ID CO1A1_BOVIN Reviewed; 1463 AA. AC P02453; Q3MHM2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 3. DT 02-SEP-2026, entry version 183. DE RecName: Full=Collagen alpha-1(I) chain; DE AltName: Full=Alpha-1 type I collagen; DE Flags: Precursor; GN Name=COL1A1; 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 MRNA]. RC STRAIN=Hereford; TISSUE=Fetal liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 162-180, ALLYSINE AT LYS-170, AND PYROGLUTAMATE RP FORMATION AT GLN-162. RX PubMed=4115172; DOI=10.1111/j.1432-1033.1972.tb01831.x; RA Rauterberg J., Timpl R., Furthmayr H.; RT "Structural characterization of N-terminal antigenic determinants in calf RT and human collagen."; RL Eur. J. Biochem. 27:231-237(1972). RN [3] RP PROTEIN SEQUENCE OF 181-306, AND HYDROXYLATION AT LYS-264. RX PubMed=1164916; DOI=10.1111/j.1432-1033.1975.tb03974.x; RA Fietzek P.P., Kuehn K.; RT "The covalent structure of collagen: amino-acid sequence of the cyanogen- RT bromide peptides alpha-1-CB2, alpha-1-CB4 and alpha-1-CB5 from calf-skin RT collagen."; RL Eur. J. Biochem. 52:77-82(1975). RN [4] RP PROTEIN SEQUENCE OF 580-728. RX PubMed=4673951; DOI=10.1016/0014-5793(72)80545-3; RA Fietzek P.P., Wendt P., Kell I., Kuehn K.; RT "The covalent structure of collagen: amino acid sequence of alpha-1-CB3 RT from calf skin collagen."; RL FEBS Lett. 26:74-76(1972). RN [5] RP PROTEIN SEQUENCE OF 729-999. RX PubMed=4359390; DOI=10.1111/j.1432-1033.1973.tb03072.x; RA Fietzek P.P., Rexrodt F.W., Hopper K.E., Kuehn K.; RT "The covalent structure of collagen. 2. The amino-acid sequence of alpha-1- RT CB7 from calf-skin collagen."; RL Eur. J. Biochem. 38:396-400(1973). RN [6] RP PROTEIN SEQUENCE OF 1000-1112. RX PubMed=4343808; DOI=10.1111/j.1432-1033.1972.tb02084.x; RA Wendt P., Mark K.V.D., Rexrodt F., Kuehn K.; RT "The covalent structure of collagen. The amino-acid sequence of the 112- RT residues. Amino-terminal part of peptide alpha-1-CB6 from calf-skin RT collagen."; RL Eur. J. Biochem. 30:169-183(1972). RN [7] RP PROTEIN SEQUENCE OF 1113-1188. RX PubMed=4343807; DOI=10.1111/j.1432-1033.1972.tb02083.x; RA Fietzek P.P., Rexrodt F.W., Wendt P., Stark M., Kuehn K.; RT "The covalent structure of collagen. Amino-acid sequence of peptide alpha- RT 1-CB6-C2."; RL Eur. J. Biochem. 30:163-168(1972). RN [8] RP PROTEIN SEQUENCE OF 1196-1215, ALLYSINE AT LYS-1207, AND HYDROXYLATION AT RP PRO-1163. RX PubMed=11946479; DOI=10.1016/0014-5793(72)80167-4; RA Rauterberg J., Fietzek P., Rexrodt F., Becker U., Stark M., Kuehn K.; RT "The amino acid sequence of the carboxyterminal nonhelical cross link RT region of the alpha 1 chain of calf skin collagen."; RL FEBS Lett. 21:75-79(1972). RN [9] RP HYDROXYLATION AT PRO-1178; PRO-1179; PRO-1181; PRO-1182; PRO-1185 AND RP PRO-1188, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25645914; DOI=10.1074/jbc.m114.634915; RA Hudson D.M., Joeng K.S., Werther R., Rajagopal A., Weis M., Lee B.H., RA Eyre D.R.; RT "Post-translationally abnormal collagens of prolyl 3-hydroxylase-2 null RT mice offer a pathobiological mechanism for the high myopia linked to human RT LEPREL1 mutations."; RL J. Biol. Chem. 290:8613-8622(2015). RN [10] RP INTERACTION WITH MFAP4. RX PubMed=26601954; DOI=10.1074/jbc.m115.681775; RA Pilecki B., Holm A.T., Schlosser A., Moeller J.B., Wohl A.P., Zuk A.V., RA Heumueller S.E., Wallis R., Moestrup S.K., Sengle G., Holmskov U., RA Sorensen G.L.; RT "Characterization of microfibrillar-associated protein 4 (MFAP4) as a RT tropoelastin- and fibrillin-binding protein involved in elastic fiber RT formation."; RL J. Biol. Chem. 291:1103-1114(2016). 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 (By similarity). Interacts with TRAM2 (By similarity). CC Interacts with MFAP4 in a Ca (2+)-dependent manner (PubMed:26601954). CC {ECO:0000250|UniProtKB:P02452, ECO:0000250|UniProtKB:P02454, CC ECO:0000269|PubMed:26601954}. 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 (By similarity). {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:1164916, CC ECO:0000269|PubMed:11946479}. 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:0000269|PubMed:11946479}. 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:0000250|UniProtKB:P11087}. 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; BC105184; AAI05185.1; -; mRNA. DR PIR; A91193; CGBO1S. DR RefSeq; NP_001029211.1; NM_001034039.2. DR AlphaFoldDB; P02453; -. DR BMRB; P02453; -. DR SMR; P02453; -. DR ComplexPortal; CPX-3101; Collagen type I trimer. DR FunCoup; P02453; 589. DR IntAct; P02453; 1. DR STRING; 9913.ENSBTAP00000017420; -. DR GlyCosmos; P02453; 2 sites, No reported glycans. DR GlyGen; P02453; 6 sites. DR PaxDb; 9913-ENSBTAP00000017420; -. DR PeptideAtlas; P02453; -. DR Ensembl; ENSBTAT00000017420.6; ENSBTAP00000017420.3; ENSBTAG00000013103.8. DR Ensembl; ENSBTAT00090074545; ENSBTAP00090041208; ENSBTAG00090035093. DR GeneID; 282187; -. DR KEGG; bta:282187; -. DR CTD; 1277; -. DR VEuPathDB; HostDB:ENSBTAG00000013103; -. DR VGNC; VGNC:27560; COL1A1. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000156584; -. DR HOGENOM; CLU_001074_2_3_1; -. DR InParanoid; P02453; -. DR OMA; YYDRDVW; -. DR OrthoDB; 8939548at2759; -. DR PRO; PR:P02453; -. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000013103; Expressed in uterine cervix and 103 other cell types or tissues. DR ExpressionAtlas; P02453; baseline. DR GO; GO:0005584; C:collagen type I trimer; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl. DR GO; GO:0002020; F:protease binding; IEA:Ensembl. DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central. DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl. DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl. DR GO; GO:0048705; P:skeletal system morphogenesis; IBA:GO_Central. DR GO; GO:0043588; P:skin development; IBA:GO_Central. DR GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl. DR GO; GO:0034505; P:tooth mineralization; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IEA:Ensembl. DR FunFam; 2.60.120.1000:FF:000001; Collagen alpha-1 type I chain; 1. DR FunFam; 2.10.70.10:FF:000013; Collagen, type I, alpha 1; 1. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR050149; Collagen_superfamily. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 10. 