ID CO1A1_RAT Reviewed; 1453 AA. AC P02454; A3KNA1; P02455; Q63079; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 5. DT 27-MAR-2024, entry version 193. DE RecName: Full=Collagen alpha-1(I) chain; DE AltName: Full=Alpha-1 type I collagen; DE Flags: Precursor; GN Name=Col1a1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Bone, and Tooth; RX PubMed=10065941; DOI=10.1177/00220345990780010101; RA Brandsten C., Lundmark C., Christersson C., Hammarstroem L., Wurtz T.; RT "Expression of collagen alpha1(I) mRNA variants during tooth and bone RT formation in the rat."; RL J. Dent. Res. 78:11-19(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Brown Norway; TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 152-170, ALLYSINE AT LYS-160, AND PYROGLUTAMATE RP FORMATION AT GLN-152. RX PubMed=5777344; DOI=10.1021/bi00829a010; RA Bornstein P.; RT "Comparative sequence studies of rat skin and tendon collagen. II. The RT absence of a short sequence at the amino terminus of the skin alpha-1 RT chain."; RL Biochemistry 8:63-71(1969). RN [5] RP PROTEIN SEQUENCE OF 156-170. RX PubMed=5337886; DOI=10.1021/bi00855a019; RA Kang A.H., Bornstein P., Piez K.A.; RT "The amino acid sequence of peptides from the cross-linking region of rat RT skin collagen."; RL Biochemistry 6:788-795(1967). RN [6] RP PROTEIN SEQUENCE OF 171-206, AND HYDROXYLATION AT PRO-179; PRO-182; RP PRO-185; PRO-194; PRO-197 AND PRO-200. RX PubMed=4290711; DOI=10.1016/s0021-9258(18)96002-3; RA Bornstein P.; RT "The incomplete hydroxylation of individual prolyl residues in collagen."; RL J. Biol. Chem. 242:2572-2574(1967). RN [7] RP PROTEIN SEQUENCE OF 207-253. RX PubMed=4327399; DOI=10.1021/bi00787a018; RA Butler W.T., Ponds S.L.; RT "Chemical studies on the cyanogen bromide peptides of rat skin collagen. RT Amino acid sequence of alpha 1-CB4."; RL Biochemistry 10:2076-2081(1971). RN [8] RP PROTEIN SEQUENCE OF 254-290, HYDROXYLATION AT LYS-254, AND GLYCOSYLATION AT RP LYS-254. RX PubMed=5411206; DOI=10.1021/bi00803a006; RA Butler W.T.; RT "Chemical studies on the cyanogen bromide peptides of rat skin collagen. RT The covalent structure of alpha 1-CB5, the major hexose-containing cyanogen RT bromide peptide of alpha 1."; RL Biochemistry 9:44-50(1970). RN [9] RP PROTEIN SEQUENCE OF 291-389. RX PubMed=4335087; DOI=10.1021/bi00800a019; RA Balian G., Click E.M., Bornstein P.; RT "Structure of rat skin collagen alpha 1-CB8. Amino acid sequence of the RT hydroxylamine-produced fragment HA1."; RL Biochemistry 10:4470-4478(1971). RN [10] RP PROTEIN SEQUENCE OF 390-569. RX PubMed=4342027; DOI=10.1021/bi00770a020; RA Balian G., Click E.M., Hermodson M.A., Bornstein P.; RT "Structure of rat skin collagen alpha 1-CBB. Amino acid sequence of the RT hydroxyl amine-produced fragment HA2."; RL Biochemistry 11:3798-3806(1972). RN [11] RP PROTEIN SEQUENCE OF 570-718. RX PubMed=4366532; DOI=10.1021/bi00711a025; RA Butler W.T., Underwood S.P., Finch J.E. Jr.; RT "Chemical studies on the cyanogen bromide peptides of rat skin collagen. RT Amino acid sequence of alpha 1-CB3."; RL Biochemistry 13:2946-2953(1974). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 680-718. RX PubMed=6395893; DOI=10.1021/bi00320a049; RA Genovese C., Rowe D., Kream B.; RT "Construction of DNA sequences complementary to rat alpha 1 and alpha 2 RT collagen mRNA and their use in studying the regulation of type I collagen RT synthesis by 1,25-dihydroxyvitamin D."; RL Biochemistry 23:6210-6216(1984). RN [13] RP PROTEIN SEQUENCE OF 1103-1186. RX PubMed=4126850; DOI=10.1111/j.1432-1033.1973.tb02987.x; RA Stoltz M., Timpl R., Furthmayr H., Kuehn K.; RT "Structural and immunogenic properties of a major antigenic determinant in RT neutral salt-extracted rat-skin collagen."; RL Eur. J. Biochem. 37:287-294(1973). RN [14] RP PROTEIN SEQUENCE OF 1186-1206. RX PubMed=4636751; DOI=10.1016/0014-5793(72)80542-8; RA Stoltz M., Timpl R., Kuehn K.; RT "Non-helical regions in rat collagen alpha 1-chain."; RL FEBS Lett. 26:61-65(1972). RN [15] RP INTERACTION WITH MRC2. RC STRAIN=Sprague-Dawley; RX PubMed=15817460; DOI=10.1074/jbc.m501155200; RA Thomas E.K., Nakamura M., Wienke D., Isacke C.M., Pozzi A., Liang P.; RT "Endo180 binds to the C-terminal region of type I collagen."; RL J. Biol. Chem. 280:22596-22605(2005). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION. RA Xiong X., Ghosh R., Hiller E., Drepper F., Knapp B., Brunner H., Rupp S.; RT "A new procedure for rapid, high yield purification of Type I collagen for RT tissue engineering."; RL Process Biochem. 44:1200-1212(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-260 AND SER-776, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [18] RP X-RAY CRYSTALLOGRAPHY (5.16 ANGSTROMS) OF 152-1207. RX PubMed=16751282; DOI=10.1073/pnas.0502718103; RA Orgel J.P.R.O., Irving T.C., Miller A., Wess T.J.; RT "Microfibrillar structure of type I collagen in situ."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9001-9005(2006). CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar CC forming collagen). CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts CC with MRC2 (PubMed:15817460). Interacts with TRAM2. Interacts with MFAP4 CC in a Ca (2+)-dependent manner. {ECO:0000250|UniProtKB:P02452, CC ECO:0000250|UniProtKB:P02453, ECO:0000269|PubMed:15817460}. CC -!- INTERACTION: CC P02454; Q9UBG0: MRC2; Xeno; NbExp=2; IntAct=EBI-915744, EBI-1104992; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. CC In bones the fibrils are mineralized with calcium hydroxyapatite. 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. {ECO:0000250}. CC -!- PTM: Contains mostly 4-hydroxyproline. Proline residues at the third CC position of the tripeptide repeating unit (G-X-Y) are hydroxylated in CC some or all of the chains. {ECO:0000269|PubMed:5411206}. 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:P11087}. 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:P02457}. CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked CC glycan consists of a Glc-Gal disaccharide. CC {ECO:0000269|PubMed:5411206}. