CO1A1_RAT
ID CO1A1_RAT Reviewed; 1453 AA.
AC P02454; A3KNA1; P02455; Q63079;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 5.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Collagen alpha-1(I) chain;
DE AltName: Full=Alpha-1 type I collagen;
DE Flags: Precursor;
GN Name=Col1a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Bone, and Tooth;
RX PubMed=10065941; DOI=10.1177/00220345990780010101;
RA Brandsten C., Lundmark C., Christersson C., Hammarstroem L., Wurtz T.;
RT "Expression of collagen alpha1(I) mRNA variants during tooth and bone
RT formation in the rat.";
RL J. Dent. Res. 78:11-19(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 152-170, ALLYSINE AT LYS-160, AND PYROGLUTAMATE
RP FORMATION AT GLN-152.
RX PubMed=5777344; DOI=10.1021/bi00829a010;
RA Bornstein P.;
RT "Comparative sequence studies of rat skin and tendon collagen. II. The
RT absence of a short sequence at the amino terminus of the skin alpha-1
RT chain.";
RL Biochemistry 8:63-71(1969).
RN [5]
RP PROTEIN SEQUENCE OF 156-170.
RX PubMed=5337886; DOI=10.1021/bi00855a019;
RA Kang A.H., Bornstein P., Piez K.A.;
RT "The amino acid sequence of peptides from the cross-linking region of rat
RT skin collagen.";
RL Biochemistry 6:788-795(1967).
RN [6]
RP PROTEIN SEQUENCE OF 171-206, AND HYDROXYLATION AT PRO-179; PRO-182;
RP PRO-185; PRO-194; PRO-197 AND PRO-200.
RX PubMed=4290711; DOI=10.1016/s0021-9258(18)96002-3;
RA Bornstein P.;
RT "The incomplete hydroxylation of individual prolyl residues in collagen.";
RL J. Biol. Chem. 242:2572-2574(1967).
RN [7]
RP PROTEIN SEQUENCE OF 207-253.
RX PubMed=4327399; DOI=10.1021/bi00787a018;
RA Butler W.T., Ponds S.L.;
RT "Chemical studies on the cyanogen bromide peptides of rat skin collagen.
RT Amino acid sequence of alpha 1-CB4.";
RL Biochemistry 10:2076-2081(1971).
RN [8]
RP PROTEIN SEQUENCE OF 254-290, HYDROXYLATION AT LYS-254, AND GLYCOSYLATION AT
RP LYS-254.
RX PubMed=5411206; DOI=10.1021/bi00803a006;
RA Butler W.T.;
RT "Chemical studies on the cyanogen bromide peptides of rat skin collagen.
RT The covalent structure of alpha 1-CB5, the major hexose-containing cyanogen
RT bromide peptide of alpha 1.";
RL Biochemistry 9:44-50(1970).
RN [9]
RP PROTEIN SEQUENCE OF 291-389.
RX PubMed=4335087; DOI=10.1021/bi00800a019;
RA Balian G., Click E.M., Bornstein P.;
RT "Structure of rat skin collagen alpha 1-CB8. Amino acid sequence of the
RT hydroxylamine-produced fragment HA1.";
RL Biochemistry 10:4470-4478(1971).
RN [10]
RP PROTEIN SEQUENCE OF 390-569.
RX PubMed=4342027; DOI=10.1021/bi00770a020;
RA Balian G., Click E.M., Hermodson M.A., Bornstein P.;
RT "Structure of rat skin collagen alpha 1-CBB. Amino acid sequence of the
RT hydroxyl amine-produced fragment HA2.";
RL Biochemistry 11:3798-3806(1972).
RN [11]
RP PROTEIN SEQUENCE OF 570-718.
RX PubMed=4366532; DOI=10.1021/bi00711a025;
RA Butler W.T., Underwood S.P., Finch J.E. Jr.;
RT "Chemical studies on the cyanogen bromide peptides of rat skin collagen.
RT Amino acid sequence of alpha 1-CB3.";
RL Biochemistry 13:2946-2953(1974).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 680-718.
RX PubMed=6395893; DOI=10.1021/bi00320a049;
RA Genovese C., Rowe D., Kream B.;
RT "Construction of DNA sequences complementary to rat alpha 1 and alpha 2
RT collagen mRNA and their use in studying the regulation of type I collagen
RT synthesis by 1,25-dihydroxyvitamin D.";
RL Biochemistry 23:6210-6216(1984).
RN [13]
RP PROTEIN SEQUENCE OF 1103-1186.
RX PubMed=4126850; DOI=10.1111/j.1432-1033.1973.tb02987.x;
RA Stoltz M., Timpl R., Furthmayr H., Kuehn K.;
RT "Structural and immunogenic properties of a major antigenic determinant in
RT neutral salt-extracted rat-skin collagen.";
RL Eur. J. Biochem. 37:287-294(1973).
