Secreted {ECO:0000269|PubMed:21643827}.
            [TISSUE SPECIFICITY] Component of the organic matrix of calcified
            shell layers like nacre and prisms. {ECO:0000269|PubMed:21643827}.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Mytilus galloprovincialis"
                     /db_xref="taxon:29158"
     Protein         1..156
                     /product="Perlucin-like protein"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          23..156
                     /region_name="Mature chain"
                     /note="Perlucin-like protein. /evidence=ECO:0000255.
                     /id=PRO_0000404080."
     Region          30..156
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(30,41)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q07108,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          37..156
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(58,156)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q07108,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(90,122,124,129,135..136,143..146)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(97,101,125,129..130)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(101,130)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Bond            bond(131,147)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q07108,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mgkltvvgil tlfifyivaa sgkctapvnc pagwkkyktn cyffspdgkn whdaakqcqt
       61 mggylvkitd seenswvvdm itksvkhkyg ywmgmadlkn egdwrwvnds savsysnwhr
      121 gqpnnanned cghfwsavny ewndivcntd qmgyic
//
LOCUS       RCAL2_RHEAM              143 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Rheacalcin-2; Short=RCA-2.
ACCESSION   P84618
VERSION     P84618.2
DBSOURCE    UniProtKB: locus RCAL2_RHEAM, accession P84618;
            class: standard.
            created: Aug 30, 2005.
            sequence updated: Feb 7, 2006.
            annotation updated: Feb 22, 2023.
            xrefs (non-sequence databases): AlphaFoldDB:P84618, SMR:P84618,
            iPTMnet:P84618, GO:0005576, GO:0030246, CDD:cd03594,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR016187, PANTHER:PTHR22803, PANTHER:PTHR22803:SF116,
            Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS50041
KEYWORDS    Direct protein sequencing; Disulfide bond; Extracellular matrix;
            Lectin; Phosphoprotein; Secreted.
SOURCE      Rhea americana (greater rhea)
  ORGANISM  Rhea americana
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
            Coelurosauria; Aves; Palaeognathae; Rheiformes; Rheidae; Rhea.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Mann,K. and Siedler,F.
  TITLE     Amino acid sequences and phosphorylation sites of emu and rhea
            eggshell C-type lectin-like proteins
  JOURNAL   Comp. Biochem. Physiol. 143B, 160-170 (2006)
   PUBMED   16403478
  REMARK    PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-66
            AND SER-68.;
            TISSUE=Eggshell matrix
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Mann,K.
  TITLE     Identification of the major proteins of the organic matrix of emu
            (Dromaius novaehollandiae) and rhea (Rhea americana) eggshell
            calcified layer
  JOURNAL   Br Poult Sci 45 (4), 483-490 (2004)
   PUBMED   15484722
  REMARK    PROTEIN SEQUENCE OF 1-30.;
            TISSUE=Eggshell matrix {ECO:0000269|PubMed:15484722}
COMMENT     On Mar 21, 2006 this sequence version replaced gi:73913752.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix. Note=Eggshell matrix.
            [MASS SPECTROMETRY] Mass=16847.2; Method=Electrospray;
            Evidence={ECO:0000269|PubMed:16403478}.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Rhea americana"
                     /db_xref="taxon:8797"
     Protein         1..143
                     /product="Rheacalcin-2"
                     /note="RCA-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..143
                     /region_name="Mature chain"
                     /note="Rheacalcin-2. /id=PRO_0000046719."
     Region          6..141
                     /region_name="CLECT_REG-1_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in Human REG-1 (lithostathine), REG-4, and avian
                     eggshell-specific proteins: ansocalcin,
                     structhiocalcin-1(SCA-1), and -2(SCA-2); cd03594"
                     /db_xref="CDD:153064"
     Bond            bond(6,17)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9PRS8,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          13..140
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(34,139)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9PRS8,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16403478."
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16403478."
     Site            order(112,127..128)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153064"
     Bond            bond(114,131)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250|UniProtKB:Q9PRS8,
                     ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 deqegcasgw vpfdgrcfgf fpqelswrra egfcqrlgar thlasihsee ehqaimsmla
       61 ssqpysesee evadeevwig lhrpmgrrhw ewsdgtkmdy sswyregfpr rracaaleds
      121 tdfaswdtel csdrkpfice yhv
//
LOCUS       C209C_MOUSE              178 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=CD209 antigen-like protein C; AltName:
            Full=DC-SIGN-related protein 2; Short=DC-SIGNR2; AltName:
            CD_antigen=CD209.
ACCESSION   Q91ZW9
VERSION     Q91ZW9.1
DBSOURCE    UniProtKB: locus C209C_MOUSE, accession Q91ZW9;
            class: standard.
            extra accessions:Q0VB37
            created: Apr 13, 2004.
            sequence updated: Dec 1, 2001.
            annotation updated: Sep 13, 2023.
            xrefs: AF373410.1, AAL13236.1, BC120804.1, AAI20805.1, BC132635.1,
            AAI32636.1, BC145088.1, AAI45089.1, NP_570973.1
            xrefs (non-sequence databases): CCDS:CCDS22078.1,
            AlphaFoldDB:Q91ZW9, SMR:Q91ZW9, BioGRID:228434,
            STRING:10090.ENSMUSP00000039861, GlyCosmos:Q91ZW9, GlyGen:Q91ZW9,
            PaxDb:Q91ZW9, DNASU:170776, Ensembl:ENSMUST00000044060,
            Ensembl:ENSMUSP00000039861, Ensembl:ENSMUSG00000040165,
            GeneID:170776, KEGG:mmu:170776, UCSC:uc009ksw.1, AGR:MGI:2157945,
            CTD:170776, MGI:2157945, VEuPathDB:HostDB:ENSMUSG00000040165,
            eggNOG:KOG4297, GeneTree:ENSGT00940000155012,
            HOGENOM:CLU_049894_7_0_1, InParanoid:Q91ZW9, OMA:YWICKKS,
            OrthoDB:3676313at2759, PhylomeDB:Q91ZW9, TreeFam:TF333341,
            BioGRID-ORCS:170776, PRO:PR:Q91ZW9, Proteomes:UP000000589,
            RNAct:Q91ZW9, Bgee:ENSMUSG00000040165, ExpressionAtlas:Q91ZW9,
            Genevisible:Q91ZW9, GO:0009897, GO:0005886, GO:0005537, GO:0046872,
            GO:0001618, GO:0097323, GO:0006955, GO:0042102, GO:1903902,
            GO:0046718, CDD:cd03590, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033989,
            InterPro:IPR016187, PANTHER:PTHR46784, PANTHER:PTHR46784:SF1,
            Pfam:PF00059, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    Calcium; Disulfide bond; Glycoprotein; Lectin; Mannose-binding;
            Metal-binding; Receptor; Reference proteome.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Park,C.G., Takahara,K., Umemoto,E., Yashima,Y., Matsubara,K.,
            Matsuda,Y., Clausen,B.E., Inaba,K. and Steinman,R.M.
  TITLE     Five mouse homologues of the human dendritic cell C-type lectin,
            DC-SIGN
  JOURNAL   Int Immunol 13 (10), 1283-1290 (2001)
   PUBMED   11581173
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=C57BL/6J
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Brain
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     On Oct 13, 2009 this sequence version replaced gi:123782700.
            [FUNCTION] Probable pathogen-recognition receptor. May recognize in
            a calcium-dependent manner high mannose N-linked oligosaccharides
            in a variety of pathogen antigens.
            [CAUTION] In mouse, 5 genes homologous to human CD209/DC-SIGN and
            CD209L/DC-SIGNR have been identified. {ECO:0000305}.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=SIGNR2;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_163'.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..178
                     /gene="Cd209c"
     Protein         1..178
                     /product="CD209 antigen-like protein C"
                     /note="DC-SIGN-related protein 2; DC-SIGNR2"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..178
                     /region_name="Mature chain"
                     /note="CD209 antigen-like protein C. /id=PRO_0000046606."
     Region          48..170
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(48,59)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          54..169
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(76,168)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(104,138,140,145,151..152,156..159)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(111,115,141,145..146)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(115,146)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Bond            bond(147,160)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mrmhtrlqfl krvsnvaysh gqeqakkekv ykemtqlksq inrlcrpcpw dwtvfqgncy
       61 ffskfqqnwn dsvnacrkld aqlvviksdd eqsflqqtsk ekgyawmgls dlkhegrwhw
      121 vdgshllfsf mkywnkgepn neweedcaef rgdgwndapc tikkywickk samsctek
//
LOCUS       ASGR2_RAT                301 aa            linear   ROD 28-JUN-2023
DEFINITION  RecName: Full=Asialoglycoprotein receptor 2; Short=ASGP-R 2;
            Short=ASGPR 2; AltName: Full=Hepatic lectin R2/3; Short=HL-2;
            Short=rHL-2.
ACCESSION   P08290
VERSION     P08290.4
DBSOURCE    UniProtKB: locus ASGR2_RAT, accession P08290;
            class: standard.
            extra accessions:Q5M8C9
            created: Aug 1, 1988.
            sequence updated: May 1, 2007.
            annotation updated: Jun 28, 2023.
            xrefs: M16347.1, AAA42038.1, J02762.1, AAA41522.1, X07636.1,
            CAA30476.1, BC088099.1, AAH88099.1, LNRT2, NP_058885.1,
            XP_006246738.1
            xrefs (non-sequence databases): AlphaFoldDB:P08290, SMR:P08290,
            IntAct:P08290, STRING:10116.ENSRNOP00000060474, GlyCosmos:P08290,
            GlyGen:P08290, iPTMnet:P08290, PhosphoSitePlus:P08290,
            SwissPalm:P08290, PaxDb:P08290, Ensembl:ENSRNOT00000065370,
            Ensembl:ENSRNOP00000060474, Ensembl:ENSRNOG00000030726,
            GeneID:29403, KEGG:rno:29403, UCSC:RGD:2161, AGR:RGD:2161, CTD:433,
            RGD:2161, eggNOG:KOG4297, GeneTree:ENSGT00940000162310,
            HOGENOM:CLU_049894_2_0_1, InParanoid:P08290, OMA:RTLTCQM,
            OrthoDB:3991783at2759, PhylomeDB:P08290, TreeFam:TF352155,
            Reactome:R-RNO-446203, PRO:PR:P08290, Proteomes:UP000002494,
            Bgee:ENSRNOG00000030726, ExpressionAtlas:P08290,
            Genevisible:P08290, GO:0044322, GO:0009897, GO:0048471, GO:0042806,
            GO:0005537, GO:0030282, GO:0006897, GO:0009100, GO:0055088,
            GO:0031647, CDD:cd03590, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033989,
            InterPro:IPR016187, PANTHER:PTHR22802:SF433, PANTHER:PTHR22802,
            Pfam:PF00059, Pfam:PF03954, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Calcium; Direct protein sequencing; Disulfide bond; Endocytosis;
            Glycoprotein; Lectin; Lipoprotein; Membrane; Palmitate;
            Phosphoprotein; Receptor; Reference proteome; Signal-anchor;
            Transmembrane; Transmembrane helix.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   McPhaul,M. and Berg,P.
  TITLE     Identification and characterization of cDNA clones encoding two
            homologous proteins that are part of the asialoglycoprotein
            receptor
  JOURNAL   Mol Cell Biol 7 (5), 1841-1847 (1987)
   PUBMED   3600647
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Halberg,D.F., Wager,R.E., Farrell,D.C., Hildreth,J. IV,
            Quesenberry,M.S., Loeb,J.A., Holland,E.C. and Drickamer,K.
