ID CO1A1_CANLF Reviewed; 1460 AA. AC Q9XSJ7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=Collagen alpha-1(I) chain; DE AltName: Full=Alpha-1 type I collagen; DE Flags: Precursor; GN Name=COL1A1; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT OI ALA-208. RC TISSUE=Skin; RX PubMed=11147834; DOI=10.1006/abbi.2000.2099; RA Campbell B.G., Wootton J.A.M., MacLeod J.N., Minor R.R.; RT "Sequence of normal canine COL1A1 cDNA and identification of a heterozygous RT alpha1(I) collagen Gly208Ala mutation in a severe case of canine RT osteogenesis imperfecta."; RL Arch. Biochem. Biophys. 384:37-46(2000). 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. Interacts with TRAM2. Interacts with MFAP4 in a Ca (2+)- CC dependent manner. {ECO:0000250|UniProtKB:P02452, CC ECO:0000250|UniProtKB:P02453, ECO:0000250|UniProtKB:P02454}. 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: 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:0000250|UniProtKB:P11087}. 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:0000250|UniProtKB:P11087}. CC -!- DISEASE: Note=Defects in COL1A1 are a cause of osteogenesis imperfecta CC (OI). 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; AF153062; AAD34619.1; -; mRNA. DR RefSeq; NP_001003090.1; NM_001003090.1. DR AlphaFoldDB; Q9XSJ7; -. DR SMR; Q9XSJ7; -. DR ComplexPortal; CPX-3103; Collagen type I trimer. DR STRING; 9615.ENSCAFP00000025056; -. DR ChEMBL; CHEMBL3751652; -. DR GlyCosmos; Q9XSJ7; 3 sites, No reported glycans. DR PaxDb; 9612-ENSCAFP00000025056; -. DR GeneID; 403651; -. DR KEGG; cfa:403651; -. DR CTD; 1277; -. DR eggNOG; KOG3544; Eukaryota. DR InParanoid; Q9XSJ7; -. DR OrthoDB; 2970887at2759; -. DR Proteomes; UP000002254; Unplaced. DR Proteomes; UP000694429; Unplaced. DR Proteomes; UP000694542; Unplaced. DR Proteomes; UP000805418; Unplaced. DR GO; GO:0005584; C:collagen type I trimer; IBA:GO_Central. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001568; P:blood vessel development; IBA:GO_Central. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0001503; P:ossification; IBA:GO_Central. DR GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central. DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central. DR GO; GO:0043588; P:skin development; IBA:GO_Central. 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:SF569; COLLAGEN ALPHA-1(I) CHAIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 11. 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; Disease variant; Disulfide bond; Extracellular matrix; KW Glycoprotein; Hydroxylation; Metal-binding; Phosphoprotein; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000250|UniProtKB:P02452" FT PROPEP 23..157 FT /note="N-terminal propeptide" FT /evidence="ECO:0000250|UniProtKB:P02452" FT /id="PRO_0000005713" FT CHAIN 158..1214 FT /note="Collagen alpha-1(I) chain" FT /evidence="ECO:0000250|UniProtKB:P02452" FT /id="PRO_0000005714" FT PROPEP 1215..1460 FT /note="C-terminal propeptide" FT /evidence="ECO:0000250|UniProtKB:P02452" FT /id="PRO_0000005715" FT DOMAIN 34..92 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 1225..1460 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 96..1213 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 158..174 FT /note="Nonhelical region (N-terminal)" FT REGION 175..1188 FT /note="Triple-helical region" FT REGION 1189..1214 FT /note="Nonhelical region (C-terminal)" FT MOTIF 741..743 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1089..1091 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 118..152 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 179..222 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 415..429 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 545..568 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 838..852 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1172..1191 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1273 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1275 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" 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 1281 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 166 FT /note="Allysine" FT /evidence="ECO:0000250|UniProtKB:P02452" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 186 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" 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 201 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 222 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 237 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 243 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 252 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 258 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 261 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 267 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 285 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 288 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 294 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 303 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 309 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 330 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 339 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 369 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 384 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 390 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 399 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 405 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 423 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 426 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 432 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 435 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 447 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 456 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 471 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 477 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 486 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 492 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 501 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 510 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 519 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 525 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 531 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 540 