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 Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..161 FT /note="N-terminal propeptide" FT /evidence="ECO:0000269|PubMed:4115172" FT /id="PRO_0000236804" FT CHAIN 162..1217 FT /note="Collagen alpha-1(I) chain" FT /evidence="ECO:0000305|PubMed:11946479" FT /id="PRO_0000059396" FT PROPEP 1218..1463 FT /note="C-terminal propeptide" FT /evidence="ECO:0000305|PubMed:11946479" FT /id="PRO_0000236805" FT DOMAIN 38..96 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 1228..1463 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 98..1217 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 162..177 FT /note="Nonhelical region (N-terminal)" FT REGION 178..1191 FT /note="Triple-helical region" FT REGION 1192..1215 FT /note="Nonhelical region (C-terminal)" FT MOTIF 744..746 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1092..1094 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 138..153 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..216 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..242 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 278..294 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 317..330 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 332..344 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 349..358 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 378..417 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 484..493 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 494..525 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 537..563 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 572..591 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 633..660 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 695..723 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 783..797 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 810..837 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 839..851 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 852..882 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 930..954 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 995..1005 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1041..1056 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1077..1091 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1092..1106 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1125..1149 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1176..1191 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1206..1217 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1276 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1278 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1279 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1281 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1284 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 162 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:4115172" FT MOD_RES 170 FT /note="Allysine" FT /evidence="ECO:0000269|PubMed:4115172" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 189 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 192 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 195 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 204 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 207 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 210 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 225 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 240 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 246 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 255 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 261 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 264 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:1164916" FT MOD_RES 270 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 276 FT /note="5-hydroxylysine" FT /evidence="ECO:0000255" FT MOD_RES 285 FT /note="5-hydroxylysine" FT /evidence="ECO:0000255" FT MOD_RES 288 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 291 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 297 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 306 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 312 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 333 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 342 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 345 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 372 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 375 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 387 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 393 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 402 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 408 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 411 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 426 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 429 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 435 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 438 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 450 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 459 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 474 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 480 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 489 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 495 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 504 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 513 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 522 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 528 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 534 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 543 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 546 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 555 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 564 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 570 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 582 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 591 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 600 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 603 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 621 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 639 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 645 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 651 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 657 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 663 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 669 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 681 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 690 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 702 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 714 