  TITLE     Major and minor forms of the rat liver asialoglycoprotein receptor
            are independent galactose-binding proteins. Primary structure and
            glycosylation heterogeneity of minor receptor forms
  JOURNAL   J Biol Chem 262 (20), 9828-9838 (1987)
   PUBMED   3597443
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Sanford,J.P., Elliott,R.W. and Doyle,D.
  TITLE     Asialoglycoprotein receptor genes are linked on chromosome 11 in
            the mouse
  JOURNAL   DNA 7 (10), 721-728 (1988)
   PUBMED   3234178
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=Sprague-Dawley; TISSUE=Liver
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Liver
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Drickamer,K., Mamon,J.F., Binns,G. and Leung,J.O.
  TITLE     Primary structure of the rat liver asialoglycoprotein receptor.
            Structural evidence for multiple polypeptide species
  JOURNAL   J Biol Chem 259 (2), 770-778 (1984)
   PUBMED   6319386
  REMARK    PROTEIN SEQUENCE OF 201-301.
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Zeng,F.Y. and Weigel,P.H.
  TITLE     Fatty acylation of the rat and human asialoglycoprotein receptors.
            A conserved cytoplasmic cysteine residue is acylated in all
            receptor subunits
  JOURNAL   J Biol Chem 271 (50), 32454-32460 (1996)
   PUBMED   8943311
  REMARK    PALMITOYLATION AT CYS-54.
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Lundby,A., Secher,A., Lage,K., Nordsborg,N.B., Dmytriyev,A.,
            Lundby,C. and Olsen,J.V.
  TITLE     Quantitative maps of protein phosphorylation sites across 14
            different rat organs and tissues
  JOURNAL   Nat Commun 3, 876 (2012)
   PUBMED   22673903
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
            Publication Status: Online-Only
COMMENT     On or before May 9, 2007 this sequence version replaced
            gi:81886218, gi:126136.
            [FUNCTION] Mediates the endocytosis of plasma glycoproteins to
            which the terminal sialic acid residue on their complex
            carbohydrate moieties has been removed. The receptor recognizes
            terminal galactose and N-acetylgalactosamine units. After ligand
            binding to the receptor, the resulting complex is internalized and
            transported to a sorting organelle, where receptor and ligand are
            disassociated. The receptor then returns to the cell membrane
            surface.
            [SUBUNIT] Interacts with LASS2. {ECO:0000250}.
            [SUBCELLULAR LOCATION] Membrane; Single-pass type II membrane
            protein.
            [TISSUE SPECIFICITY] Expressed exclusively in hepatic parenchymal
            cells.
            [MISCELLANEOUS] Calcium is required for ligand binding.
            [MISCELLANEOUS] Two types of rat hepatic lectin have been
            identified, RHL-1 and RHL-2/3, having a relative abundance of 4:1.
            RHL-2 and RHL-3 only differs in their carbohydrate structures.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Hepatic asialoglycoprotein receptor subunit 2/3;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_rat_Ctlect_357'.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..301
                     /gene="Asgr2"
                     /gene_synonym="Asgr-2"
     Protein         1..301
                     /product="Asialoglycoprotein receptor 2"
                     /note="ASGP-R 2; ASGPR 2; Hepatic lectin R2/3; HL-2;
                     rHL-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..301
                     /region_name="Mature chain"
                     /note="Asialoglycoprotein receptor 2. /id=PRO_0000046656."
     Region          1..58
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          1..29
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1..24
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          4..162
                     /region_name="Lectin_N"
                     /note="Hepatic lectin, N-terminal domain; pfam03954"
                     /db_xref="CDD:427612"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903."
     Site            54
                     /site_type="lipid-binding"
                     /note="S-palmitoyl cysteine.
                     /evidence=ECO:0000269|PubMed:8943311."
     Region          59..79
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          80..301
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine."
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine."
     Region          153
                     /region_name="Conflict"
                     /note="R -> A (in Ref. 1; AAA42038).
                     /evidence=ECO:0000305."
     Site            165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine."
     Region          169..295
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          170..295
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(170,181)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(198,293)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          202
                     /region_name="Conflict"
                     /note="N -> I (in Ref. 1; AAA42038).
                     /evidence=ECO:0000305."
     Site            order(225,256,258,269,275..276,281..284)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(232,234,259,269..270)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(234,270)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Region          260
                     /region_name="Conflict"
                     /note="W -> C (in Ref. 1; AAA42038 and 5; AA sequence).
                     /evidence=ECO:0000305."
     Bond            bond(271,285)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          282..283
                     /region_name="Conflict"
                     /note="DN -> ND (in Ref. 5; AA sequence).
                     /evidence=ECO:0000305."
ORIGIN
        1 mekdfqdiqq ldseendhql igdeeqgshv qnlrtenprw ggqppsrpfp qrlcskfrls
       61 llalafnill lvvicvvssq smqlqkefwt lketlsnfst ttlmefkald shggsrndnl
      121 tswetilekk qkdikadhst llfhlkhfpl dlrtltcqla fflsngtecc pvnwvefggs
      181 cywfsrdglt waeadqycqm enahllvins reeqefvvkh rgafhiwigl tdkdgswkwv
      241 dgteyrsnfk nwaftqpdnw qgheeggsed caeilsdglw ndnfcqqvnr wacerkrdit
      301 y
//
LOCUS       CSPG2_BOVIN             3381 aa            linear   MAM 13-SEP-2023
DEFINITION  RecName: Full=Versican core protein; AltName: Full=Chondroitin
            sulfate proteoglycan core protein 2; Short=Chondroitin sulfate
            proteoglycan 2; AltName: Full=Glial hyaluronate-binding protein;
            Short=GHAP; AltName: Full=Large fibroblast proteoglycan; AltName:
            Full=PG-M; Flags: Precursor.
ACCESSION   P81282
VERSION     P81282.2
DBSOURCE    UniProtKB: locus CSPG2_BOVIN, accession P81282;
            class: standard.
            extra accessions:O77609,O77610,O77611,O77612
            created: Dec 15, 1998.
            sequence updated: Sep 26, 2001.
            annotation updated: Sep 13, 2023.
            xrefs: AF060456.1, AAC24358.1, AF060457.1, AAC24359.1, AF060458.1,
            AAC24360.1, AF060459.1, AAC24361.1, T14274, T42389, NP_851378.1,
            XP_015327844.1
            xrefs (non-sequence databases): SMR:P81282,
            STRING:9913.ENSBTAP00000019848, GlyCosmos:P81282, PaxDb:P81282,
            PeptideAtlas:P81282, Ensembl:ENSBTAT00000042717,
            Ensembl:ENSBTAP00000040348, Ensembl:ENSBTAG00000014906,
            GeneID:282662, KEGG:bta:282662, CTD:1462,
            VEuPathDB:HostDB:ENSBTAG00000014906, eggNOG:ENOG502QRBE,
            GeneTree:ENSGT00940000156102, InParanoid:P81282,
            OrthoDB:5323609at2759, Reactome:R-BTA-1971475,
            Reactome:R-BTA-2022870, Reactome:R-BTA-2022923,
            Reactome:R-BTA-2024101, Reactome:R-BTA-3000178,
            Reactome:R-BTA-381426, Reactome:R-BTA-8957275,
            Proteomes:UP000009136, Bgee:ENSBTAG00000014906,
            ExpressionAtlas:P81282, GO:0005576, GO:0005615, GO:0033165,
            GO:0072534, GO:0001750, GO:0045202, GO:0005509, GO:0030246,
            GO:0005540, GO:0007155, GO:0007417, GO:0010001, GO:0002052,
            GO:0001501, CDD:cd00033, CDD:cd03588, CDD:cd00054, CDD:cd05901,
            CDD:cd03517, CDD:cd03520, Gene3D:2.10.70.10, Gene3D:2.60.40.10,
            Gene3D:2.10.25.10, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033987,
            InterPro:IPR016187, InterPro:IPR001881, InterPro:IPR000742,
            InterPro:IPR000152, InterPro:IPR018097, InterPro:IPR007110,
            InterPro:IPR036179, InterPro:IPR013783, InterPro:IPR003599,
            InterPro:IPR013106, InterPro:IPR000538, InterPro:IPR035976,
            InterPro:IPR000436, PANTHER:PTHR22804, PANTHER:PTHR22804:SF57,
            Pfam:PF00008, Pfam:PF00059, Pfam:PF00084, Pfam:PF07686,
            Pfam:PF00193, PRINTS:PR01265, SMART:SM00032, SMART:SM00034,
            SMART:SM00181, SMART:SM00179, SMART:SM00409, SMART:SM00406,
            SMART:SM00445, SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF57196,
            SUPFAM:SSF48726, PROSITE:PS00010, PROSITE:PS00615, PROSITE:PS50041,
            PROSITE:PS00022, PROSITE:PS01186, PROSITE:PS50026, PROSITE:PS01187,
            PROSITE:PS50835, PROSITE:PS01241, PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Alternative splicing; Calcium; Cell projection; Direct protein
            sequencing; Disulfide bond; EGF-like domain; Extracellular matrix;
            Glycoprotein; Hyaluronic acid; Immunoglobulin domain; Lectin;
            Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted;
            Signal; Sushi.
SOURCE      Bos taurus (cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 3381)
  AUTHORS   Schmalfeldt,M., Dours-Zimmermann,M.T., Winterhalter,K.H. and
            Zimmermann,D.R.
  TITLE     Versican V2 is a major extracellular matrix component of the mature
            bovine brain
  JOURNAL   J Biol Chem 273 (25), 15758-15764 (1998)
   PUBMED   9624174
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0; V1; V2 AND V3).;
            TISSUE=Forebrain
REFERENCE   2  (residues 1 to 3381)
  AUTHORS   Perides,G., Biviano,F. and Bignami,A.
  TITLE     Interaction of a brain extracellular matrix protein with hyaluronic
            acid
  JOURNAL   Biochim Biophys Acta 1075 (3), 248-258 (1991)
   PUBMED   1720020
  REMARK    PROTEIN SEQUENCE OF 21-53; 78-96; 226-250; 262-277; 295-306;
            314-324; 329-331 AND 342-348.;
            TISSUE=Spinal cord
COMMENT     On or before Mar 15, 2005 this sequence version replaced
            gi:7513547, gi:7513546, gi:3914313.
            [FUNCTION] May play a role in intercellular signaling and in
            connecting cells with the extracellular matrix. May take part in
            the regulation of cell motility, growth and differentiation. Binds
            hyaluronic acid.
            [SUBUNIT] Interacts with FBLN1. {ECO:0000250}.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000250|UniProtKB:P13611}. Cell projection, cilium,
            photoreceptor outer segment {ECO:0000250|UniProtKB:P13611}.
            Secreted, extracellular space, extracellular matrix,
            interphotoreceptor matrix {ECO:0000250|UniProtKB:P13611}. Secreted
            {ECO:0000250|UniProtKB:P13611}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=4; Comment=Additional isoforms seem to exist.; Name=V0;
            IsoId=P81282-1; Sequence=Displayed; Name=V1; IsoId=P81282-2;
            Sequence=VSP_003078, VSP_003079; Name=V2; IsoId=P81282-3;
            Sequence=VSP_003080; Name=V3; IsoId=P81282-4; Sequence=VSP_003078,
            VSP_003081.
            [TISSUE SPECIFICITY] Cerebral white matter. Isoform V0 and isoform
            V1 are expressed in the central nervous system, and in a number of
            mesenchymal and epithelial tissues; the major isoform V2 is
            restricted to the central nervous system.
            [DEVELOPMENTAL STAGE] Disappears after the cartilage development.
            [PTM] Phosphorylated by FAM20C in the extracellular medium.
            {ECO:0000250|UniProtKB:P13611}.