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z78279; CAB01633.1; -; mRNA. DR EMBL; CH473948; EDM05727.1; -; Genomic_DNA. DR EMBL; BC133728; AAI33729.1; -; mRNA. DR EMBL; M11432; AAA40832.1; ALT_SEQ; mRNA. DR PIR; A90559; CGRT1S. DR RefSeq; NP_445756.1; NM_053304.1. DR PDB; 3HQV; Fiber; 5.16 A; A/C=152-1207. DR PDB; 3HR2; Fiber; 5.16 A; A/C=152-1207. DR PDBsum; 3HQV; -. DR PDBsum; 3HR2; -. DR AlphaFoldDB; P02454; -. DR SMR; P02454; -. DR BioGRID; 248045; 4. DR ComplexPortal; CPX-3104; Collagen type I trimer. DR DIP; DIP-36887N; -. DR IntAct; P02454; 6. DR STRING; 10116.ENSRNOP00000005311; -. DR GlyCosmos; P02454; 4 sites, No reported glycans. DR GlyGen; P02454; 4 sites. DR iPTMnet; P02454; -. DR PhosphoSitePlus; P02454; -. DR jPOST; P02454; -. DR PaxDb; 10116-ENSRNOP00000005311; -. DR Ensembl; ENSRNOT00000005311.7; ENSRNOP00000005311.5; ENSRNOG00000003897.7. DR Ensembl; ENSRNOT00055055926; ENSRNOP00055046083; ENSRNOG00055032354. DR Ensembl; ENSRNOT00060034429; ENSRNOP00060028260; ENSRNOG00060019866. DR Ensembl; ENSRNOT00065033789; ENSRNOP00065027042; ENSRNOG00065020003. DR GeneID; 29393; -. DR KEGG; rno:29393; -. DR UCSC; RGD:61817; rat. DR AGR; RGD:61817; -. DR CTD; 1277; -. DR RGD; 61817; Col1a1. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000156584; -. DR HOGENOM; CLU_001074_2_3_1; -. DR InParanoid; P02454; -. DR OMA; YYDRDVW; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P02454; -. DR TreeFam; TF344135; -. DR Reactome; R-RNO-114604; GPVI-mediated activation cascade. DR Reactome; R-RNO-1442490; Collagen degradation. DR Reactome; R-RNO-1474244; Extracellular matrix organization. DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall. DR Reactome; R-RNO-216083; Integrin cell surface interactions. DR Reactome; R-RNO-2243919; Crosslinking of collagen fibrils. DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-RNO-3000178; ECM proteoglycans. DR Reactome; R-RNO-430116; GP1b-IX-V activation signalling. DR Reactome; R-RNO-75892; Platelet Adhesion to exposed collagen. DR Reactome; R-RNO-76009; Platelet Aggregation (Plug Formation). DR Reactome; R-RNO-8874081; MET activates PTK2 signaling. DR Reactome; R-RNO-8948216; Collagen chain trimerization. DR EvolutionaryTrace; P02454; -. DR PRO; PR:P02454; -. DR Proteomes; UP000002494; Chromosome 10. DR Proteomes; UP000234681; Chromosome 10. DR Bgee; ENSRNOG00000003897; Expressed in quadriceps femoris and 18 other cell types or tissues. DR GO; GO:0005581; C:collagen trimer; ISO:RGD. DR GO; GO:0005584; C:collagen type I trimer; ISO:RGD. DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0031012; C:extracellular matrix; ISO:RGD. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:RGD. DR GO; GO:0030141; C:secretory granule; IDA:RGD. DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:RGD. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD. DR GO; GO:0002020; F:protease binding; ISO:RGD. DR GO; GO:0001568; P:blood vessel development; ISO:RGD. DR GO; GO:0060346; P:bone trabecula formation; ISO:RGD. DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; ISO:RGD. DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD. DR GO; GO:1902618; P:cellular response to fluoride; IEP:RGD. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD. DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD. DR GO; GO:0071306; P:cellular response to vitamin E; IEP:RGD. DR GO; GO:0032964; P:collagen biosynthetic process; ISO:RGD. DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD. DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IDA:MGI. DR GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD. DR GO; GO:0001958; P:endochondral ossification; ISO:RGD. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0060325; P:face morphogenesis; ISO:RGD. DR GO; GO:0001957; P:intramembranous ossification; ISO:RGD. DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:RGD. DR GO; GO:0001503; P:ossification; IEP:RGD. DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD. DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD. DR GO; GO:0015031; P:protein transport; ISO:RGD. DR GO; GO:0051591; P:response to cAMP; IEP:RGD. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:1902617; P:response to fluoride; IEP:RGD. DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD. DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD. DR GO; GO:0032868; P:response to insulin; IEP:RGD. DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD. DR GO; GO:0007584; P:response to nutrient; IEP:RGD. DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD. DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD. DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD. DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD. DR GO; GO:0001501; P:skeletal system development; ISO:RGD. DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD. DR GO; GO:0043588; P:skin development; ISO:RGD. DR GO; GO:0043589; P:skin morphogenesis; ISO:RGD. DR GO; GO:0034505; P:tooth mineralization; ISO:RGD. DR GO; GO:0007601; P:visual perception; ISO:RGD. 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:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 9. 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. DR Genevisible; P02454; RN. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Collagen; Direct protein sequencing; Disulfide bond; KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding; KW Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..151 FT /note="N-terminal propeptide" FT /evidence="ECO:0000269|PubMed:5777344" FT /id="PRO_0000043358" FT CHAIN 152..1207 FT /note="Collagen alpha-1(I) chain" FT /id="PRO_0000043359" FT PROPEP 1208..1453 FT /note="C-terminal propeptide" FT /evidence="ECO:0000250" FT /id="PRO_0000043360" FT DOMAIN 29..87 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 1218..1453 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 97..1206 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 152..167 FT /note="Nonhelical region (N-terminal)" FT REGION 168..1181 FT /note="Triple-helical region" FT REGION 1176..1186 FT /note="Major antigenic determinant (of neutral salt- FT extracted rat skin collagen)" FT REGION 1182..1207 FT /note="Nonhelical region (C-terminal)" FT MOTIF 734..736 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1082..1084 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 108..144 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 172..215 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 538..554 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 831..845 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 877..891 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1165..1184 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1266 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1268 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1269 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1271 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1274 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 152 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:5777344" FT MOD_RES 160 FT /note="Allysine" FT /evidence="ECO:0000269|PubMed:5777344" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 179 FT /note="4-hydroxyproline" FT /evidence="ECO:0000305|PubMed:4290711" FT MOD_RES 182 FT /note="4-hydroxyproline" FT /evidence="ECO:0000305|PubMed:4290711" FT MOD_RES 185 FT /note="4-hydroxyproline" FT /evidence="ECO:0000305|PubMed:4290711" FT MOD_RES 194 FT /note="4-hydroxyproline" FT /evidence="ECO:0000305|PubMed:4290711" FT MOD_RES 197 FT /note="4-hydroxyproline" FT /evidence="ECO:0000305|PubMed:4290711" FT MOD_RES 200 FT /note="4-hydroxyproline" FT /evidence="ECO:0000305|PubMed:4290711" FT MOD_RES 215 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 230 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 236 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 245 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 251 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 254 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:5411206" FT MOD_RES 260 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 278 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 281 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 287 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 296 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 302 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 323 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 332 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 335 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 362 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 365 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 377 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 383 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 392 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 398 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 401 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 416 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 419 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 425 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 428 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 440 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 449 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 464 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 470 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 479 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 485 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 494 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 503 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 512 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 518 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 524 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 533 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 536 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 545 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 554 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 560 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 572 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 581 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 590 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 593 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 611 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 629 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 635 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 641 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 647 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 653 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 659 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 671 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 680 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 692 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 704 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 707 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 713 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 719 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 728 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 740 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 746 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 761 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 767 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 776 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 788 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 794 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 797 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 806 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 812 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 830 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 839 