ID   CO2A1_BOVIN             Reviewed;        1487 AA.
AC   P02459; Q28070; Q9XT24; Q9XT25;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 4.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Collagen alpha-1(II) chain {ECO:0000250|UniProtKB:P02458};
DE   AltName: Full=Alpha-1 type II collagen {ECO:0000250|UniProtKB:P02458};
DE   Flags: Precursor;
GN   Name=COL2A1 {ECO:0000250|UniProtKB:P02458};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 201-362, HYDROXYLATION AT PRO-212; PRO-218; PRO-230;
RP   PRO-233; PRO-245; PRO-248; PRO-251; PRO-260; PRO-269; PRO-278; PRO-281;
RP   PRO-284; LYS-287; PRO-293; LYS-299; PRO-305; LYS-308; PRO-314; PRO-320;
RP   PRO-329; PRO-350 AND PRO-356, AND GLYCOSYLATION AT LYS-287; LYS-299 AND
RP   LYS-308.
RC   TISSUE=Cartilage;
RX   PubMed=782511; DOI=10.1021/bi00659a010;
RA   Butler W.T., Miller E.J., Finch J.E. Jr.;
RT   "The covalent structure of cartilage collagen. Amino acid sequence of the
RT   NH2-terminal helical portion of the alpha 1 (II) chain.";
RL   Biochemistry 15:3000-3006(1976).
RN   [3]
RP   PROTEIN SEQUENCE OF 345-359, HYDROXYLATION AT PRO-350 AND PRO-356, AND
RP   VARIANT LEU-349.
RC   TISSUE=Cartilage;
RX   PubMed=833147; DOI=10.1016/s0021-9258(17)32766-7;
RA   Butler W.T., Finch J.E. Jr., Miller E.J.;
RT   "The covalent structure of cartilage collagen. Evidence for sequence
RT   heterogeneity of bovine alpha1(II) chains.";
RL   J. Biol. Chem. 252:639-643(1977).
RN   [4]
RP   PROTEIN SEQUENCE OF 324-602, HYDROXYLATION AT PRO-329; PRO-350; PRO-356;
RP   PRO-365; PRO-368; PRO-371; LYS-374; PRO-395; PRO-398; PRO-401; PRO-410;
RP   PRO-416; LYS-419; PRO-425; PRO-431; PRO-434; PRO-440; LYS-452; PRO-458;
RP   LYS-464; LYS-470; PRO-473; PRO-482; PRO-497; PRO-506; PRO-512; PRO-518;
RP   LYS-527; PRO-530; LYS-542; PRO-551; PRO-557; PRO-566; PRO-581; PRO-587;
RP   PRO-590 AND PRO-599, AND GLYCOSYLATION AT LYS-374.
RC   TISSUE=Cartilage;
RX   PubMed=2714276; DOI=10.1111/j.1432-1033.1989.tb14707.x;
RA   Seyer J.M., Hasty K.A., Kang A.H.;
RT   "Covalent structure of collagen. Amino acid sequence of an arthritogenic
RT   cyanogen bromide peptide from type II collagen of bovine cartilage.";
RL   Eur. J. Biochem. 181:159-173(1989).
RN   [5]
RP   PROTEIN SEQUENCE OF 603-677, HYDROXYLATION AT PRO-605; LYS-608; PRO-614;
RP   LYS-620; PRO-623; PRO-626; PRO-632; PRO-644; PRO-659; PRO-668; PRO-671 AND
RP   PRO-674, AND GLYCOSYLATION AT LYS-608 AND LYS-620.
RX   PubMed=4857180; DOI=10.1016/s0006-291x(74)80375-x;
RA   Butler W.T., Miller E.J., Finch J.E. Jr., Inagami T.;
RT   "Homologous regions of collagen alpha1(I) and alpha1(II) chains: apparent
RT   clustering of variable and invariant amino acid residues.";
RL   Biochem. Biophys. Res. Commun. 57:190-195(1974).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 323-602.
