CO1A1_CHICK
ID CO1A1_CHICK Reviewed; 1453 AA.
AC P02457;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Collagen alpha-1(I) chain;
DE AltName: Full=Alpha-1 type I collagen;
DE Flags: Precursor;
GN Name=COL1A1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
RX PubMed=3678834; DOI=10.1016/0378-1119(87)90159-4;
RA Finer M.H., Boedtker H., Doty P.;
RT "Construction and characterization of cDNA clones encoding the 5' end of
RT the chicken pro alpha 1(I) collagen mRNA.";
RL Gene 56:71-78(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-144.
RX PubMed=2820966; DOI=10.1016/s0021-9258(18)45204-0;
RA Finer M.H., Aho S., Gerstenfeld L.C., Boedtker H., Doty P.;
RT "Unusual DNA sequences located within the promoter region and the first
RT intron of the chicken pro-alpha 1(I) collagen gene.";
RL J. Biol. Chem. 262:13323-13332(1987).
RN [3]
RP PROTEIN SEQUENCE OF 152-206, PYROGLUTAMATE FORMATION AT GLN-152, AND
RP HYDROXYLATION AT PRO-179; PRO-182; PRO-185; PRO-194; PRO-197 AND PRO-200.
RX PubMed=4313735; DOI=10.1021/bi00806a012;
RA Kang A.H., Gross J.;
RT "Amino acid sequence of cyanogen bromide peptides from the amino-terminal
RT region of chick skicollagen.";
RL Biochemistry 9:796-804(1970).
RN [4]
RP PROTEIN SEQUENCE OF 207-290, HYDROXYLATION AT PRO-215; PRO-230; PRO-236;
RP PRO-245; PRO-251; LYS-254; PRO-269; PRO-278; PRO-281 AND PRO-287, AND
RP GLYCOSYLATION AT LYS-254.
RX PubMed=1165248; DOI=10.1016/s0021-9258(19)40962-9;
RA Kang A.H., Dixit S.N., Corbett C., Gross J.;
RT "The covalent structure of collagen. Amino acid sequence of alpha1-CB5
RT glycopeptide and alpha1-CB4 from chick skin collagen.";
RL J. Biol. Chem. 250:7428-7434(1975).
RN [5]
RP PROTEIN SEQUENCE OF 291-569, AND HYDROXYLATION AT PRO-296; PRO-302;
RP PRO-317; PRO-323; PRO-332; PRO-335; PRO-362; PRO-365; PRO-377; PRO-383;
RP PRO-392; PRO-398; PRO-401; PRO-416; LYS-419; PRO-425; PRO-428; PRO-440;
RP PRO-449; PRO-464; PRO-470; PRO-479; PRO-485; LYS-494; PRO-497; PRO-503;
RP PRO-512; PRO-518; PRO-524; PRO-533; PRO-536; PRO-545; PRO-554 AND PRO-560.
RX PubMed=7093229; DOI=10.1021/bi00538a011;
RA Highberger J.H., Corbett C., Dixit S.N., Yu W., Seyer J.M., Kang A.H.,
RA Gross J.;
RT "Amino acid sequence of chick skin collagen alpha 1(I)-CB8 and the complete
RT primary structure of the helical portion of the chick skin collagen alpha
RT 1(I) chain.";
RL Biochemistry 21:2048-2055(1982).
RN [6]
RP PROTEIN SEQUENCE OF 570-718, AND HYDROXYLATION AT PRO-572; PRO-581;
RP PRO-584; PRO-590; PRO-593; PRO-611; PRO-629; PRO-635; PRO-641; PRO-647;
RP PRO-653; PRO-659; PRO-671; PRO-680; PRO-692; PRO-704; PRO-707 AND PRO-713.
RX PubMed=1125203; DOI=10.1021/bi00680a019;
RA Dixit S.N., Kang A.H., Gross J.;
RT "Covalent structure of collagen: amino acid sequence of alpha1-CB3 of chick
RT skin collagen.";
RL Biochemistry 14:1929-1933(1975).
RN [7]
RP PROTEIN SEQUENCE OF 719-989, AND HYDROXYLATION AT PRO-719; PRO-728;
RP PRO-737; LYS-740; PRO-746; PRO-761; PRO-767; PRO-776; PRO-788; PRO-794;
RP PRO-797; PRO-806; PRO-812; PRO-830; PRO-839; PRO-848; LYS-851; PRO-860;
RP PRO-866; PRO-875; PRO-884; PRO-887; PRO-908; PRO-911; PRO-917; PRO-920;
RP PRO-926; PRO-935; PRO-953; PRO-962; PRO-965; PRO-971 AND PRO-986.