            [PTM] Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the
            pericellular matrix surrounding myoblasts, facilitating myoblast
            contact and fusion which is required for skeletal muscle
            development and regeneration. {ECO:0000250|UniProtKB:Q62059}.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..3381
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
     gene            1..3381
                     /gene="VCAN"
                     /gene_synonym="CSPG2"
     Protein         1..3381
                     /product="Versican core protein"
                     /note="Chondroitin sulfate proteoglycan core protein 2;
                     Glial hyaluronate-binding protein; Large fibroblast
                     proteoglycan; PG-M; Chondroitin sulfate proteoglycan 2;
                     GHAP"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..20
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          21..3381
                     /region_name="Mature chain"
                     /note="Versican core protein. /id=PRO_0000017521."
     Region          21..147
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          25
                     /region_name="Conflict"
                     /note="Missing (in Ref. 2; AA sequence).
                     /evidence=ECO:0000305."
     Region          26..153
                     /region_name="Ig_Versican"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), versican;
                     cd05901"
                     /db_xref="CDD:409482"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409482"
     Region          32..34
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409482"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409482"
     Bond            bond(44,131)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          51
                     /region_name="Conflict"
                     /note="Missing (in Ref. 2; AA sequence).
                     /evidence=ECO:0000305."
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          64..70
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409482"
     Region          81..84
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409482"
     Region          89
                     /region_name="Conflict"
                     /note="N -> D (in Ref. 2; AA sequence).
                     /evidence=ECO:0000305."
     Region          96
                     /region_name="Conflict"
                     /note="Q -> D (in Ref. 2; AA sequence).
                     /evidence=ECO:0000305."
     Region          102..107
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409482"
     Region          113..119
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409482"
     Region          127..134
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409482"
     Region          144..153
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409482"
     Region          151..246
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          151..245
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            161..162
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(173,244)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(197,218)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          252..348
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          252..347
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            259..260
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(271,346)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(295,316)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          346
                     /region_name="Conflict"
                     /note="C -> R (in Ref. 2; AA sequence).
                     /evidence=ECO:0000305."
     Region          349..1336
                     /region_name="Region of interest in the sequence"
                     /note="GAG-alpha (glucosaminoglycan attachment domain)."
     Region          349
                     /region_name="Splicing variant"
                     /note="P -> R (in isoform V1 and isoform V3).
                     /evidence=ECO:0000303|PubMed:9624174. /id=VSP_003078."
     Region          350..3074
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V3).
                     /evidence=ECO:0000303|PubMed:9624174. /id=VSP_003081."
     Region          350..1336
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V1).
                     /evidence=ECO:0000303|PubMed:9624174. /id=VSP_003079."
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          417..437
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          603..623
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            660
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          816..866
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            817
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          850..864
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            965
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1017
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1043..1081
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1054..1069
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1218..1244
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1337..3074
                     /region_name="Region of interest in the sequence"
                     /note="GAG-beta."
     Region          1337..3074
                     /region_name="Splicing variant"
                     /note="Missing (in isoform V2).
                     /evidence=ECO:0000303|PubMed:9624174. /id=VSP_003080."
     Region          1338..1362
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1417..1512
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1423..1424
                     /site_type="cleavage"
                     /note="Cleavage; by ADAMTS15.
                     /evidence=ECO:0000250|UniProtKB:Q62059."
     Region          1430..1451
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1463
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            1539
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            1621
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            1653
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          1708..1785
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1724..1785
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1928
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            1952
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          1964..1986
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1974
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2041..2126
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2045..2062
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2045
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2074
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            2240
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            2247
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            2263
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2290
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2338..2388
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2342..2388
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          2490..2512
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2594..2615
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62059."
     Site            2608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62059."
     Site            2612
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Site            2623
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2641
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            2714
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            2715
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            2759
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P13611."
     Region          2819..2893
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2832..2855
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            2919
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            3052
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          3074..3110
                     /region_name="Domain"
                     /note="EGF-like 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Region          3076..3110
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Bond            bond(3078,3089)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3083,3098)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3100,3109)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3112..3148
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          3112..3148
                     /region_name="Domain"
                     /note="EGF-like 2; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(3112,3115,3129)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Bond            bond(3116,3127)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3121,3136)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(3138,3147)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3154..3277
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Bond            bond(3154,3165)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3161..3275
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(3172,3204..3207,3236,3246,3254,3256,3262,3265,
                     3267..3269)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Bond            bond(3182,3274)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(3215,3219,3242,3248..3249)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3219,3249)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3239,3241,3248,3262..3263)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Bond            bond(3250,3266)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          3279..3339
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          3281..3337
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(3281,3324)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(3291,3311)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(3310,3337)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            3354
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          3355..3381
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          3363..3381
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            3364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
ORIGIN
        1 mliniksilw mcstliaaha lqkvnmeksp pvkgslsgkv nlpchfstmp tlppsyntts
       61 eflrikwski eldktgkdlk ettvlvaqng nikigqdykg rvsvpthped vgdasltmvk
      121 llasdagryr cdvmygiedt qdtvsltveg vvfhyraats rytlnfemaq kacvdigavi
      181 atpeqlhaay edgfeqcdag wlsdqtvryp irvpregcyg dmmgkegvrt ygfraphety
      241 dvycyvdhld gdvfhitapn kftfeeagee cktqdarlat vgelqaawrn gfdrcdygwl
      301 ldasvrhpvt varaqcgggl lgvrtlyrfe nqtgfptpds rfdaycfkpk qniseattie
      361 lnmlaetvsp tlleelqvgl drmtpivpli telpvittkv ppignivnfe qkstvqplts
      421 thrsateslp pdgsmkkpwd mdyyspsasg plgepdvsei keevpqsttv vshhapdswd
      481 gvkedlqikd svtqieqiev gplvtsmeis khipskeftv tvtpfvsttm tlesktekka
      541 istvsesvtt shygftlreg dgedristvr sgqstsifsq ipevitvskt sedttrgqle
      601 dvesvsasti vspdsdgspm dhrqekqthg ritegflgqy vsttpfpsqh htevelfpys
      661 gdkrlvegts tvisptprtg rertetlrpa mrtvtytnde iqekitkdss iekieeegfs
      721 gmkfptaspe qihhtkysvg mtksfespal mtttkpgvtp teatdveedf ttpsgletdg
      781 yqdtteyeeg ittvhliqst lnvevvtvsk wsldedntts kplgstehvg spklppalit
      841 ttgvsgkdke mpsltedgrd eftripgstq rpleefteed ttdhekftvr fqpttsiatt
      901 ekstlrdsit eervppftst evrvthatie gsaldegedv dvskplstvp qfahpsdveg
      961 stfvnysstq epttyvdtsh tiplpvipkt ewgvlvpsip segevlgeps qdirvinqth
     1021 feasmypetv rttteitqea tredflwkeq tpekpvspps sttdtakett ppldeqesdg
     1081 saytvfedrs vmgsdrvsvl vttpigkfeq htsfppgavt kaktdevvtl tpttgskvtf
     1141 spwpkqkyet egtsprgfvs pfsigvtqli eetttekrek tsldyidlgs glfekpkate
     1201 lpefstvkat vpsdtaafss adrlhtpsas tekpplidre pdeettsdmv iigestsrvp
     1261 pttledivak ktetdidrey fttsststtq ptrpptvegk eafgpqafst peppagtkfh
     1321 pdinvyiiev renktgrmsd fsvsghpids eskedepcse etdpehdlia eilpellgml
     1381 hseedeedee canatdvttt psvqyingkh vvttvpkdpe aaearrgqfe svapsqnfsd
     1441 ssesdshqfi ithaglptam qpneskette sleitwrpei ypetaepfss gepdifptas
     1501 ihegeategp dsiteknpel dhlvhehaes vplfpeessg daaidqesqk iifsgategt
     1561 fgeeaeksst thtpsmvass vsapvsedas filtgtpqsd eplstveswv eitprhtvef
     1621 sgspsipipe gsgeaeedkd kifamitdls qrnttdprvt sdtskimite slvdvpttti
     1681 ysiseqvsav vptkfvretd tyewvfsppl eettrkeeek gttgtastve vhsptqrldq
     1741 fvspseless setppddsaa atrksftsqm tptqserett sstvvfkete vldnlaaqtt
     1801 dpslssqpgv levsptvpgs pvslfmeqgs geaavdpett tvsslslnie peilakeeaa
     1861 gawspnvetv fpfepteqvl stavdrevae tisqtskenl vseisgepth raeikgfstd
     1921 fpleedfsgd freystvsyp itkeeivmme gsgdaafkdt qmlpsvtpts dlsnhtadse
     1981 epgstlvsts afpweeftas aegsgeplls vsssvdqvfp saagkasgtd spfidqrlge
     2041 egainetdqr stilptaeae stkasteege vkenhtvsmd fpptvepdel wprqevnpvr
     2101 qgngseivse ektqeqesfe plqssvapeq ttfdsqtfpe pglqttgyft lttkktystd
     2161 ermeeevisl advstptlds kglvlyttlp evtekshffl atasvtesvp aesviagsti
     2221 keeesikpfp kvtspiikes dtdlifsglg sgeevlptlg svnfteieqv lstlypltsq
     2281 vqsleasiln dtsgdyegme nvanemrpli sktdsifedg etassttlpe ilsdartegp
     2341 ftapltfstg pgqpqnqthr raeeiqtsrp qpltdqvsse nsvtaetket atpatdflar
     2401 tydlemakgf vtptpkpsdl fyehsgegsg eldavgaevh asgmtqatrq gsttfvsdrs
     2461 lekhpkvpsv eavtvngfpt vsmvlplhpe qregspeatg tpastasyek ategaadsfq
     2521 dhfwgfkdst lkpdkrkate siiidldked kdliltmtes tileiipelt sdkntvidid
     2581 htkpiyedil gmqtdldpev psgppdssee stqvqekyea avnlssteen feasgdilla
     2641 nytqatpesk apedrnpldh tdfifttgip ilsseteldv llptatslpi psksatvnpe
     2701 skteaktled ifesstlsdg qaiadqsevi stlgylertq nedeakkyvs psfqpefssg
     2761 aeealtdptp yvsigttylt aqslteapdv megarlpdsi dtstvsafse llsqtpsfpp
     2821 lsihlgsgds ehsedlqpsa lpstdastpp vssgelanie atfkpsseed fyiteppslp
     2881 pdtepsedes kpklleptea sateliaqee ieifqnsdnt tsvqvsgeav kvfpsietpe
     2941 aeaivtaase tklegatlrp hstsasvihg veagvvpqps pqtserptil spleispetq
     3001 aalirgedst vaapkqqvpt rmldsnkqat lsttelntel atpsfpllet snetsfligi
     3061 neesvegtav ylpgpdrckm npclnggtcy ptetsyvctc vpgysgdrce ldfdechsnp
     3121 crngatcidg fntfrclclp syvgalceqd tetcdygwhk fqgqcykyfa hrrtwdaaer
     3181 ecrlqgahlt silsheeqmf vnrvghdyqw iglndkmfeh dfrwtdgstl qyenwrpnqp
     3241 dsffstgedc vviiwhengq wndvpcnyhl tytckkgtva cgqppvvena ktfgkmkpry
     3301 einsliryhc kdgfiqrhlp tirclgngrw ampkitclnp sayqrtyskk yfknsssakd
     3361 nsintskhdh rwsrrwqesr r
//
LOCUS       CLC4F_RAT                550 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 4 member F; AltName:
            Full=C-type lectin superfamily member 13; Short=C-type lectin 13;
            AltName: Full=Kupffer cell receptor.