RC   TISSUE=Chondrocyte;
RX   PubMed=7511638;
RA   Brand D.D., Myers L.K., Terato K., Whittington K.B., Stuart J.M.,
RA   Kang A.H., Rosloniec E.F.;
RT   "Characterization of the T cell determinants in the induction of autoimmune
RT   arthritis by bovine alpha 1(II)-CB11 in H-2q mice.";
RL   J. Immunol. 152:3088-3097(1994).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 602-751.
RC   TISSUE=Chondrocyte;
RX   PubMed=10479530; DOI=10.1006/clim.1999.4755;
RA   Tang B., Chiang T.M., Brand D.D., Gumanovskaya M.L., Stuart J.M.,
RA   Kang A.H., Myers L.K.;
RT   "Molecular definition and characterization of recombinant bovine CB8 and
RT   CB10: immunogenicity and arthritogenicity.";
RL   Clin. Immunol. 92:256-264(1999).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1307-1487.
RX   PubMed=2582365; DOI=10.1093/nar/13.8.2815;
RA   Sangiorgi F.O., Benson-Chanda V., de Wet W.J., Sobel M.E., Ramirez F.;
RT   "Analysis of cDNA and genomic clones coding for the pro alpha 1 chain of
RT   calf type II collagen.";
RL   Nucleic Acids Res. 13:2815-2826(1985).
CC   -!- FUNCTION: Type II collagen is specific for cartilaginous tissues. It is
CC       essential for the normal embryonic development of the skeleton, for
CC       linear growth and for the ability of cartilage to resist compressive
CC       forces.
CC   -!- SUBUNIT: Homotrimers of alpha 1(II) chains.
CC   -!- INTERACTION:
CC       P02459; P21941: MATN1; Xeno; NbExp=3; IntAct=EBI-5281315, EBI-20828128;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC   -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC       crucial roles in tissue growth and repair by controlling both the
CC       intracellular assembly of procollagen molecules and the extracellular
CC       assembly of collagen fibrils. It binds a calcium ion which is essential
CC       for its function (By similarity). {ECO:0000250}.
CC   -!- PTM: Probably 3-hydroxylated on prolines by LEPREL1 (By similarity).
CC       Proline residues at the third position of the tripeptide repeating unit
CC       (G-X-P) are hydroxylated in some or all of the chains. Proline residues
CC       at the second position of the tripeptide repeating unit (G-P-X) are
CC       hydroxylated in some of the chains. {ECO:0000250,
CC       ECO:0000269|PubMed:2714276, ECO:0000269|PubMed:4857180,
CC       ECO:0000269|PubMed:782511, ECO:0000269|PubMed:833147}.
CC   -!- PTM: O-linked glycans consist of Glc-Gal disaccharides bound to the
CC       oxygen atom of post-translationally added hydroxyl groups.
CC       {ECO:0000269|PubMed:2714276, ECO:0000269|PubMed:4857180,
CC       ECO:0000269|PubMed:782511}.
CC   -!- PTM: Contains mostly 4-hydroxyproline. Prolines at the third position
CC       of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or
CC       all of the chains. {ECO:0000269|PubMed:2714276,
CC       ECO:0000269|PubMed:4857180, ECO:0000269|PubMed:782511,
CC       ECO:0000269|PubMed:833147}.
CC   -!- PTM: Contains 3-hydroxyproline at a few sites. This modification occurs
CC       on the first proline residue in the sequence motif Gly-Pro-Hyp, where
CC       Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P05539}.
CC   -!- PTM: Lysine residues at the third position of the tripeptide repeating
CC       unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
CC       {ECO:0000250|UniProtKB:P05539}.
CC   -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
CC       glycan consists of a Glc-Gal disaccharide. {ECO:0000269|PubMed:2714276,
CC       ECO:0000269|PubMed:4857180, ECO:0000269|PubMed:782511}.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR   EMBL; AAFC03017082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03017085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03056593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L28918; AAA30436.2; -; mRNA.
