CO1A1_CANLF
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 03-AUG-2022, entry version 123.
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}.
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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 PaxDb; Q9XSJ7; -.
DR PRIDE; Q9XSJ7; -.
DR GeneID; 403651; -.
DR KEGG; cfa:403651; -.
DR CTD; 1277; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q9XSJ7; -.
DR OrthoDB; 337699at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005584; C:collagen type I trimer; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO: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 InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 12.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen; 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
