ID CO1A1_CHICK Reviewed; 1453 AA. AC P02457; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 3. DT 02-SEP-2026, entry version 140. DE RecName: Full=Collagen alpha-1(I) chain; DE AltName: Full=Alpha-1 type I collagen; DE Flags: Precursor; GN Name=COL1A1; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-153. RX PubMed=3678834; DOI=10.1016/0378-1119(87)90159-4; RA Finer M.H., Boedtker H., Doty P.; RT "Construction and characterization of cDNA clones encoding the 5' end of RT the chicken pro alpha 1(I) collagen mRNA."; RL Gene 56:71-78(1987). RN [2] RP NUCLEOTIDE SEQUENCE OF 1-144. RX PubMed=2820966; DOI=10.1016/s0021-9258(18)45204-0; RA Finer M.H., Aho S., Gerstenfeld L.C., Boedtker H., Doty P.; RT "Unusual DNA sequences located within the promoter region and the first RT intron of the chicken pro-alpha 1(I) collagen gene."; RL J. Biol. Chem. 262:13323-13332(1987). RN [3] RP PROTEIN SEQUENCE OF 152-206, PYROGLUTAMATE FORMATION AT GLN-152, AND RP HYDROXYLATION AT PRO-179; PRO-182; PRO-185; PRO-194; PRO-197 AND PRO-200. RX PubMed=4313735; DOI=10.1021/bi00806a012; RA Kang A.H., Gross J.; RT "Amino acid sequence of cyanogen bromide peptides from the amino-terminal RT region of chick skicollagen."; RL Biochemistry 9:796-804(1970). RN [4] RP PROTEIN SEQUENCE OF 207-290, HYDROXYLATION AT PRO-215; PRO-230; PRO-236; RP PRO-245; PRO-251; LYS-254; PRO-269; PRO-278; PRO-281 AND PRO-287, AND RP GLYCOSYLATION AT LYS-254. RX PubMed=1165248; DOI=10.1016/s0021-9258(19)40962-9; RA Kang A.H., Dixit S.N., Corbett C., Gross J.; RT "The covalent structure of collagen. Amino acid sequence of alpha1-CB5 RT glycopeptide and alpha1-CB4 from chick skin collagen."; RL J. Biol. Chem. 250:7428-7434(1975). RN [5] RP PROTEIN SEQUENCE OF 291-569, AND HYDROXYLATION AT PRO-296; PRO-302; RP PRO-317; PRO-323; PRO-332; PRO-335; PRO-362; PRO-365; PRO-377; PRO-383; RP PRO-392; PRO-398; PRO-401; PRO-416; LYS-419; PRO-425; PRO-428; PRO-440; RP PRO-449; PRO-464; PRO-470; PRO-479; PRO-485; LYS-494; PRO-497; PRO-503; RP PRO-512; PRO-518; PRO-524; PRO-533; PRO-536; PRO-545; PRO-554 AND PRO-560. RX PubMed=7093229; DOI=10.1021/bi00538a011; RA Highberger J.H., Corbett C., Dixit S.N., Yu W., Seyer J.M., Kang A.H., RA Gross J.; RT "Amino acid sequence of chick skin collagen alpha 1(I)-CB8 and the complete RT primary structure of the helical portion of the chick skin collagen alpha RT 1(I) chain."; RL Biochemistry 21:2048-2055(1982). RN [6] RP PROTEIN SEQUENCE OF 570-718, AND HYDROXYLATION AT PRO-572; PRO-581; RP PRO-584; PRO-590; PRO-593; PRO-611; PRO-629; PRO-635; PRO-641; PRO-647; RP PRO-653; PRO-659; PRO-671; PRO-680; PRO-692; PRO-704; PRO-707 AND PRO-713. RX PubMed=1125203; DOI=10.1021/bi00680a019; RA Dixit S.N., Kang A.H., Gross J.; RT "Covalent structure of collagen: amino acid sequence of alpha1-CB3 of chick RT skin collagen."; RL Biochemistry 14:1929-1933(1975). RN [7] RP PROTEIN SEQUENCE OF 719-989, AND HYDROXYLATION AT PRO-719; PRO-728; RP PRO-737; LYS-740; PRO-746; PRO-761; PRO-767; PRO-776; PRO-788; PRO-794; RP PRO-797; PRO-806; PRO-812; PRO-830; PRO-839; PRO-848; LYS-851; PRO-860; RP PRO-866; PRO-875; PRO-884; PRO-887; PRO-908; PRO-911; PRO-917; PRO-920; RP PRO-926; PRO-935; PRO-953; PRO-962; PRO-965; PRO-971 AND PRO-986. RX PubMed=167810; DOI=10.1021/bi00684a013; RA Highberger J.H., Corbett C., Kang A.H., Gross J.; RT "The amino acid sequence of chick skin collagen alpha1-CB7."; RL Biochemistry 14:2872-2881(1975). RN [8] RP PROTEIN SEQUENCE OF 990-1096, HYDROXYLATION AT PRO-992; PRO-998; PRO-1007; RP PRO-1013; LYS-1022; PRO-1034; PRO-1037; PRO-1040; PRO-1067 AND LYS-1085, RP AND LACK OF GLYCOSYLATION AT LYS-1022 AND LYS-1085. RX PubMed=1125204; DOI=10.1021/bi00680a020; RA Dixit S.N., Seyer J.M., Oronsky A.O., Corbett C., Kang A.H., Gross J.; RT "Covalent structure of collagen: amino acid sequence of alpha1-CB6A of RT chick skin collagen."; RL Biochemistry 14:1933-1938(1975). RN [9] RP PROTEIN SEQUENCE OF 1097-1187, HYDROXYLATION AT LYS-1097; PRO-1109; RP PRO-1112; PRO-1115; PRO-1133; PRO-1148; PRO-1153; PRO-1154; PRO-1169; RP PRO-1172; PRO-1175 AND PRO-1178, AND GLYCOSYLATION AT LYS-1097. RX PubMed=728430; DOI=10.1021/bi00619a018; RA Dixit S.N., Seyer J.M., Kang A.H., Gross J.; RT "Covalent structure of collagen: amino acid sequence of chick skin collagen RT alpha1(1)-CB6B."; RL Biochemistry 17:5719-5722(1978). RN [10] RP PROTEIN SEQUENCE OF 1200-1205. RX PubMed=5047697; DOI=10.1016/0006-291x(72)90408-1; RA Eyre D.R., Glimcher M.J.; RT "Evidence for a previously undetected sequence at the carboxyterminus of RT the alpha 1 chain of chicken bone collagen."; RL Biochem. Biophys. Res. Commun. 48:720-726(1972). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 981-1453, AND C-TERMINAL PROPEPTIDE CLEAVAGE RP SITE. RX PubMed=6927845; DOI=10.1021/bi00507a054; RA Fuller F., Boedtker H.; RT "Sequence determination and analysis of the 3' region of chicken pro-alpha RT 1(I) and pro-alpha 2(I) collagen messenger ribonucleic acids including the RT carboxy-terminal propeptide sequences."; RL Biochemistry 20:996-1006(1981). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1453. RX PubMed=6987088; DOI=10.1016/0014-5793(80)80761-7; RA Showalter A.M., Pesciotta D.M., Eikenberry E.F., Yamamoto T., Pastan I., RA Decrombrugghe B., Fietzek P.P., Olsen B.R.; RT "Nucleotide sequence of a collagen cDNA-fragment coding for the carboxyl RT end of pro alpha 1(I)-chains."; RL FEBS Lett. 111:61-65(1980). 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. 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 4-hydroxylated in CC some or all of the chains. {ECO:0000269|PubMed:1125203, CC ECO:0000269|PubMed:167810, ECO:0000269|PubMed:4313735, CC ECO:0000269|PubMed:7093229, ECO:0000269|PubMed:728430}. CC -!- PTM: Contains 3-hydroxyproline. This modification occurs on the first CC proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4- CC hydroxyproline. {ECO:0000269|PubMed:728430}. 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:0000269|PubMed:1125204, ECO:0000269|PubMed:1165248, CC ECO:0000269|PubMed:728430}. CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked CC glycan consists of a Glc-Gal disaccharide. {ECO:0000269|PubMed:1165248, CC ECO:0000269|PubMed:728430}. 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; M17839; AAA48704.1; -; Genomic_DNA. DR EMBL; M17838; AAA48704.1; JOINED; Genomic_DNA. DR EMBL; V00401; CAA23695.1; -; mRNA. DR EMBL; M10571; AAA48671.1; ALT_SEQ; mRNA. DR EMBL; M17607; AAA48672.1; -; mRNA. DR PIR; A27179; A27179. DR PIR; A90458; CGCH1S. DR PIR; I50629; I50629. DR PIR; S07234; S07234. DR ComplexPortal; CPX-3102; Collagen type I trimer. DR FunCoup; P02457; 642. DR IntAct; P02457; 1. DR STRING; 9031.ENSGALP00000058148; -. DR GlyCosmos; P02457; 3 sites, No reported glycans. DR GlyGen; P02457; 9 sites. DR PaxDb; 9031-ENSGALP00000058148; -. DR VEuPathDB; HostDB:geneid_395069; -. DR VEuPathDB; HostDB:geneid_395532; -. DR VEuPathDB; HostDB:geneid_424526; -. DR InParanoid; P02457; -. DR OrthoDB; 8939548at2759; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005584; C:collagen type I trimer; IBA:GO_Central. 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:0030199; P:collagen fibril organization; IBA:GO_Central. DR GO; GO:0048705; P:skeletal system morphogenesis; IBA:GO_Central. DR GO; GO:0043588; P:skin development; IBA:GO_Central. 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. 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 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 Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..22 FT PROPEP 23..151 FT /note="N-terminal propeptide" FT /evidence="ECO:0000269|PubMed:4313735" FT /id="PRO_0000005716" FT CHAIN 152..1207 FT /note="Collagen alpha-1(I) chain" FT /evidence="ECO:0000303|PubMed:6927845" FT /id="PRO_0000005717" FT PROPEP 1208..1453 FT /note="C-terminal propeptide" FT /evidence="ECO:0000303|PubMed:6927845" FT /id="PRO_0000005718" FT DOMAIN 31..89 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 98..1203 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 106..116 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 131..143 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 162..176 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 187..206 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 265..284 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 307..319 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..334 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 350..361 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 368..418 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 463..482 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 527..581 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 623..664 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 685..722 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 800..827 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 835..883 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 890..908 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 910..920 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 985..995 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 997..1021 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1031..1046 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1070..1081 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1082..1096 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1115..1139 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1166..1181 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 SITE 1022 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:1125204" FT SITE 1085 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 152 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:4313735" FT MOD_RES 160 FT /note="Allysine" FT /evidence="ECO:0000250|UniProtKB:P02452" FT MOD_RES 179 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4313735" FT MOD_RES 182 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4313735" FT MOD_RES 185 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4313735" FT MOD_RES 194 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4313735" FT MOD_RES 197 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4313735" FT MOD_RES 200 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4313735" FT MOD_RES 215 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 230 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 236 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 245 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 251 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 254 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 269 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 278 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 281 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 287 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1165248" FT MOD_RES 296 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 302 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 317 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 323 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 332 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 335 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 362 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 365 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 377 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 383 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 392 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 398 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 401 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 416 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 419 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 425 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 428 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 440 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 449 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 464 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 470 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 479 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 485 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 494 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 497 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 503 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 512 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 518 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 524 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 533 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 536 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 545 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 554 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 560 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7093229" FT MOD_RES 572 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 581 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 584 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 590 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 593 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 611 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 629 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 635 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 641 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 647 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 653 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 659 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 671 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 680 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 692 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 704 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 707 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 713 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125203" FT MOD_RES 719 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 728 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 737 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 740 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 746 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 761 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 767 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 776 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 788 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 794 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 797 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 806 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 812 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 830 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 839 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 848 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 851 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 860 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 866 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" 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:0000269|PubMed:167810" FT MOD_RES 884 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 887 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 908 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 911 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 917 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 920 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 926 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 935 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 953 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 962 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 965 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 971 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 986 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:167810" FT MOD_RES 992 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 998 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1007 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1013 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1022 FT /note="5-hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1034 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1037 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1040 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1067 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1085 FT /note="5-hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:1125204" FT MOD_RES 1097 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:728430" FT MOD_RES 1109 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:728430" FT MOD_RES 1112 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:728430" FT MOD_RES 1115 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:728430" FT MOD_RES 1133 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:728430" FT MOD_RES 1148 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:728430" FT MOD_RES 1153 FT /note="3-hydroxyproline" FT /evidence="ECO:0000269|PubMed:728430" FT MOD_RES 1154 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:728430" 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:0000269|PubMed:728430" 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:0000269|PubMed:728430" 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:0000269|PubMed:728430" FT MOD_RES 1178 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:728430" 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:P02452" FT CARBOHYD 254 FT /note="O-linked (Gal...) hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:1165248" FT CARBOHYD 1097 FT /note="O-linked (Gal...) hydroxylysine; partial" FT /evidence="ECO:0000269|PubMed:728430" FT CARBOHYD 1354 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250" 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 1441 FT /note="Q -> H (in Ref. 12; AAA48671)" FT /evidence="ECO:0000305" SQ SEQUENCE 1453 AA; 137755 MW; 61C617239E271A82 CRC64; MFSFVDSRLL LLIAATVLLT RGEGEEDIQT GSCVQDGLTY NDKDVWKPEP CQICVCDSGN ILCDEVICED TSDCPNAEIP FGECCPICPD VDASPVYPES AGVEGPKGDT GPRGDRGLPG PPGRDGIPGQ PGLPGPPGPP GPPGLGGNFA PQMSYGYDEK SAGVAVPGPM GPAGPRGLPG PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PAGPPGKNGD DGEAGKPGRP GQRGPPGPQG ARGLPGTAGL PGMKGHRGFS GLDGAKGQPG PAGPKGEPGS PGENGAPGQM GPRGLPGERG RPGPSGPAGA RGNDGAPGAA GPPGPTGPAG PPGFPGAAGA KGETGPQGAR GSEGPQGSRG EPGPPGPAGA AGPAGNPGAD GQPGAKGATG APGIAGAPGF PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG PAGEEGKRGA RGEPGPAGLP GPAGERGAPG SRGFPGADGI AGPKGPPGER GSPGAVGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGAAGE PGKPGERGAP GPPGAVGAAG KDGEAGAQGP PGPTGPAGER GEQGPAGAPG FQGLPGPAGP PGEAGKPGEQ GVPGNAGAPG PAGARGERGF PGERGVQGPP GPQGPRGANG APGNDGAKGD AGAPGAPGNE GPPGLEGMPG ERGAAGLPGA KGDRGDPGPK GADGAPGKDG LRGLTGPIGP PGPAGAPGDK GEAGPPGPAG PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGETGD AGAKGDAGPP GPAGPTGAPG PAGZVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN IGLPGPPGPA GKZGSKGPRG ETGPAGRPGE PGPAGPPGPP GEKGSPGADG PIGAPGTPGP QGIAGQRGVV GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE AGREGAPGAE GAPGRDGAAG PKGDRGETGP AGPPGAPGAP GAPGPVGPAG KNGDRGETGP AGPAGPPGPA GARGPAGPQG PRGDKGETGE QGDRGMKGHR GFSGLQGPPG PPGAPGEQGP SGASGPAGPR GPPGSAGAAG KDGLNGLPGP IGPPGPRGRT GEVGPVGPPG PPGPPGPPGP PSGGFDLSFL PQPPQEKAHD GGRYYRADDA NVMRDRDLEV DTTLKSLSQQ IENIRSPEGT RKNPARTCRD LKMCHGDWKS GEYWIDPNQG CNLDAIKVYC NMETGETCVY PTQATIAQKN WYLSKNPKEK KHVWFGETMS DGFQFEYGGE GSNPADVAIQ LTFLRLMSTE ATQNVTYHCK NSVAYMDHDT GNLKKALLLQ GANEIEIRAE GNSRFTYGVT EDGCTSHTGA WGKTVIEYKT TKTSRLPIID LAPMDVGAPD QEFGIDIGPV CFL //