DR   EMBL; AF138883; AAD42346.1; -; mRNA.
DR   EMBL; AF138957; AAD42347.1; -; mRNA.
DR   EMBL; X02420; CAA26269.1; -; mRNA.
DR   PIR; A90369; CGBO6C.
DR   PIR; I45876; I45876.
DR   RefSeq; NP_001001135.2; NM_001001135.3.
DR   AlphaFoldDB; P02459; -.
DR   PCDDB; P02459; -.
DR   SMR; P02459; -.
DR   ComplexPortal; CPX-3105; Collagen type II trimer.
DR   ComplexPortal; CPX-3108; Collagen type XI trimer variant 1.
DR   IntAct; P02459; 3.
DR   STRING; 9913.ENSBTAP00000017505; -.
DR   GlyCosmos; P02459; 9 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000017505; -.
DR   ABCD; P02459; 5 sequenced antibodies.
DR   Ensembl; ENSBTAT00000017505.6; ENSBTAP00000017505.5; ENSBTAG00000013155.6.
DR   GeneID; 407142; -.
DR   KEGG; bta:407142; -.
DR   CTD; 1280; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013155; -.
DR   VGNC; VGNC:27564; COL2A1.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000155224; -.
DR   InParanoid; P02459; -.
DR   OMA; HIRMGET; -.
DR   OrthoDB; 2970887at2759; -.
DR   TreeFam; TF344135; -.
DR   Reactome; R-BTA-1442490; Collagen degradation.
DR   Reactome; R-BTA-1474244; Extracellular matrix organization.
DR   Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-BTA-186797; Signaling by PDGF.
DR   Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-BTA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-BTA-216083; Integrin cell surface interactions.
DR   Reactome; R-BTA-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-BTA-3000178; ECM proteoglycans.
DR   Reactome; R-BTA-8874081; MET activates PTK2 signaling.
DR   Reactome; R-BTA-8948216; Collagen chain trimerization.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000013155; Expressed in laryngeal cartilage and 58 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0005585; C:collagen type II trimer; IBA:GO_Central.
DR   GO; GO:0005592; C:collagen type XI trimer; NAS:ComplexPortal.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042289; F:MHC class II protein binding; IEA:Ensembl.
DR   GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR   GO; GO:0097065; P:anterior head development; IEA:Ensembl.
DR   GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR   GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR   GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IEA:Ensembl.
DR   GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR   GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR   GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
DR   GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0030903; P:notochord development; IBA:GO_Central.
DR   GO; GO:0071599; P:otic vesicle development; IEA:Ensembl.
DR   GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 6.
DR   Pfam; PF00093; VWC; 1.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Collagen; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..181
FT                   /note="N-terminal propeptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000401210"
FT   CHAIN           182..1487
FT                   /note="Collagen alpha-1(II) chain"
FT                   /id="PRO_0000005725"
FT   DOMAIN          32..90
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          1253..1487
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   REGION          96..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..1214
FT                   /note="Triple-helical region"
FT                   /evidence="ECO:0000250"
FT   REGION          1215..1241
FT                   /note="Nonhelical region (C-terminal)"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        133..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..174
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..251
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..365
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..446
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..924
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1200..1217
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1301
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1303
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1306
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         1309
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            181..182
FT                   /note="Cleavage; by procollagen N-endopeptidase"
FT                   /evidence="ECO:0000250"
FT   SITE            1241..1242
FT                   /note="Cleavage; by procollagen C-endopeptidase"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         190
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         212
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         218
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         230
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         233
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         245
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         248
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         251
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         260
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         269
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         278
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         281
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         284
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         287
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         293
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         299
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         305
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         308
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         314
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         320
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   MOD_RES         329
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276,
FT                   ECO:0000269|PubMed:782511"
FT   MOD_RES         350
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276,
FT                   ECO:0000269|PubMed:782511, ECO:0000269|PubMed:833147"
FT   MOD_RES         356
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276,
FT                   ECO:0000269|PubMed:782511, ECO:0000269|PubMed:833147"
FT   MOD_RES         365
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         368
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         371
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         374
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         395
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         398
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         401
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         410
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         416
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         419
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         425
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         431
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         434
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         440
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         452
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         458
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         464
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         470
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         473
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         482
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         497
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         506
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         512
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         518