RN [14]
RP PROTEIN SEQUENCE OF 1186-1206.
RX PubMed=4636751; DOI=10.1016/0014-5793(72)80542-8;
RA Stoltz M., Timpl R., Kuehn K.;
RT "Non-helical regions in rat collagen alpha 1-chain.";
RL FEBS Lett. 26:61-65(1972).
RN [15]
RP INTERACTION WITH MRC2.
RC STRAIN=Sprague-Dawley;
RX PubMed=15817460; DOI=10.1074/jbc.m501155200;
RA Thomas E.K., Nakamura M., Wienke D., Isacke C.M., Pozzi A., Liang P.;
RT "Endo180 binds to the C-terminal region of type I collagen.";
RL J. Biol. Chem. 280:22596-22605(2005).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION.
RA Xiong X., Ghosh R., Hiller E., Drepper F., Knapp B., Brunner H., Rupp S.;
RT "A new procedure for rapid, high yield purification of Type I collagen for
RT tissue engineering.";
RL Process Biochem. 44:1200-1212(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-260 AND SER-776, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (5.16 ANGSTROMS) OF 152-1207.
RX PubMed=16751282; DOI=10.1073/pnas.0502718103;
RA Orgel J.P.R.O., Irving T.C., Miller A., Wess T.J.;
RT "Microfibrillar structure of type I collagen in situ.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9001-9005(2006).
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 (PubMed:15817460). Interacts with TRAM2. Interacts with MFAP4
CC in a Ca (2+)-dependent manner. {ECO:0000250|UniProtKB:P02452,
CC ECO:0000250|UniProtKB:P02453, ECO:0000269|PubMed:15817460}.
CC -!- INTERACTION:
CC P02454; Q9UBG0: MRC2; Xeno; NbExp=2; IntAct=EBI-915744, EBI-1104992;
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. {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:5411206}.
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:0000269|PubMed:5411206}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; Z78279; CAB01633.1; -; mRNA.
DR EMBL; CH473948; EDM05727.1; -; Genomic_DNA.
DR EMBL; BC133728; AAI33729.1; -; mRNA.
DR EMBL; M11432; AAA40832.1; ALT_SEQ; mRNA.
DR PIR; A90559; CGRT1S.
DR RefSeq; NP_445756.1; NM_053304.1.
DR PDB; 3HQV; Fiber; 5.16 A; A/C=152-1207.
DR PDB; 3HR2; Fiber; 5.16 A; A/C=152-1207.
DR PDBsum; 3HQV; -.
DR PDBsum; 3HR2; -.
DR AlphaFoldDB; P02454; -.
DR SMR; P02454; -.
DR BioGRID; 248045; 4.
DR ComplexPortal; CPX-3104; Collagen type I trimer.
DR DIP; DIP-36887N; -.
DR IntAct; P02454; 5.
DR STRING; 10116.ENSRNOP00000005311; -.
DR GlyGen; P02454; 4 sites.
DR iPTMnet; P02454; -.
DR PhosphoSitePlus; P02454; -.
DR jPOST; P02454; -.
DR PaxDb; P02454; -.
DR PRIDE; P02454; -.
DR Ensembl; ENSRNOT00000005311; ENSRNOP00000005311; ENSRNOG00000003897.
DR GeneID; 29393; -.
DR KEGG; rno:29393; -.
DR UCSC; RGD:61817; rat.
DR CTD; 1277; -.
DR RGD; 61817; Col1a1.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000156584; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; P02454; -.
DR OMA; YYDRDVW; -.
DR OrthoDB; 337699at2759; -.
DR PhylomeDB; P02454; -.
DR TreeFam; TF344135; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1474244; Extracellular matrix organization.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-430116; GP1b-IX-V activation signalling.
DR Reactome; R-RNO-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-RNO-76009; Platelet Aggregation (Plug Formation).
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8948216; Collagen chain trimerization.
DR EvolutionaryTrace; P02454; -.
DR PRO; PR:P02454; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000003897; Expressed in quadriceps femoris and 18 other tissues.
DR Genevisible; P02454; RN.
DR GO; GO:0005581; C:collagen trimer; ISO:RGD.
DR GO; GO:0005584; C:collagen type I trimer; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0060346; P:bone trabecula formation; ISO:RGD.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:1902618; P:cellular response to fluoride; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0071306; P:cellular response to vitamin E; IEP:RGD.
DR GO; GO:0032964; P:collagen biosynthetic process; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IDA:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0001957; P:intramembranous ossification; ISO:RGD.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
DR GO; GO:0015031; P:protein transport; ISO:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0031960; P:response to corticosteroid; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:1902617; P:response to fluoride; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0043589; P:skin morphogenesis; ISO:RGD.
DR GO; GO:0044691; P:tooth eruption; IEP:RGD.
DR GO; GO:0034505; P:tooth mineralization; ISO:RGD.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IMP:RGD.