ACCESSION   P10716
VERSION     P10716.1
DBSOURCE    UniProtKB: locus CLC4F_RAT, accession P10716;
            class: standard.
            extra accessions:Q4KMB0
            created: Apr 1, 1990.
            sequence updated: Apr 1, 1990.
            annotation updated: Sep 13, 2023.
            xrefs: J03734.1, AAA41472.1, M55532.1, AAA40892.1, BC098661.1,
            AAH98661.1, A28166, NP_446205.1
            xrefs (non-sequence databases): AlphaFoldDB:P10716, SMR:P10716,
            STRING:10116.ENSRNOP00000017643, GlyCosmos:P10716, GlyGen:P10716,
            PaxDb:P10716, Ensembl:ENSRNOT00000017643,
            Ensembl:ENSRNOP00000017643, Ensembl:ENSRNOG00000013137,
            GeneID:114598, KEGG:rno:114598, UCSC:RGD:621062, AGR:RGD:621062,
            CTD:165530, RGD:621062, eggNOG:KOG4297,
            GeneTree:ENSGT01030000234575, HOGENOM:CLU_030099_1_0_1,
            InParanoid:P10716, OMA:LSFQTQM, OrthoDB:4633257at2759,
            PhylomeDB:P10716, TreeFam:TF333341, PRO:PR:P10716,
            Proteomes:UP000002494, Bgee:ENSRNOG00000013137, Genevisible:P10716,
            GO:0009897, GO:0005886, GO:0030246, GO:0005534, GO:0051861,
            GO:0006897, GO:0051132, GO:0010628, CDD:cd03590, Gene3D:1.20.5.170,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033989, InterPro:IPR016187,
            PANTHER:PTHR22801, PANTHER:PTHR22801:SF61, Pfam:PF00059,
            SMART:SM00034, SUPFAM:SSF56436, SUPFAM:SSF57997, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    Direct protein sequencing; Disulfide bond; Endocytosis;
            Glycoprotein; Lectin; Membrane; Receptor; Reference proteome;
            Signal-anchor; Transmembrane; Transmembrane helix.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Hoyle,G.W. and Hill,R.L.
  TITLE     Molecular cloning and sequencing of a cDNA for a carbohydrate
            binding receptor unique to rat Kupffer cells
  JOURNAL   J Biol Chem 263 (16), 7487-7492 (1988)
   PUBMED   2836387
  REMARK    NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 83-104.
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Hoyle,G.W. and Hill,R.L.
  TITLE     Structure of the gene for a carbohydrate-binding receptor unique to
            rat kupffer cells
  JOURNAL   J Biol Chem 266 (3), 1850-1857 (1991)
   PUBMED   1846367
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA].
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Thymus
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     On or before May 9, 2007 this sequence version replaced
            gi:123782133, gi:92446.
            [FUNCTION] Receptor with an affinity for galactose and fucose.
            Could be involved in endocytosis.
            [SUBCELLULAR LOCATION] Membrane; Single-pass type II membrane
            protein.
            [TISSUE SPECIFICITY] Kupffer cells.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Kupffer cell receptor;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_rat_Ctlect_367'.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
     gene            1..550
                     /gene="Clec4f"
                     /gene_synonym="Clecsf13"
                     /gene_synonym="Kclr"
     Protein         1..550
                     /product="C-type lectin domain family 4 member F"
                     /note="C-type lectin superfamily member 13; Kupffer cell
                     receptor; C-type lectin 13"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..550
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 4 member F.
                     /id=PRO_0000046624."
     Region          1..42
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          43..69
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          70..550
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          <100..390
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            255
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          414..538
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Region          438..538
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(440,536)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(467,502,504,514,524..527)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(474,478,505,514..515)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(478,515)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Bond            bond(516,528)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mkeaelnrdv akfctdnqcv ilqpqglgpk saapmaprtl rhvqaivalv vvtvffslla
       61 lfvvvlqpwr qkqnedhpvk aglhggnysg sdncsqfvrr aemqeaiqsl rasgnsssch
      121 keiqtlkyqm dnvssqvqll gghleeanad iqqakdvlkg tgalasetqa lrsslevasa
      181 dihslrgdle kanamtsqtq gllksstdnt saelhvlgrg leeaqseiqa lrgslqssnd
      241 lgsrtqnflq hsmdnisaei qamrdgmqra geemtslkkd letltaqiqn anghleqtdt
      301 qiqglkaqlk stsslnsqie vvngklkdss relqtlrrdl sdvsalksnv qmlqsnlqka
      361 kaevqslktg leatktlaak iqgqqsdlea lqkavaahtq gqktqnqvlq limqdwkyfn
      421 gkfyyfsrdk kswheaenfc vsqgahlasv tsqeeqaflv qitnavdhwi gltdqgtegn
      481 wrwvdgtpfd yvqsrrfwrk gqpdnwrhgn geredcvhlq rmwndmacgt aynwvckkst
      541 dwsvartdqs
//
LOCUS       PGCA_BOVIN              2364 aa            linear   MAM 13-SEP-2023
DEFINITION  RecName: Full=Aggrecan core protein; AltName:
            Full=Cartilage-specific proteoglycan core protein; Short=CSPCP;
            Flags: Precursor.
ACCESSION   P13608
VERSION     P13608.3
DBSOURCE    UniProtKB: locus PGCA_BOVIN, accession P13608;
            class: standard.
            extra accessions:P79117,Q28159,Q6XL66
            created: Jan 1, 1990.
            sequence updated: Jul 15, 1998.
            annotation updated: Sep 13, 2023.
            xrefs: U76615.1, AAB38524.1, AY226875.1, AAP44492.1, AY226858.1,
            AY226859.1, AY226860.1, AY226861.1, AY226862.1, AY226863.1,
            AY226864.1, AY226865.1, AY226866.1, AY226867.1, AY226868.1,
            AY226871.1, AY226872.1, AY226873.1, AY226874.1, L07053.1, A29164,
            A39808, B29164, S74144, T42630, NP_776406.1
            xrefs (non-sequence databases): AlphaFoldDB:P13608, SMR:P13608,
            IntAct:P13608, STRING:9913.ENSBTAP00000021512, BindingDB:P13608,
            ChEMBL:CHEMBL4295716, GlyCosmos:P13608, PaxDb:P13608,
            PeptideAtlas:P13608, GeneID:280985, KEGG:bta:280985, CTD:176,
            eggNOG:ENOG502QUX8, InParanoid:P13608, OrthoDB:5402504at2759,
            Proteomes:UP000009136, GO:0005576, GO:0005615, GO:0072534,
            GO:0045202, GO:0005509, GO:0030246, GO:0005540, GO:0007155,
            GO:0007417, GO:0010001, GO:0002052, GO:0001501, CDD:cd00033,
            CDD:cd03588, CDD:cd00054, CDD:cd05900, CDD:cd03517, CDD:cd03520,
            Gene3D:2.10.70.10, Gene3D:2.60.40.10, Gene3D:2.10.25.10,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033987, InterPro:IPR016187,
            InterPro:IPR001881, InterPro:IPR000742, InterPro:IPR000152,
            InterPro:IPR018097, InterPro:IPR007110, InterPro:IPR036179,
            InterPro:IPR013783, InterPro:IPR003599, InterPro:IPR013106,
            InterPro:IPR000538, InterPro:IPR035976, InterPro:IPR000436,
            PANTHER:PTHR22804, PANTHER:PTHR22804:SF54, Pfam:PF00008,
            Pfam:PF00059, Pfam:PF00084, Pfam:PF07686, Pfam:PF00193,
            PRINTS:PR01265, SMART:SM00032, SMART:SM00034, SMART:SM00181,
            SMART:SM00179, SMART:SM00409, SMART:SM00406, SMART:SM00445,
            SUPFAM:SSF56436, SUPFAM:SSF57535, SUPFAM:SSF57196, SUPFAM:SSF48726,
            PROSITE:PS00010, PROSITE:PS00615, PROSITE:PS50041, PROSITE:PS00022,
            PROSITE:PS50026, PROSITE:PS01187, PROSITE:PS50835, PROSITE:PS01241,
            PROSITE:PS50963, PROSITE:PS50923
KEYWORDS    Alternative splicing; Calcium; Direct protein sequencing; Disulfide
            bond; EGF-like domain; Extracellular matrix; Glycoprotein;
            Immunoglobulin domain; Lectin; Metal-binding; Proteoglycan;
            Reference proteome; Repeat; Secreted; Signal; Sushi.
SOURCE      Bos taurus (cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 2364)
  AUTHORS   Hering,T.M., Kollar,J. and Huynh,T.D.
  TITLE     Complete coding sequence of bovine aggrecan: comparative structural
            analysis
  JOURNAL   Arch Biochem Biophys 345 (2), 259-270 (1997)
   PUBMED   9308898
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
            Erratum:[Arch Biochem Biophys 1999 Jul 1;367(1):151]
REFERENCE   2  (residues 1 to 2364)
  AUTHORS   Cavanagh,J.A., Tammen,I., Hayden,M.J., Gill,C.A., Nicholas,F.W. and
            Raadsma,H.W.
  TITLE     Characterization of the bovine aggrecan gene: genomic structure and
            physical and linkage mapping
  JOURNAL   Anim Genet 36 (5), 452-454 (2005)
   PUBMED   16167996
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA].
REFERENCE   3  (residues 1 to 2364)
  AUTHORS   Antonsson,P., Heinegard,D. and Oldberg,A.
  TITLE     The keratan sulfate-enriched region of bovine cartilage
            proteoglycan consists of a consecutively repeated hexapeptide motif
  JOURNAL   J Biol Chem 264 (27), 16170-16173 (1989)
   PUBMED   2528543
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 563-1056.
REFERENCE   4  (residues 1 to 2364)
  AUTHORS   Oldberg,A., Antonsson,P. and Heinegard,D.
  TITLE     The partial amino acid sequence of bovine cartilage proteoglycan,
            deduced from a cDNA clone, contains numerous Ser-Gly sequences
            arranged in homologous repeats
  JOURNAL   Biochem J 243 (1), 255-259 (1987)
   PUBMED   3111460
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 1609-2113 AND 2151-2364.
REFERENCE   5  (residues 1 to 2364)
  AUTHORS   Fulop,C., Walcz,E., Valyon,M. and Glant,T.T.
  TITLE     Expression of alternatively spliced epidermal growth factor-like
            domains in aggrecans of different species. Evidence for a novel
            module
  JOURNAL   J Biol Chem 268 (23), 17377-17383 (1993)
   PUBMED   8349621
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] OF 2114-2150 (ISOFORM 1).;
            TISSUE=Cartilage
REFERENCE   6  (residues 1 to 2364)
  AUTHORS   Perin,J.P., Bonnet,F., Jolles,J. and Jolles,P.
  TITLE     Sequence data concerning the protein core of the cartilage
            proteoglycan monomers. Characterization of a sequence allowing the
            synthesis of an oligonucleotide probe
  JOURNAL   FEBS Lett 176 (1), 37-42 (1984)
   PUBMED   6489519
  REMARK    PARTIAL PROTEIN SEQUENCE.
REFERENCE   7  (residues 1 to 2364)
  AUTHORS   Perin,J.P., Bonnet,F. and Jolles,P.
  TITLE     Structural relationship between link proteins and proteoglycan
            monomers
  JOURNAL   FEBS Lett 206 (1), 73-77 (1986)
   PUBMED   3530809
  REMARK    PARTIAL PROTEIN SEQUENCE.
REFERENCE   8  (residues 1 to 2364)
  AUTHORS   Sandy,J.D., Boynton,R.E. and Flannery,C.R.