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 848 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 851 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 860 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 866 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 874 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 875 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 884 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 887 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 908 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 917 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 926 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 935 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 953 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 962 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 965 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 971 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 986 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 992 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 998 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1007 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1013 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1022 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1034 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1037 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1040 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1085 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1097 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1109 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1112 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1115 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1133 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1148 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1153 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1154 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1168 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1169 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1171 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1172 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1174 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1175 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1178 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1181 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1197 FT /note="Allysine" FT /evidence="ECO:0000250|UniProtKB:P02453" FT CARBOHYD 56 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 254 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:5411206" FT CARBOHYD 1097 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT CARBOHYD 1354 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 1248..1280 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1254 FT /note="Interchain (with C-1271)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1271 FT /note="Interchain (with C-1254)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1288..1451 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1359..1404 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT CONFLICT 143 FT /note="P -> L (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 202 FT /note="A -> G (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 209 FT /note="R -> P (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 232 FT /note="E -> Q (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 268 FT /note="D -> N (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 286 FT /note="A -> T (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 307 FT /note="S -> T (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="N -> D (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 421 FT /note="N -> T (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 497 FT /note="A -> S (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 773 FT /note="T -> A (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 794 FT /note="P -> A (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 958 FT /note="E -> K (in Ref. 1; CAB01633)" FT /evidence="ECO:0000305" FT CONFLICT 1111 FT /note="S -> P (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1163 FT /note="S -> A (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1166 FT /note="A -> S (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1187 FT /note="F -> L (in Ref. 14; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1190 FT /note="L -> F (in Ref. 14; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 1453 AA; 137953 MW; BCDDC40C3167AE59 CRC64; MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPDVCL ICICHNGTAV CDGVLCKEDL DCPNPQKREG ECCPFCPEEY VSPDAEVIGV EGPKGDPGPQ GPRGPVGPPG QDGIPGQPGL PGPPGPPGPP GPPGLGGNFA SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG ARGLPGTAGL PGMKGHRGFS GLDGAKGDTG PAGPKGEPGS PGENGAPGQM GPRGLPGERG RPGPPGSAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAAGA KGEAGPQGAR GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG PAGEEGKRGA RGEPGPSGLP GPPGERGGPG SRGFPGADGV AGPKGPAGER GSPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGVP GPPGAVGPAG KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD TGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK GADGSPGKDG VRGLTGPIGP PGPAGAPGDK GETGPSGPAG PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG PIGNVGAPGP KGSRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE SGREGSPGAE GSPGRDGAPG AKGDRGETGP AGPPGAPGAP GAPGPVGPAG KNGDRGETGP AGPAGPIGPA GARGPAGPQG PRGDKGETGE QGDRGIKGHR GFSGLQGPPG SPGSPGEQGP SGASGPAGPR GPPGSAGSPG KDGLNGLPGP IGPPGPRGRT GDSGPAGPPG PPGPPGPPGP PSGGYDFSFL PQPPQEKSQD GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD LKMCHSDWKS GEYWIDPNQG CNLDAIKVYC NMETGQTCVF PTQPSVPQKN WYISPNPKEK KHVWFGESMT DGFQFEYGSE GSDPADVAIQ LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKSLLLQ GSNEIELRGE GNSRFTYSTL VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD QEFGMDIGPA CFV //