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         527
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         530
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         542
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         551
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         557
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         566
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         581
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         587
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         590
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         599
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2714276"
FT   MOD_RES         605
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         608
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         614
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         620
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         623
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         626
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         632
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         644
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         659
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         668
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         670
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         671
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         674
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   MOD_RES         907
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         908
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         914
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         920
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1130
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1144
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1181
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1186
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1187
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1201
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1202
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1205
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1207
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1208
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1211
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1213
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   MOD_RES         1214
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P05539"
FT   CARBOHYD        190
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        287
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   CARBOHYD        299
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   CARBOHYD        308
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:782511"
FT   CARBOHYD        374
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        608
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   CARBOHYD        620
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:4857180"
FT   CARBOHYD        1130
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        1388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1283..1315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1289
FT                   /note="Interchain (with C-1306)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1306
FT                   /note="Interchain (with C-1289)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1323..1485
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   DISULFID        1393..1438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT   VARIANT         349
FT                   /note="Q -> L"
FT                   /evidence="ECO:0000269|PubMed:833147"
FT   CONFLICT        202
FT                   /note="P -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="T -> Q (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="S -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="T -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        436
FT                   /note="P -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="Q -> T (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="T -> S (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476
FT                   /note="A -> T (in Ref. 6; AAA30436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        478
FT                   /note="P -> V (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        514
FT                   /note="N -> S (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        518
FT                   /note="P -> S (in Ref. 6; AAA30436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        523
FT                   /note="L -> I (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        529
FT                   /note="A -> P (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535..539
FT                   /note="PSGLA -> SPGAV (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        544..548
FT                   /note="ANGDP -> SPGEA (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="P -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        560
FT                   /note="R -> K (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        677
FT                   /note="G -> P (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        712
FT                   /note="S -> A (in Ref. 7; AAD42347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        718
FT                   /note="A -> P (in Ref. 7; AAD42347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        734
FT                   /note="A -> S (in Ref. 7; AAD42347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1372
FT                   /note="N -> D (in Ref. 8; CAA26269)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1487 AA;  141828 MW;  F99891F6FD1E47F9 CRC64;
     MIRLGAPQTL VLLTLLVAAV LRCHGQDVQK AGSCVQDGQR YNDKDVWKPE PCRICVCDTG
     TVLCDDIICE DMKDCLSPET PFGECCPICS ADLPTASGQP GPKGQKGEPG DIKDIVGPKG
     PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA
     AQMAGGFDEK AGGAQMGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG
     PRGPPGPPGK PGDDGEAGKP GKSGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
     EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG
     PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS PGPAGAAGNP GTDGIPGAKG
     SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG
     APGPAGEEGK RGARGEPGGA GPAGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG
     PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
     VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA GERGEQGAPG
     PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE RGFPGERGSP GSQGLQGARG
     LPGTPGTDGP KGAAGPAGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG
     KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PAGTAGARGA PGERGETGPP GPAGFAGPPG
     ADGQPGAKGE QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
     AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGDPGLQGPA GPPGEKGEPG
     DDGPSGPDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG
     PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG
     PIGKQGDRGE AGAQGPMGPA GPAGARGMPG PQGPRGDKGE TGEAGERGLK GHRGFTGLQG
     LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG
     PPGNPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPLQYMR ADEAAGNLRQ HDAEVDATLK
     SLNNQIESLR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG
     ETCVYPNPAS VPKKNWWSSK SKDKKHIWFG ETINGGFHFS YGDDNLAPNT ANVQMTFLRL
     LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTVLKDGCTK
     HTGKWGKTMI EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL
//