CO1A1_BOVIN
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 03-AUG-2022, entry version 166.
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}.
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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 IntAct; P02453; 1.
DR STRING; 9913.ENSBTAP00000017420; -.
DR PaxDb; P02453; -.
DR PeptideAtlas; P02453; -.
DR PRIDE; P02453; -.
DR Ensembl; ENSBTAT00000017420; ENSBTAP00000017420; ENSBTAG00000013103.
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; 337699at2759; -.
DR TreeFam; TF344135; -.
DR Reactome; R-BTA-114604; GPVI-mediated activation cascade.
DR Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000013103; Expressed in uterine cervix and 103 other tissues.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; 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; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
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:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; 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 InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
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 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 122..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..855
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1194
FT /note="Pro 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