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 3D-structure; 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..151
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000269|PubMed:5777344"
FT /id="PRO_0000043358"
FT CHAIN 152..1207
FT /note="Collagen alpha-1(I) chain"
FT /id="PRO_0000043359"
FT PROPEP 1208..1453
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043360"
FT DOMAIN 29..87
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 97..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..167
FT /note="Nonhelical region (N-terminal)"
FT REGION 168..1181
FT /note="Triple-helical region"
FT REGION 1176..1186
FT /note="Major antigenic determinant (of neutral salt-
FT extracted rat skin collagen)"
FT REGION 1182..1207
FT /note="Nonhelical region (C-terminal)"
FT MOTIF 734..736
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1082..1084
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 108..144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1184
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 MOD_RES 152
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:5777344"
FT MOD_RES 160
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:5777344"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 179
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:4290711"
FT MOD_RES 182
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:4290711"
FT MOD_RES 185
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:4290711"
FT MOD_RES 194
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:4290711"
FT MOD_RES 197
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:4290711"
FT MOD_RES 200
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:4290711"
FT MOD_RES 215
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 230
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 236
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 245
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 251
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 254
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:5411206"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 278
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 281
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 287
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 296
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 302
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 323
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 332
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 335
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 362
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 365
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 377
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 383
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 392
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 398
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 401
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 416
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 419
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 425
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 428
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 440
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 449
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 464
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 470
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 479
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 485
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 494
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 503
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 512
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 518
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 524
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 533
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 536
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 545
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 554
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 560
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 572
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 581
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 590
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 593
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 611
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 629
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 635
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 641
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 647
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 653
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 659
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 671
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 680
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 692
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 704
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 707
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 713
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 719
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 728
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 740
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 746
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 761
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 767
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 788
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 794
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 797
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 806
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 812
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 830
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 839
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 848
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 851
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 860
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 866
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
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:0000250|UniProtKB:P11087"
FT MOD_RES 884
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 887
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 908
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 917
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 926
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 935
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 953
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 962
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 965
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 971
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 986
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 992
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 998
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1007
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1013
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1022
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1034
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1037
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1040
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1085
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1097
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1109
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1112
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1115
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1133
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1148
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1153
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1154
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
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:0000250|UniProtKB:P11087"
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:0000250|UniProtKB:P11087"
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:0000250|UniProtKB:P11087"
FT MOD_RES 1178
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
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:P02453"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:5411206"
FT CARBOHYD 1097
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 143
FT /note="P -> L (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="A -> G (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="R -> P (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="E -> Q (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="D -> N (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> T (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="S -> T (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="N -> D (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="N -> T (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> S (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="T -> A (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="P -> A (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 958
FT /note="E -> K (in Ref. 1; CAB01633)"
FT /evidence="ECO:0000305"
FT CONFLICT 1111
FT /note="S -> P (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1163
FT /note="S -> A (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1166
FT /note="A -> S (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1187
FT /note="F -> L (in Ref. 14; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="L -> F (in Ref. 14; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1453 AA; 137953 MW; BCDDC40C3167AE59 CRC64;
MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPDVCL ICICHNGTAV
CDGVLCKEDL DCPNPQKREG ECCPFCPEEY VSPDAEVIGV EGPKGDPGPQ GPRGPVGPPG
QDGIPGQPGL PGPPGPPGPP GPPGLGGNFA SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG
PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG
ARGLPGTAGL PGMKGHRGFS GLDGAKGDTG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
RPGPPGSAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAAGA KGEAGPQGAR GSEGPQGVRG
EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF PGARGPSGPQ GPSGAPGPKG
NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG PAGEEGKRGA RGEPGPSGLP GPPGERGGPG
SRGFPGADGV AGPKGPAGER GSPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG
KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGVP GPPGAVGPAG
KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ GVPGDLGAPG
PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD TGAPGAPGSQ GAPGLQGMPG
ERGAAGLPGP KGDRGDAGPK GADGSPGKDG VRGLTGPIGP PGPAGAPGDK GETGPSGPAG
PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG
PIGNVGAPGP KGSRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG
ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV GLPGQRGERG
FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE SGREGSPGAE GSPGRDGAPG
AKGDRGETGP AGPPGAPGAP GAPGPVGPAG KNGDRGETGP AGPAGPIGPA GARGPAGPQG
PRGDKGETGE QGDRGIKGHR GFSGLQGPPG SPGSPGEQGP SGASGPAGPR GPPGSAGSPG
KDGLNGLPGP IGPPGPRGRT GDSGPAGPPG PPGPPGPPGP PSGGYDFSFL PQPPQEKSQD
GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD LKMCHSDWKS
GEYWIDPNQG CNLDAIKVYC NMETGQTCVF PTQPSVPQKN WYISPNPKEK KHVWFGESMT
DGFQFEYGSE GSDPADVAIQ LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKSLLLQ
GSNEIELRGE GNSRFTYSTL VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD
QEFGMDIGPA CFV