  TITLE     Analysis of the catabolism of aggrecan in cartilage explants by
            quantitation of peptides from the three globular domains
  JOURNAL   J Biol Chem 266 (13), 8198-8205 (1991)
   PUBMED   2022637
  REMARK    PROTEIN SEQUENCE OF 152-157; 210-230; 482-506; 566-584; 631-641;
            660-684; 2161-2167; 2276-2291; 2298-2307 AND 2318-2334.
COMMENT     On or before Apr 3, 2008 this sequence version replaced
            gi:75072067, gi:89450, gi:89449, gi:7513474, gi:1083074,
            gi:11276915, gi:2506813.
            [FUNCTION] This proteoglycan is a major component of extracellular
            matrix of cartilagenous tissues. A major function of this protein
            is to resist compression in cartilage. It binds avidly to
            hyaluronic acid via an N-terminal globular region. May play a
            regulatory role in the matrix assembly of the cartilage.
            [SUBUNIT] Interacts with FBLN1 and COMP. {ECO:0000250}.
            [INTERACTION] P13608; Q9UNA0: ADAMTS5; Xeno; NbExp=2;
            IntAct=EBI-6259246, EBI-2808663; P13608; P49747: COMP; Xeno;
            NbExp=2; IntAct=EBI-6259246, EBI-2531022.
            [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular
            matrix {ECO:0000250}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1; IsoId=P13608-1; Sequence=Displayed; Name=2;
            IsoId=P13608-2; Sequence=VSP_003072.
            [DOMAIN] Two globular domains, G1 and G2, comprise the N-terminus
            of the proteoglycan, while another globular region, G3, makes up
            the C-terminus. G1 contains Link domains and thus consists of three
            disulfide-bonded loop structures designated as the A, B, B' motifs.
            G2 is similar to G1. The keratan sulfate (KS) and the chondroitin
            sulfate (CS) attachment domains lie between G2 and G3.
            [PTM] Contains mostly chondroitin sulfate, but also N-linked and
            O-linked (about 40) oligosaccharides.
            [PTM] The keratan sulfate contents differ considerably between
            adult and fetal bovine proteoglycans.
            [SIMILARITY] Belongs to the aggrecan/versican proteoglycan family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..2364
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
     gene            1..2364
                     /gene="ACAN"
                     /gene_synonym="AGC1"
     Protein         1..2364
                     /product="Aggrecan core protein"
                     /note="Cartilage-specific proteoglycan core protein;
                     CSPCP"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..16
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          17..2364
                     /region_name="Mature chain"
                     /note="Aggrecan core protein. /id=PRO_0000017502."
     Region          25..147
                     /region_name="Domain"
                     /note="Ig-like V-type."
     Region          33..155
                     /region_name="Ig_Aggrecan"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), aggrecan;
                     cd05900"
                     /db_xref="CDD:409481"
     Region          33..36
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409481"
     Region          39..41
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409481"
     Region          45..53
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409481"
     Bond            bond(51,133)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          72..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409481"
     Region          83..86
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409481"
     Region          104..109
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409481"
     Region          115..121
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409481"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          129..136
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409481"
     Region          146..155
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409481"
     Region          153..248
                     /region_name="Domain"
                     /note="Link 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          153..247
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            163..164
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(175,246)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(199,220)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          254..350
                     /region_name="Domain"
                     /note="Link 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          254..349
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            261..262
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(273,348)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(297,318)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            371
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (keratan sulfate) threonine.
                     /evidence=ECO:0000250."
     Site            376
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (keratan sulfate) threonine.
                     /evidence=ECO:0000250."
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          487..582
                     /region_name="Domain"
                     /note="Link 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          487..581
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            497..498
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Bond            bond(509,580)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(533,554)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          573..576
                     /region_name="Conflict"
                     /note="SETY -> QSET (in Ref. 8; AA sequence).
                     /evidence=ECO:0000305."
     Region          588..684
                     /region_name="Domain"
                     /note="Link 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00323."
     Region          588..683
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan; cd03520"
                     /db_xref="CDD:239597"
     Site            595..596
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Bond            bond(607,682)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            611
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Bond            bond(631,652)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            667
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          <686..971
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          749..1021
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          774..905
                     /region_name="Region of interest in the sequence"
                     /note="22 X 6 AA tandem repeats of
                     E-[EKGV]-[PL]-[FSI]-[PAT]-[STPL]."
     Region          774..779
                     /region_name="Repetitive region"
                     /note="1."
     Region          780..785
                     /region_name="Repetitive region"
                     /note="2."
     Region          786..791
                     /region_name="Repetitive region"
                     /note="3."
     Region          789..897
                     /region_name="Compositionally biased region"
                     /note="Pro residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          792..797
                     /region_name="Repetitive region"
                     /note="4."
     Region          798..803
                     /region_name="Repetitive region"
                     /note="5."
     Region          804..809
                     /region_name="Repetitive region"
                     /note="6."
     Region          810..815
                     /region_name="Repetitive region"
                     /note="7."
     Region          816..821
                     /region_name="Repetitive region"
                     /note="8."
     Region          822..827
                     /region_name="Repetitive region"
                     /note="9."
     Region          828..833
                     /region_name="Repetitive region"
                     /note="10."
     Region          834..839
                     /region_name="Repetitive region"
                     /note="11."
     Region          840..845
                     /region_name="Repetitive region"
                     /note="12."
     Region          846..851
                     /region_name="Repetitive region"
                     /note="13."
     Region          852..857
                     /region_name="Repetitive region"
                     /note="14."
     Region          858..863
                     /region_name="Repetitive region"
                     /note="15."
     Region          864..869
                     /region_name="Repetitive region"
                     /note="16."
     Region          870..875
                     /region_name="Repetitive region"
                     /note="17."
     Region          876..881
                     /region_name="Repetitive region"
                     /note="18."
     Region          882..887
                     /region_name="Repetitive region"
                     /note="19."
     Region          888..893
                     /region_name="Repetitive region"
                     /note="20."
     Region          894..899
                     /region_name="Repetitive region"
                     /note="21."
     Region          900..905
                     /region_name="Repetitive region"
                     /note="22."
     Region          904..918
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          939..974
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1052..1293
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          <1068..>1513
                     /region_name="PRK15319"
                     /note="fibronectin-binding autotransporter adhesin ShdA"
                     /db_xref="CDD:185219"
     Region          1321..1414
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1350
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P16112."
     Site            1387
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P16112."
     Site            1401
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            1407
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            1411
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255."
     Site            1421
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P16112."
     Region          1433..2112
                     /region_name="Region of interest in the sequence"
                     /note="CS-2."
     Region          1435..1466
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            1523
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P16112."
     Region          1528..1550
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1529..1550
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1719..1761
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1719..1733
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1743..1761
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1784..1870
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1818..1832
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          <1822..>2109
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          1839..1869
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1906..2110
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1925..>2063
                     /region_name="PHA03255"
                     /note="BDLF3; Provisional"
                     /db_xref="CDD:165513"
     Region          1954..1973
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2000..2068
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2076..2110
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          2113..2149
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          2113..2149
                     /region_name="Domain"
                     /note="EGF-like; calcium-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00076."
     Site            order(2113,2116,2130)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          2114..2364
                     /region_name="Region of interest in the sequence"
                     /note="G3."
     Region          2114..2150
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:9308898. /id=VSP_003072."
     Bond            bond(2117,2128)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(2122,2137)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Bond            bond(2139,2148)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2154..2277
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Region          2161..2276
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(2172,2204..2207,2236,2246,2254,2256,2262,2265,
                     2267..2269)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Bond            bond(2182,2274)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(2215,2219,2242,2248..2249)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(2219,2249)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(2239,2241,2248,2262..2263)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Bond            bond(2250,2266)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Region          2279..2339
                     /region_name="Domain"
                     /note="Sushi.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00302."
     Region          2281..2337
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Bond            bond(2281,2324)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
     Site            order(2291,2311)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Bond            bond(2310,2337)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000250."
ORIGIN
        1 mttlllvfvt lrvitaaisv evsepdnsls vsipepsplr vllgssltip cyfidpmhpv
       61 ttapstapla prikwsrisk ekevvllvat egrvrvnsay qdkvtlpnyp aipsdatlei
      121 qnmrsndsgi lrcevmhgie dsqatlevvv kgivfhyrai strytldfdr aqraclqnsa
      181 iiatpeqlqa ayedgfhqcd agwladqtvr ypihtpregc ygdkdefpgv rtygirdtne
      241 tydvycfaee megevfyats pekftfqeaa necrrlgarl attgqlylaw qggmdmcsag
      301 wladrsvryp iskarpncgg nllgvrtvyl hanqtgypdp ssrydaicyt gedfvdipes
      361 ffgvggeedi tiqtvtwpdv elplprnite geargsvilt akpdfevspt apepeepftf
      421 vpevratafp evenrteeat rpwafprest pglgaptaft sedlvvqvtl apgaaevpgq
      481 prlpggvvfh yrpgssrysl tfeeakqacl rtgaiiaspe qlqaayeagy eqcdagwlqd
      541 qtvrypivsp rtpcvgdkds spgvrtygvr ppsetydvyc yvdrlegevf fatrleqftf
      601 weaqefcesq natlattgql yaawsrgldk cyagwladgs lrypivtprp acggdkpgvr
      661 tvylypnqtg lldplsrhha fcfrgvsaap speeeegsap tagpdveewm vtqvgpgvaa
      721 vpigeettai pgftvepenk tewelaytpa gtlplpgipp twpptgeate ehtegpsate
      781 vpsasekpfp seepfppeep fpsekpfppe elfpsekpfp sekpfpseep fpsekpfppe
      841 elfpsekpip seepfpseep fpsekpfppe epfpsekpip seepfpsekp fpseepfpse
      901 epstlsapvp srtelpssge vsgvpeisgd ftgsgeisgh ldfsgqpsge sasglpsedl
      961 dssgltstvg sglpvesglp sgeeeritwt sapkvdrlps ggegpevsgv edisglpsgg
     1021 evhleisasg vedisglpsg gevhleisas gvedlsrips gegpeisasg vedisglpsg
     1081 eeghleisas gvedlsgips gegpevsasg vedliglpsg egpevsasgv edlsrlpsge
     1141 gpevsasgve dlsglpsgeg pevsvsgved lsrlpsgegp evsasgvedl srlpsgegpe
     1201 isvsgvedis ilpsgegpev sasgvedlsv lpsgeghlei stsgvedlsv lpsgeghlet
     1261 ssgvedisrl psgegpevsa sgvedlsvlp sgedhleisa sgvedlgvlp sgedhleisa
     1321 sgvedisrlp sgegpevsas gvedlsvlps geghleisas gvedlsrlps ggedhletsa
     1381 sgvgdlsglp sgregleisa sgagdlsglt sgkedltgsa sgaldlgrip svtlgsgqap
     1441 easglpsgfs geysgvdles gpssglpdfs glpsgfptvs lvdttlvevv tattageleg
     1501 rgtidisgag etsglpfsel disggasgls sgaelsgqas gspdisgets glfgvsgqps
     1561 gfpdisgets gllevsgqps gfygeisgvt elsglasgqp eisgeasgil sglgppfgit
     1621 dlsgeapgip dlsgqpsglp efsgtasgip dlvssavsgs gessgitfvd tslvevtptt
     1681 fkeeeglgsv elsglpsgel gvsgtsglad vsglssgaid ssgftsqppe fsglpsgvte
     1741 vsgeasgaes gsslpsgayd ssglpsgfpt vsfvdrtlve svtqaptaqe agegpsgile
     1801 lsgapsgapd msgdhlgsld qsglqsglve psgepastpy fsgdfsgttd vsgessaats
     1861 tsgeasglpe vtlitselve gvteptvsqe lgqrppvtyt pqlfessgea sasgdvprfp
     1921 gsgvevssvp essgetsayp eaevgasaap easggasgsp nlsettstfh eadlegtsgl
     1981 gvsgspsafp egpteglatp evsgesttaf dvsveasgsp satplasgdr tdtsgdlsgh
     2041 tsgldivist tipesewtqq tqrpaearle iessspvhsg eesqtadtat sptdasipas
     2101 aggtddseat ttdideclss pclngatcvd aidsftclcl psyqgdvcei qklceegwtk
     2161 fqghcyrhfp dratwvdaes qcrkqqshls sivtpeeqef vnnnaqdyqw iglndktieg
     2221 dfrwsdghsl qfenwrpnqp dnffatgedc vvmiwhekge wndvpcnyql pftckkgtva
     2281 cgeppvveha rifgqkkdry einalvryqc tegfiqghvp tircqpsghw eepritctdp
     2341 atykrrlqkr ssrplrrshp stah
//
LOCUS       SL_CRODU                 148 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=Snaclec crotocetin; Short=CRC; Flags: Precursor.
