CO2A1_BOVIN
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 03-AUG-2022, entry version 172.
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 PaxDb; P02459; -.
DR PRIDE; P02459; -.
DR ABCD; P02459; 5 sequenced antibodies.
DR Ensembl; ENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155.
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; GWQPGPK; -.
DR OrthoDB; 337699at2759; -.
DR TreeFam; TF344135; -.
DR Reactome; R-BTA-1442490; Collagen degradation.
DR Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-BTA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-BTA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-BTA-3000178; ECM proteoglycans.
DR Reactome; R-BTA-8948216; Collagen chain trimerization.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000013155; Expressed in laryngeal cartilage and 58 other tissues.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central.
DR GO; GO:0005585; C:collagen type II trimer; IBA:GO_Central.
DR GO; GO:0005592; C:collagen type XI trimer; IC:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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: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:0030198; P:extracellular matrix organization; IBA:GO_Central.
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 InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 7.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 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