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 552 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 561 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 567 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 579 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 588 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 597 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 618 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 636 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 642 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 648 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 654 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 660 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 666 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 678 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 687 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 699 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 711 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 720 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 726 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 735 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 747 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 753 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 768 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 774 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 783 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 795 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 801 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 813 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 819 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 837 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 846 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 855 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 858 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 867 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 873 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 881 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 882 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 891 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 915 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 924 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 933 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 942 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 960 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 969 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 978 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 993 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 999 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1005 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1014 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1020 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1029 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1041 FT /note="4-hydroxyproline" 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 1092 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1104 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1116 FT /note="4-hydroxyproline" 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 1140 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1155 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1160 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1161 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1175 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1176 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1178 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1179 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1181 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1182 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1185 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1188 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1204 FT /note="Allysine" FT /evidence="ECO:0000250|UniProtKB:P02452" FT CARBOHYD 261 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT CARBOHYD 1104 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT CARBOHYD 1361 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250" FT DISULFID 1255..1287 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1261 FT /note="Interchain (with C-1278)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1278 FT /note="Interchain (with C-1261)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1295..1458 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1366..1411 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VARIANT 208 FT /note="G -> A (in OI; severe)" FT /evidence="ECO:0000269|PubMed:11147834" SQ SEQUENCE 1460 AA; 138762 MW; 58E3674D2B570697 CRC64; MFSFVDLRLL LLLAATALLT HGQEEGQEED IPPVTCVQNG LRYYDRDVWK PEACRICVCD NGNVLCDDVI CDETKNCPGA QVPPGECCPV CPDGEASPTD QETTGVEGPK GDTGPRGPRG PAGPPGRDGI PGQPGLPGPP GPPGPPGPPG LGGNFAPQMS YGYDEKSTGG ISVPGPMGPS GPRGLPGPPG APGPQGFQGP PGEPGEPGAS GPMGPRGPPG PPGKNGDDGE AGKPGRPGER GPPGPQGARG LPGTAGLPGM KGHRGFSGLD GAKGDAGPAG PKGEPGSPGE NGAPGQMGPR GLPGERGRPG APGPAGARGN DGATGAAGPP GPTGPAGPPG FPGAVGAKGE AGPQGARGSE GPQGVRGEPG PPGPAGAAGP AGNPGADGQP GAKGANGAPG IAGAPGFPGA RGPSGPQGPS GPPGPKGNSG EPGAPGNKGD TGAKGEPGPT GIQGPPGPAG EEGKRGARGE PGPTGLPGPP GERGGPGSRG FPGADGVAGP KGPAGERGSP GPAGPKGSPG EAGRPGEAGL PGAKGLTGSP GSPGPDGKTG PPGPAGQDGR PGPPGPPGAR GQAGVMGFPG PKGAAGEPGK AGERGVPGPP GAVGPAGKDG EAGAQGPPGP AGPAGERGEQ GPAGSPGFQG LPGPAGPPGE AGKPGEQGVP GDLGAPGPSG ARGERGFPGE RGVQGPPGPA GPRGANGAPG NDGAKGDAGA PGAPGSQGAP GLQGMPGERG AAGLPGPKGD RGDAGPKGAD GSPGKDGVRG LTGPIGPPGP AGAPGDKGEA GPSGPAGPTG ARGAPGDRGE PGPPGPAGFA GPPGADGQPG AKGEPGDAGA KGDAGPPGPA GPTGPPGPIG NVGAPGPKGA RGSAGPPGAT GFPGAAGRVG PPGPSGNAGP PGPPGPAGKE GGKGARGETG PAGRPGEVGP PGPPGPAGEK GSPGADGPAG APGTPGPQGI AGQRGVVGLP GQRGERGFPG LPGPSGEPGK QGPSGTSGER GPPGPMGPPG LAGPPGESGR EGSPGAEGSP GRDGSPGPKG DRGETGPAGP PGAPGAPGAP GPVGPAGKNG DRGETGPAGP AGPIGPVGAR GPAGPQGPRG DKGETGEQGD RGIKGHRGFS GLQGPPGPPG SPGEQGPSGA SGPAGPRGPP GSAGSPGKDG LNGLPGPIGP PGPRGRTGDA GPVGPPGPPG PPGPPGPPSG GFDFSFLPQP PQEKAHDGGR YYRADDANVV RDRDLEVDTT LKSLSQQIEN IRSPEGSRKN PARTCRDLKM CHSDWKSGEY WIDPNQGCNL DAIKVFCNME TGETCVYPTQ PQVAQKNWYI SKNPKEKRHV WYGESMTDGF QFEYGGQGSD PADVAIQLTF LRLMSTEASQ NITYHCKNSV AYMDQQTGNL KKALLLQGSN EIEIRAEGNS RFTYSVTYDG CTSHTGAWGK TVIEYKTTKT SRLPIIDVAP LDVGAPDQEF GMDIGPVCFL //