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 717 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 723 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 729 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 738 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 750 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 756 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 771 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 777 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 786 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 798 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 804 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 807 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 816 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 822 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 840 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 849 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 858 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 861 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 870 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 876 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 884 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 885 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 894 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 897 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 918 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 927 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 936 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 945 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 963 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 972 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 975 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 981 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 996 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1002 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1008 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1017 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1023 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1032 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1044 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1047 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1050 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1095 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1107 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1119 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1122 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1125 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1143 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1158 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1163 FT /note="3-hydroxyproline" FT /evidence="ECO:0000269|PubMed:11946479" FT MOD_RES 1164 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1178 FT /note="3-hydroxyproline" FT /evidence="ECO:0000269|PubMed:25645914" FT MOD_RES 1179 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:25645914" FT MOD_RES 1181 FT /note="3-hydroxyproline" FT /evidence="ECO:0000269|PubMed:25645914" FT MOD_RES 1182 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:25645914" FT MOD_RES 1184 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1185 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:25645914" FT MOD_RES 1188 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:25645914" FT MOD_RES 1191 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1207 FT /note="Allysine" FT /evidence="ECO:0000269|PubMed:11946479" FT CARBOHYD 264 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT CARBOHYD 1107 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT DISULFID 1258..1290 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1264 FT /note="Interchain (with C-1281)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1281 FT /note="Interchain (with C-1264)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1298..1461 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1369..1414 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT CONFLICT 687 FT /note="Q -> E (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 790..792 FT /note="Missing (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 794 FT /note="A -> T (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1043 FT /note="P -> A (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1046 FT /note="A -> P (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1074 FT /note="A -> I (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1077 FT /note="I -> V (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1080 FT /note="V -> A (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1206 FT /note="E -> QZ (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 1463 AA; 138938 MW; 8A6E17F276C4C6FA CRC64; MFSFVDLRLL LLLAATALLT HGQEEGQEEG QEEDIPPVTC VQNGLRYHDR DVWKPVPCQI CVCDNGNVLC DDVICDELKD CPNAKVPTDE CCPVCPEGQE SPTDQETTGV EGPKGDTGPR GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGISVPGPM GPSGPRGLPG PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG ARGLPGTAGL PGMKGHRGFS GLDGAKGDAG PAGPKGEPGS PGENGAPGQM GPRGLPGERG RPGAPGPAGA RGNDGATGAA GPPGPTGPAG PPGFPGAVGA KGEGGPQGPR GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF PGARGPSGPQ GPSGPPGPKG NSGEPGAPGS KGDTGAKGEP GPTGIQGPPG PAGEEGKRGA RGEPGPAGLP GPPGERGGPG SRGFPGADGV AGPKGPAGER GAPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ DGRPGPPGPP GARGQAGVMG FPGPKGAAGE PGKAGERGVP GPPGAVGPAG KDGEAGAQGP PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGANG APGNDGAKGD AGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK GADGAPGKDG VRGLTGPIGP PGPAGAPGDK GEAGPSGPAG PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGEPGD AGAKGDAGPP GPAGPAGPPG PIGNVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPA GKEGSKGPRG ETGPAGRPGE VGPPGPPGPA GEKGAPGADG PAGAPGTPGP QGIAGQRGVV GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE SGREGAPGAE GSPGRDGSPG AKGDRGETGP AGPPGAPGAP GAPGPVGPAG KSGDRGETGP AGPAGPIGPV GARGPAGPQG PRGDKGETGE QGDRGIKGHR GFSGLQGPPG PPGSPGEQGP SGASGPAGPR GPPGSAGSPG KDGLNGLPGP IGPPGPRGRT GDAGPAGPPG PPGPPGPPGP PSGGYDLSFL PQPPQEKAHD GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD LKMCHSDWKS GEYWIDPNQG CNLDAIKVFC NMETGETCVY PTQPSVAQKN WYISKNPKEK RHVWYGESMT GGFQFEYGGQ GSDPADVAIQ LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKALLLQ GSNEIEIRAE GNSRFTYSVT YDGCTSHTGA WGKTVIEYKT TKTSRLPIID VAPLDVGAPD QEFGFDVGPA CFL //