ACCESSION   Q719L8
VERSION     Q719L8.1
DBSOURCE    UniProtKB: locus SL_CRODU, accession Q719L8;
            class: standard.
            created: Nov 25, 2008.
            sequence updated: Jul 5, 2004.
            annotation updated: Feb 22, 2023.
            xrefs: AF541884.1, AAQ11365.1
            xrefs (non-sequence databases): AlphaFoldDB:Q719L8, SMR:Q719L8,
            GO:0005576, GO:0090729, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR016187,
            PANTHER:PTHR22803:SF124, PANTHER:PTHR22803, Pfam:PF00059,
            PRINTS:PR01504, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    Disulfide bond; Hemostasis impairing toxin; Secreted; Signal;
            Toxin.
SOURCE      Crotalus durissus terrificus (tropical rattlesnake)
  ORGANISM  Crotalus durissus terrificus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
            Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
            Crotalus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Radis-Baptista,G., Camargo,A.C.M. and Yamane,T.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-AUG-2002) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            TISSUE=Venom gland
COMMENT     [FUNCTION] Interferes with one step of hemostasis (modulation of
            platelet aggregation, or coagulation cascade, for example).
            {ECO:0000250}.
            [SUBUNIT] Heterodimer; disulfide-linked. {ECO:0000250}.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000250}.
            [TISSUE SPECIFICITY] Expressed by the venom gland.
            [MISCELLANEOUS] Shows greater sequence similarity to the beta than
            alpha subunits compared to other heterodimer snaclecs.
            [SIMILARITY] Belongs to the snaclec family. {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Crotalus durissus terrificus"
                     /sub_species="terrificus"
                     /db_xref="taxon:8732"
     Protein         1..148
                     /product="Snaclec crotocetin"
                     /note="CRC"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..23
                     /region_name="Signal"
                     /note="/evidence=ECO:0000250."
     Region          24..148
                     /region_name="Mature chain"
                     /note="Snaclec crotocetin. /id=PRO_0000355262."
     Region          27..145
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Bond            bond(27,38)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          34..145
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(55,144)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(100)
                     /bond_type="disulfide"
                     /note="Interchain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(121,136)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(123,130,132..135,138..140)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
ORIGIN
        1 mgrlvfvsfg llvvflsltg tgagfccplg wssyeghcyk vfkqdmtwed aekfctqqhe
       61 gshlvslqss eevdfvismt apmlklglvw iglsniwnec tlewtngnkv dykawsaepe
      121 civskstdkh wfsrpcskth kvvckfqa
//
LOCUS       CLC10_HUMAN              316 aa            linear   PRI 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 10 member A; AltName:
            Full=C-type lectin superfamily member 14; AltName: Full=Macrophage
            lectin 2; AltName: CD_antigen=CD301.
ACCESSION   Q8IUN9
VERSION     Q8IUN9.1
DBSOURCE    UniProtKB: locus CLC10_HUMAN, accession Q8IUN9;
            class: standard.
            extra accessions:A8K8J8,Q14538,Q6PIW3
            created: Feb 15, 2005.
            sequence updated: Mar 1, 2003.
            annotation updated: Sep 13, 2023.
            xrefs: D50532.1, BAA09101.1, AK292363.1, BAF85052.1, BC027858.1,
            AAH27858.1, BC039011.1, AAH39011.1, NP_006335.2, NP_878910.1,
            6PUV_A, 6PY1_A, 6W12_A, 6XIY_A
            xrefs (non-sequence databases): CCDS:CCDS11087.1, CCDS:CCDS45597.1,
            PDBsum:6PUV, PDBsum:6PY1, PDBsum:6W12, PDBsum:6XIY,
            AlphaFoldDB:Q8IUN9, SMR:Q8IUN9, BioGRID:115725, IntAct:Q8IUN9,
            STRING:9606.ENSP00000254868, UniLectin:Q8IUN9, GlyCosmos:Q8IUN9,
            GlyGen:Q8IUN9, iPTMnet:Q8IUN9, PhosphoSitePlus:Q8IUN9,
            BioMuta:CLEC10A, DMDM:59797948, MassIVE:Q8IUN9, MaxQB:Q8IUN9,
            PaxDb:Q8IUN9, PeptideAtlas:Q8IUN9, Antibodypedia:11754,
            DNASU:10462, Ensembl:ENST00000254868.8, Ensembl:ENSP00000254868.4,
            Ensembl:ENSG00000132514.14, Ensembl:ENST00000571664.1,
            Ensembl:ENSP00000460252.1, Ensembl:ENST00000576617.5,
            Ensembl:ENSP00000458728.1, GeneID:10462, KEGG:hsa:10462,
            UCSC:uc002gej.4, AGR:HGNC:16916, CTD:10462, DisGeNET:10462,
            GeneCards:CLEC10A, HGNC:16916, HPA:ENSG00000132514, MIM:605999,
            neXtProt:NX_Q8IUN9, OpenTargets:ENSG00000132514,
            PharmGKB:PA134975011, VEuPathDB:HostDB:ENSG00000132514,
            eggNOG:KOG4297, GeneTree:ENSGT00940000162036,
            HOGENOM:CLU_1093963_0_0_1, InParanoid:Q8IUN9,
            OrthoDB:3991783at2759, PhylomeDB:Q8IUN9, TreeFam:TF352155,
            PathwayCommons:Q8IUN9, Reactome:R-HSA-5621480, SignaLink:Q8IUN9,
            BioGRID-ORCS:10462, GeneWiki:CLEC10A, GenomeRNAi:10462,
            Pharos:Q8IUN9, PRO:PR:Q8IUN9, Proteomes:UP000005640, RNAct:Q8IUN9,
            Bgee:ENSG00000132514, ExpressionAtlas:Q8IUN9, Genevisible:Q8IUN9,
            GO:0009897, GO:0005886, GO:0030246, GO:0042806, GO:0005537,
            GO:0002250, GO:0006897, GO:0045087, CDD:cd03590,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033989, InterPro:IPR016187,
            PANTHER:PTHR22803, PANTHER:PTHR22803:SF116, Pfam:PF00059,
            Pfam:PF03954, SMART:SM00034, SUPFAM:SSF56436, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    3D-structure; Adaptive immunity; Alternative splicing; Coiled coil;
            Disulfide bond; Endocytosis; Glycoprotein; Immunity; Innate
            immunity; Lectin; Membrane; Reference proteome; Signal-anchor;
            Transmembrane; Transmembrane helix.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Suzuki,N., Yamamoto,K., Toyoshima,S., Osawa,T. and Irimura,T.
  TITLE     Molecular cloning and expression of cDNA encoding human macrophage
            C-type lectin. Its unique carbohydrate binding specificity for Tn
            antigen
  JOURNAL   J Immunol 156 (1), 128-135 (1996)
   PUBMED   8598452
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND VARIANT
            ARG-35.;
            TISSUE=Peripheral blood monocyte
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).;
            TISSUE=Testis
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).;
            TISSUE=Brain
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     [FUNCTION] Probable role in regulating adaptive and innate immune
            responses. Binds in a calcium-dependent manner to terminal
            galactose and N-acetylgalactosamine units, linked to serine or
            threonine. These sugar moieties are known as Tn-Ag and are
            expressed in a variety of carcinoma cells.
            {ECO:0000269|PubMed:8598452}.
            [INTERACTION] Q8IUN9; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-2873246,
            EBI-2876502; Q8IUN9; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-2873246,
            EBI-10827839; Q8IUN9; P05090: APOD; NbExp=3; IntAct=EBI-2873246,
            EBI-715495; Q8IUN9; O15155: BET1; NbExp=3; IntAct=EBI-2873246,
            EBI-749204; Q8IUN9; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-2873246,
            EBI-6165897; Q8IUN9; P31513: FMO3; NbExp=3; IntAct=EBI-2873246,
            EBI-12361463; Q8IUN9; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-2873246,
            EBI-713304; Q8IUN9; Q8WWP7: GIMAP1; NbExp=4; IntAct=EBI-2873246,
            EBI-11991950; Q8IUN9; Q13021: MALL; NbExp=3; IntAct=EBI-2873246,
            EBI-750078; Q8IUN9; Q9H115: NAPB; NbExp=5; IntAct=EBI-2873246,
            EBI-3921185; Q8IUN9; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-2873246,
            EBI-981985; Q8IUN9; O60831: PRAF2; NbExp=3; IntAct=EBI-2873246,
            EBI-2506064; Q8IUN9; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2873246,
            EBI-8652744; Q8IUN9; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-2873246,
            EBI-10314552; Q8IUN9; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-2873246,
            EBI-8640191; Q8IUN9; A2RU14: TMEM218; NbExp=3; IntAct=EBI-2873246,
            EBI-10173151; Q8IUN9; P01375: TNF; NbExp=3; IntAct=EBI-2873246,
            EBI-359977; Q8IUN9; P30536: TSPO; NbExp=3; IntAct=EBI-2873246,
            EBI-6623146; Q8IUN9; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-2873246,
            EBI-10243654; Q8IUN9; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-2873246,
            EBI-11988865; Q8IUN9; Q53HI1: UNC50; NbExp=3; IntAct=EBI-2873246,
            EBI-7601760; Q8IUN9; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-2873246,
            EBI-12190699; Q8IUN9; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-2873246,
            EBI-12837904; Q8IUN9; O95159: ZFPL1; NbExp=3; IntAct=EBI-2873246,
            EBI-718439; Q8IUN9; P0DTC2: S; Xeno; NbExp=4; IntAct=EBI-2873246,
            EBI-25474821; Q8IUN9-2; P0DTC2: S; Xeno; NbExp=4;
            IntAct=EBI-25776912, EBI-25474821.
            [SUBCELLULAR LOCATION] Membrane {ECO:0000305}; Single-pass type II
            membrane protein {ECO:0000305}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=3; Name=1; IsoId=Q8IUN9-1; Sequence=Displayed; Name=2;
            IsoId=Q8IUN9-2; Sequence=VSP_012848, VSP_012849; Name=3;
            IsoId=Q8IUN9-3; Sequence=VSP_012848, VSP_012850, VSP_012851.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=MGL;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_hum_Ctlect_217'.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..316
                     /gene="CLEC10A"
                     /gene_synonym="CLECSF13"
                     /gene_synonym="CLECSF14"
                     /gene_synonym="HML"
     Protein         1..316
                     /product="C-type lectin domain family 10 member A"
                     /note="C-type lectin superfamily member 14; Macrophage
                     lectin 2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..316
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 10 member A.
                     /id=PRO_0000046639."
     Region          1..39
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          5..170
                     /region_name="Lectin_N"
                     /note="Hepatic lectin, N-terminal domain; pfam03954"
                     /db_xref="CDD:427612"
     Region          5..8
                     /region_name="Short sequence motif of biological interest"
                     /note="Endocytosis signal. /evidence=ECO:0000255."
     Region          35
                     /region_name="Variant"
                     /note="C -> R (in dbSNP:rs90951).
                     /evidence=ECO:0000269|PubMed:8598452. /id=VAR_021262."
     Region          40..60
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          61..316
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          73
                     /region_name="Variant"
                     /note="R -> K (in dbSNP:rs16956478). /id=VAR_050113."
     Site            78
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          85..176
                     /region_name="Coiled-coil region"
                     /note="/evidence=ECO:0000255."
     Region          100
                     /region_name="Variant"
                     /note="T -> M (in dbSNP:rs35318160). /id=VAR_050114."
     Region          112
                     /region_name="Conflict"
                     /note="K -> R (in Ref. 3; AAH27858).
                     /evidence=ECO:0000305."
     Region          118..144
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2 and isoform 3).
                     /evidence=ECO:0000303|PubMed:14702039,
                     ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8598452.
                     /id=VSP_012848."
     Region          173
                     /region_name="Splicing variant"
                     /note="N -> NGEE (in isoform 2).
                     /evidence=ECO:0000303|PubMed:8598452. /id=VSP_012849."
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          181..305
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(181,192)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          186..188
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6PUV."
     Region          188..305
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          191..195
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6PUV."
     Region          202..211
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:6PUV."
     Region          203
                     /region_name="Variant"
                     /note="A -> G (in dbSNP:rs35101468). /id=VAR_050115."
     Bond            bond(209,304)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          222..229
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:6PUV."
     Region          226..283
                     /region_name="Splicing variant"
                     /note="NFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPDDWQGHGL
                     GGGEDCA ->
                     VRASGTQFLRHVPFREMVLKLGRTLESSGSFQNDCHLCHTLRDLIGLSIQRNISKLLS
                     (in isoform 3). /evidence=ECO:0000303|PubMed:14702039,
                     ECO:0000303|PubMed:15489334. /id=VSP_012850."
     Site            order(236,267,269,280,286,292..295)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Region          237..242
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6PUV."
     Site            order(243,245,270,280..281)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(245,281)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Region          276..278
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6PY1."
     Region          281..285
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6PUV."
     Bond            bond(282,296)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          284..316
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 3).
                     /evidence=ECO:0000303|PubMed:14702039,
                     ECO:0000303|PubMed:15489334. /id=VSP_012851."
     Region          291..295
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6PUV."
     Region          300..307
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6PUV."
ORIGIN
        1 mtrtyenfqy lenkvkvqgf kngplplqsl lqrlcsgpch lllslglgll llviicvvgf
       61 qnskfqrdlv tlrtdfsnft sntvaeiqal tsqgssleet iaslkaeveg fkqerqagvs
      121 elqehttqka hlghcphcps vcvpvhseml lrvqqlvqdl kkltcqvatl nnnastegtc
      181 cpvnwvehqd scywfshsgm swaeaekycq lknahlvvin sreeqnfvqk ylgsaytwmg
      241 lsdpegawkw vdgtdyatgf qnwkpgqpdd wqghglggge dcahfhpdgr wnddvcqrpy
      301 hwvceaglgq tsqesh
//
LOCUS       LECM6_PSEPL              158 aa            linear   VRT 22-FEB-2023
DEFINITION  RecName: Full=C-type lectin lectoxin-Enh6; Short=CTL; Flags:
            Precursor.
ACCESSION   A7X3Y2
VERSION     A7X3Y2.1
DBSOURCE    UniProtKB: locus LECM6_PSEPL, accession A7X3Y2;
            class: standard.
            created: Dec 16, 2008.
            sequence updated: Oct 23, 2007.
            annotation updated: Feb 22, 2023.
            xrefs: EU029694.1, ABU68494.1
            xrefs (non-sequence databases): AlphaFoldDB:A7X3Y2, SMR:A7X3Y2,
            GO:0005576, GO:0030246, GO:0046872, GO:0090729, Gene3D:3.10.100.10,
            InterPro:IPR001304, InterPro:IPR016186, InterPro:IPR018378,
            InterPro:IPR016187, PANTHER:PTHR22803, PANTHER:PTHR22803:SF116,
            Pfam:PF00059, PRINTS:PR01504, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Calcium; Disulfide bond; Hemagglutinin; Lectin; Metal-binding;
            Secreted; Signal; Toxin.
SOURCE      Pseudoferania polylepis (Macleay's water snake)
  ORGANISM  Pseudoferania polylepis
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
            Toxicofera; Serpentes; Colubroidea; Homalopsidae; Pseudoferania.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Fry,B.G., Scheib,H., van der Weerd,L., Young,B., McNaughtan,J.,
            Ramjan,S.F., Vidal,N., Poelmann,R.E. and Norman,J.A.
  TITLE     Evolution of an arsenal: structural and functional diversification
            of the venom system in the advanced snakes (Caenophidia)
  JOURNAL   Mol Cell Proteomics 7 (2), 215-246 (2008)
   PUBMED   17855442
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            TISSUE=Venom gland
COMMENT     [FUNCTION] Mannose-binding lectin which recognizes specific
            carbohydrate structures and agglutinates a variety of animal cells
            by binding to cell-surface glycoproteins and glycolipids. May be a
            calcium-dependent lectin (By similarity). {ECO:0000250}.
            [SUBCELLULAR LOCATION] Secreted {ECO:0000250}.
            [TISSUE SPECIFICITY] Expressed by the venom gland.
            [SIMILARITY] Belongs to the true venom lectin family.
            {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pseudoferania polylepis"
                     /db_xref="taxon:338839"
     Protein         1..158
                     /product="C-type lectin lectoxin-Enh6"
                     /note="CTL"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..23
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          24..158
                     /region_name="Mature chain"
                     /note="C-type lectin lectoxin-Enh6. /id=PRO_0000356312."
     Region          26..156
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:445781"
     Bond            bond(26,37)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          33..155
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(54,154)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          119..121
                     /region_name="Short sequence motif of biological interest"
                     /note="Mannose-binding."
     Site            order(127,131,133,140,142..145,148..150)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Bond            bond(129,146)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
ORIGIN
        1 mgqftvvslg llavflslsg akgdncpanw isrngvcnkl fpdrktwlea emycralkpg
       61 chlaslhrds dstvlawyis dhfkgaghvw iglrdtnrkr twkwsdrtst nyfswnqgep
      121 nnvqdnencv hlwapsgylk wndepcaslh psicqykl
//
LOCUS       ASGR2_MOUSE              301 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=Asialoglycoprotein receptor 2; Short=ASGP-R 2;
            Short=ASGPR 2; AltName: Full=Hepatic lectin 2; Short=HL-2;
            Short=mHL-2.
ACCESSION   P24721
VERSION     P24721.1
DBSOURCE    UniProtKB: locus ASGR2_MOUSE, accession P24721;
            class: standard.
            created: Mar 1, 1992.
            sequence updated: Mar 1, 1992.
            annotation updated: Sep 13, 2023.
            xrefs: X53042.1, CAA37211.1, BC011197.1, AAH11197.1, S13165,
            NP_001300854.1, NP_001300855.1, NP_001300856.1, NP_031519.1
            xrefs (non-sequence databases): CCDS:CCDS24934.1,
            AlphaFoldDB:P24721, SMR:P24721, STRING:10090.ENSMUSP00000099632,
            GlyCosmos:P24721, GlyGen:P24721, iPTMnet:P24721,
            PhosphoSitePlus:P24721, SwissPalm:P24721, jPOST:P24721,
            MaxQB:P24721, PaxDb:P24721, ProteomicsDB:281919,
            Antibodypedia:2656, DNASU:11890, Ensembl:ENSMUST00000102572,
            Ensembl:ENSMUSP00000099632, Ensembl:ENSMUSG00000040963,
            GeneID:11890, KEGG:mmu:11890, UCSC:uc007jtt.1, AGR:MGI:88082,
            CTD:433, MGI:88082, VEuPathDB:HostDB:ENSMUSG00000040963,
            eggNOG:KOG4297, GeneTree:ENSGT00940000162310,
            HOGENOM:CLU_049894_2_0_1, InParanoid:P24721, OMA:RTLTCQM,
            OrthoDB:3991783at2759, PhylomeDB:P24721, TreeFam:TF352155,
            Reactome:R-MMU-446203, BioGRID-ORCS:11890, ChiTaRS:Asgr2,
            PRO:PR:P24721, Proteomes:UP000000589, RNAct:P24721,
            Bgee:ENSMUSG00000040963, ExpressionAtlas:P24721,
            Genevisible:P24721, GO:0044322, GO:0009897, GO:0048471, GO:0042806,
            GO:0005537, GO:0030282, GO:0006897, GO:0009100, GO:0055088,
            GO:0031647, CDD:cd03590, Gene3D:3.10.100.10, InterPro:IPR001304,
            InterPro:IPR016186, InterPro:IPR018378, InterPro:IPR033989,
            InterPro:IPR016187, PANTHER:PTHR22802:SF433, PANTHER:PTHR22802,
            Pfam:PF00059, Pfam:PF03954, SMART:SM00034, SUPFAM:SSF56436,
            PROSITE:PS00615, PROSITE:PS50041
KEYWORDS    Calcium; Disulfide bond; Endocytosis; Glycoprotein; Lectin;
            Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
            Reference proteome; Signal-anchor; Transmembrane; Transmembrane
            helix.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Sanford,J.P. and Doyle,D.
  TITLE     Mouse asialoglycoprotein receptor cDNA sequence: conservation of
            receptor genes during mammalian evolution
  JOURNAL   Biochim Biophys Acta 1087 (2), 259-261 (1990)
   PUBMED   2223888
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=C57BL/6J; TISSUE=Liver
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=FVB/N; TISSUE=Liver
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver
COMMENT     On Mar 15, 2005 this sequence version replaced gi:109579.
            [FUNCTION] Mediates the endocytosis of plasma glycoproteins to
            which the terminal sialic acid residue on their complex
            carbohydrate moieties has been removed. The receptor recognizes
            terminal galactose and N-acetylgalactosamine units. After ligand
            binding to the receptor, the resulting complex is internalized and
            transported to a sorting organelle, where receptor and ligand are
            disassociated. The receptor then returns to the cell membrane
            surface.
            [SUBUNIT] Interacts with LASS2. {ECO:0000250}.
            [SUBCELLULAR LOCATION] Membrane; Single-pass type II membrane
            protein.
            [TISSUE SPECIFICITY] Expressed exclusively in hepatic parenchymal
            cells.
            [MISCELLANEOUS] Calcium is required for ligand binding.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Hepatic asialoglycoprotein receptor subunit 2;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_159'.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..301
                     /gene="Asgr2"
                     /gene_synonym="Asgr-2"
     Protein         1..301
                     /product="Asialoglycoprotein receptor 2"
                     /note="ASGP-R 2; ASGPR 2; Hepatic lectin 2; HL-2; mHL-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..301
                     /region_name="Mature chain"
                     /note="Asialoglycoprotein receptor 2. /id=PRO_0000046655."
     Region          1..58
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          1..43
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          1..36
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          4..162
                     /region_name="Lectin_N"
                     /note="Hepatic lectin, N-terminal domain; pfam03954"
                     /db_xref="CDD:427612"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08290."
     Site            54
                     /site_type="lipid-binding"
                     /note="S-palmitoyl cysteine. /evidence=ECO:0000250."
     Region          59..79
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          80..301
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          169..295
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          170..295
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Bond            bond(170,181)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(198,293)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            order(225,256,258,269,275..276,281..284)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(232,259,269..270)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Bond            bond(271,285)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
ORIGIN
        1 mekdcqdiqq ldseendhql sgddehgshv qdprienphw kgqplsrpfp qrlcstfrls
       61 llalafnill lvvicvvssq siqlqeefrt lketfsnfss stlmefgald tlggstnail
      121 tswlaqleek qqqlkadhst llfhlkhfpm dlrtltcqla yfqsngtecc pvnwvefggs
      181 cywfsrdglt waeadqycql enahllvins reeqdfvvkh rsqfhiwigl tdrdgswkwv
      241 dgtdyrsnyr nwaftqpdnw qgheqggged caeilsdghw ndnfcqqvnr wvcekrrnit
      301 h
//
LOCUS       CLC4F_MOUSE              548 aa            linear   ROD 13-SEP-2023
DEFINITION  RecName: Full=C-type lectin domain family 4 member F; AltName:
            Full=C-type lectin superfamily member 13; Short=C-type lectin 13;
            AltName: Full=Kupffer cell receptor.
ACCESSION   P70194
VERSION     P70194.1
DBSOURCE    UniProtKB: locus CLC4F_MOUSE, accession P70194;
            class: standard.
            extra accessions:Q8BLZ8
            created: Nov 1, 1997.
            sequence updated: Feb 1, 1997.
            annotation updated: Sep 13, 2023.
            xrefs: D88577.1, BAA13647.1, AK040696.1, BAC30671.1, BC013647.1,
            AAH13647.1, NP_058031.2, 6JJJ_A, 6JJJ_B, 6JJJ_C, 6JJJ_D, 6JJJ_E,
            6JJJ_F
            xrefs (non-sequence databases): CCDS:CCDS20281.1, PDBsum:6JJJ,
            AlphaFoldDB:P70194, SMR:P70194, STRING:10090.ENSMUSP00000014686,
            UniLectin:P70194, GlyCosmos:P70194, GlyGen:P70194, iPTMnet:P70194,
            PhosphoSitePlus:P70194, SwissPalm:P70194, CPTAC:non-CPTAC-3567,
            jPOST:P70194, MaxQB:P70194, PaxDb:P70194, PeptideAtlas:P70194,
            ProteomicsDB:285468, ABCD:P70194, DNASU:51811, GeneID:51811,
            KEGG:mmu:51811, UCSC:uc009cnv.1, AGR:MGI:1859834, CTD:165530,
            MGI:1859834, eggNOG:KOG4297, InParanoid:P70194,
            OrthoDB:4633257at2759, PhylomeDB:P70194, TreeFam:TF333341,
            BioGRID-ORCS:51811, PRO:PR:P70194, Proteomes:UP000000589,
            RNAct:P70194, GO:0009897, GO:0005886, GO:0030246, GO:0005534,
            GO:0051861, GO:0006897, GO:0051132, CDD:cd03590, Gene3D:1.20.5.170,
            Gene3D:3.10.100.10, InterPro:IPR001304, InterPro:IPR016186,
            InterPro:IPR018378, InterPro:IPR033989, InterPro:IPR016187,
            PANTHER:PTHR22801, PANTHER:PTHR22801:SF61, Pfam:PF00059,
            SMART:SM00034, SUPFAM:SSF56436, SUPFAM:SSF57997, PROSITE:PS00615,
            PROSITE:PS50041
KEYWORDS    3D-structure; Disulfide bond; Endocytosis; Glycoprotein; Lectin;
            Membrane; Receptor; Reference proteome; Signal-anchor;
            Transmembrane; Transmembrane helix.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Takezawa,R., Wagatsuma,H., Nomoto,C., Watanabe,Y. and Akaike,T.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-NOV-1996) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA].;
            STRAIN=BALB/cJ; TISSUE=Liver
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Carninci,P., Kasukawa,T., Katayama,S., Gough,J., Frith,M.C.,
            Maeda,N., Oyama,R., Ravasi,T., Lenhard,B., Wells,C., Kodzius,R.,
            Shimokawa,K., Bajic,V.B., Brenner,S.E., Batalov,S., Forrest,A.R.,
            Zavolan,M., Davis,M.J., Wilming,L.G., Aidinis,V., Allen,J.E.,
            Ambesi-Impiombato,A., Apweiler,R., Aturaliya,R.N., Bailey,T.L.,
            Bansal,M., Baxter,L., Beisel,K.W., Bersano,T., Bono,H., Chalk,A.M.,
            Chiu,K.P., Choudhary,V., Christoffels,A., Clutterbuck,D.R.,
            Crowe,M.L., Dalla,E., Dalrymple,B.P., de Bono,B., Della Gatta,G.,
            di Bernardo,D., Down,T., Engstrom,P., Fagiolini,M., Faulkner,G.,
            Fletcher,C.F., Fukushima,T., Furuno,M., Futaki,S., Gariboldi,M.,
            Georgii-Hemming,P., Gingeras,T.R., Gojobori,T., Green,R.E.,
            Gustincich,S., Harbers,M., Hayashi,Y., Hensch,T.K., Hirokawa,N.,
            Hill,D., Huminiecki,L., Iacono,M., Ikeo,K., Iwama,A., Ishikawa,T.,
            Jakt,M., Kanapin,A., Katoh,M., Kawasawa,Y., Kelso,J., Kitamura,H.,
            Kitano,H., Kollias,G., Krishnan,S.P., Kruger,A., Kummerfeld,S.K.,
            Kurochkin,I.V., Lareau,L.F., Lazarevic,D., Lipovich,L., Liu,J.,
            Liuni,S., McWilliam,S., Madan Babu,M., Madera,M., Marchionni,L.,
            Matsuda,H., Matsuzawa,S., Miki,H., Mignone,F., Miyake,S.,
            Morris,K., Mottagui-Tabar,S., Mulder,N., Nakano,N., Nakauchi,H.,
            Ng,P., Nilsson,R., Nishiguchi,S., Nishikawa,S., Nori,F., Ohara,O.,
            Okazaki,Y., Orlando,V., Pang,K.C., Pavan,W.J., Pavesi,G.,
            Pesole,G., Petrovsky,N., Piazza,S., Reed,J., Reid,J.F., Ring,B.Z.,
            Ringwald,M., Rost,B., Ruan,Y., Salzberg,S.L., Sandelin,A.,
            Schneider,C., Schonbach,C., Sekiguchi,K., Semple,C.A., Seno,S.,
            Sessa,L., Sheng,Y., Shibata,Y., Shimada,H., Shimada,K., Silva,D.,
            Sinclair,B., Sperling,S., Stupka,E., Sugiura,K., Sultana,R.,
            Takenaka,Y., Taki,K., Tammoja,K., Tan,S.L., Tang,S., Taylor,M.S.,
            Tegner,J., Teichmann,S.A., Ueda,H.R., van Nimwegen,E., Verardo,R.,
            Wei,C.L., Yagi,K., Yamanishi,H., Zabarovsky,E., Zhu,S., Zimmer,A.,
            Hide,W., Bult,C., Grimmond,S.M., Teasdale,R.D., Liu,E.T.,
            Brusic,V., Quackenbush,J., Wahlestedt,C., Mattick,J.S., Hume,D.A.,
            Kai,C., Sasaki,D., Tomaru,Y., Fukuda,S., Kanamori-Katayama,M.,
            Suzuki,M., Aoki,J., Arakawa,T., Iida,J., Imamura,K., Itoh,M.,
            Kato,T., Kawaji,H., Kawagashira,N., Kawashima,T., Kojima,M.,
            Kondo,S., Konno,H., Nakano,K., Ninomiya,N., Nishio,T., Okada,M.,
            Plessy,C., Shibata,K., Shiraki,T., Suzuki,S., Tagami,M., Waki,K.,
            Watahiki,A., Okamura-Oho,Y., Suzuki,H., Kawai,J. and Hayashizaki,Y.
  CONSRTM   FANTOM Consortium; RIKEN Genome Exploration Research Group and
            Genome Science Group (Genome Network Project Core Group)
  TITLE     The transcriptional landscape of the mammalian genome
  JOURNAL   Science 309 (5740), 1559-1563 (2005)
   PUBMED   16141072
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=C57BL/6J; TISSUE=Aorta
            Erratum:[Science. 2006 Mar 24;311(5768):1713]
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=FVB/N; TISSUE=Liver
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver
COMMENT     [FUNCTION] Receptor with an affinity for galactose and fucose.
            Could be involved in endocytosis.
            [SUBCELLULAR LOCATION] Membrane; Single-pass type II membrane
            protein.
            [TISSUE SPECIFICITY] Kupffer cells.
            [WEB RESOURCE] Name=Functional Glycomics Gateway - Glycan Binding;
            Note=Kupffer cell receptor;
            URL='http://www.functionalglycomics.org/glycomics/GBPServlet?&opera
            tionType=view&cbpId=cbp_mou_Ctlect_166'.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..548
                     /gene="Clec4f"
                     /gene_synonym="Clecsf13"
                     /gene_synonym="Kclr"
     Protein         1..548
                     /product="C-type lectin domain family 4 member F"
                     /note="C-type lectin superfamily member 13; Kupffer cell
                     receptor; C-type lectin 13"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..548
                     /region_name="Mature chain"
                     /note="C-type lectin domain family 4 member F.
                     /id=PRO_0000046623."
     Region          1..42
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          <13..93
                     /region_name="DUF2615"
                     /note="Protein of unknown function (DUF2615); pfam11027"
                     /db_xref="CDD:402563"
     Region          43..69
                     /region_name="Transmembrane region"
                     /note="Helical; Signal-anchor for type II membrane
                     protein. /evidence=ECO:0000255."
     Region          70..548
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          <83..403
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            255
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          366
                     /region_name="Conflict"
                     /note="T -> S (in Ref. 2; BAC30671).
                     /evidence=ECO:0000305."
     Region          397..413
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Region          414..538
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Region          417..419
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Region          422..426
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Region          433..442
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Region          438..538
                     /region_name="Domain"
                     /note="C-type lectin.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Bond            bond(440,536)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          453..463
                     /region_name="Helical region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Site            order(467,502,504,514,520,524..527)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Region          468..473
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Site            order(474,478,505,514..515)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Region          476..479
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Site            order(478,515)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Region          482..486
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Region          490..493
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Region          496..498
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Region          509..511
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Bond            bond(516,528)
                     /bond_type="disulfide"
                     /note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00040."
     Region          516..526
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
     Region          534..539
                     /region_name="Beta-strand region"
                     /note="/evidence=ECO:0007829|PDB:6JJJ."
ORIGIN
        1 mkeaelnrdm aryctdnqcv slqpqglgpk saalmaprtl rhvqvilalm vvtvifslla
       61 lfvvasqpwr pewnkeppsl llrgsnnsgh dnhsqfvret emqvaiqrlr dyeensssch
      121 kevqilkyqm dnvsslvqll gshledvnad ilqtkdvlke sgalaletqa lrsslevasa
      181 dihslrgdle kanamtsqtr gllksstent saelhvlgrg leeaqseiqa lrgslqsand
      241 lssqtqgflq hsmdnisaqi qtvrdgmera gekmnslkke letltaqtqk anghleqtda
      301 qiqglkaelk stsslnsrie vvngqmkdas relqtlrrdl sdvsalksnv qmlqsnlqra
      361 ktemqtlkad lqatkaltak iqgeqnrlga lqeavaaqkq eqktqnqvlq liaqnwkyfn
      421 gnfyyfsrdk kpwreaekfc tsqgahlasv tsqeeqaflv qttssgdhwi gltdqgtegi
      481 wrwvdgtpfn naqskgfwgk nqpdnwrhrn geredcvhvr qqwndmacgs sypwvckkst
      541 gwsaarvg
//