RX PubMed=167810; DOI=10.1021/bi00684a013;
RA Highberger J.H., Corbett C., Kang A.H., Gross J.;
RT "The amino acid sequence of chick skin collagen alpha1-CB7.";
RL Biochemistry 14:2872-2881(1975).
RN [8]
RP PROTEIN SEQUENCE OF 990-1096, HYDROXYLATION AT PRO-992; PRO-998; PRO-1007;
RP PRO-1013; LYS-1022; PRO-1034; PRO-1037; PRO-1040; PRO-1067 AND LYS-1085,
RP AND LACK OF GLYCOSYLATION AT LYS-1022 AND LYS-1085.
RX PubMed=1125204; DOI=10.1021/bi00680a020;
RA Dixit S.N., Seyer J.M., Oronsky A.O., Corbett C., Kang A.H., Gross J.;
RT "Covalent structure of collagen: amino acid sequence of alpha1-CB6A of
RT chick skin collagen.";
RL Biochemistry 14:1933-1938(1975).
RN [9]
RP PROTEIN SEQUENCE OF 1097-1187, HYDROXYLATION AT LYS-1097; PRO-1109;
RP PRO-1112; PRO-1115; PRO-1133; PRO-1148; PRO-1153; PRO-1154; PRO-1169;
RP PRO-1172; PRO-1175 AND PRO-1178, AND GLYCOSYLATION AT LYS-1097.
RX PubMed=728430; DOI=10.1021/bi00619a018;
RA Dixit S.N., Seyer J.M., Kang A.H., Gross J.;
RT "Covalent structure of collagen: amino acid sequence of chick skin collagen
RT alpha1(1)-CB6B.";
RL Biochemistry 17:5719-5722(1978).
RN [10]
RP PROTEIN SEQUENCE OF 1200-1205.
RX PubMed=5047697; DOI=10.1016/0006-291x(72)90408-1;
RA Eyre D.R., Glimcher M.J.;
RT "Evidence for a previously undetected sequence at the carboxyterminus of
RT the alpha 1 chain of chicken bone collagen.";
RL Biochem. Biophys. Res. Commun. 48:720-726(1972).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 981-1453, AND C-TERMINAL PROPEPTIDE CLEAVAGE
RP SITE.
RX PubMed=6927845; DOI=10.1021/bi00507a054;
RA Fuller F., Boedtker H.;
RT "Sequence determination and analysis of the 3' region of chicken pro-alpha
RT 1(I) and pro-alpha 2(I) collagen messenger ribonucleic acids including the
RT carboxy-terminal propeptide sequences.";
RL Biochemistry 20:996-1006(1981).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1453.
RX PubMed=6987088; DOI=10.1016/0014-5793(80)80761-7;
RA Showalter A.M., Pesciotta D.M., Eikenberry E.F., Yamamoto T., Pastan I.,
RA Decrombrugghe B., Fietzek P.P., Olsen B.R.;
RT "Nucleotide sequence of a collagen cDNA-fragment coding for the carboxyl
RT end of pro alpha 1(I)-chains.";
RL FEBS Lett. 111:61-65(1980).
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen).
CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones.
CC In bones the fibrils are mineralized with calcium hydroxyapatite.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function (By similarity). {ECO:0000250}.
CC -!- PTM: Contains mostly 4-hydroxyproline. Proline residues at the third
CC position of the tripeptide repeating unit (G-X-Y) are 4-hydroxylated in
CC some or all of the chains. {ECO:0000269|PubMed:1125203,
CC ECO:0000269|PubMed:167810, ECO:0000269|PubMed:4313735,
CC ECO:0000269|PubMed:7093229, ECO:0000269|PubMed:728430}.
CC -!- PTM: Contains 3-hydroxyproline. This modification occurs on the first
CC proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-
CC hydroxyproline. {ECO:0000269|PubMed:728430}.
CC -!- PTM: Lysine residues at the third position of the tripeptide repeating
CC unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
CC {ECO:0000269|PubMed:1125204, ECO:0000269|PubMed:1165248,
CC ECO:0000269|PubMed:728430}.
CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
CC glycan consists of a Glc-Gal disaccharide. {ECO:0000269|PubMed:1165248,
CC ECO:0000269|PubMed:728430}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; M17839; AAA48704.1; -; Genomic_DNA.
DR EMBL; M17838; AAA48704.1; JOINED; Genomic_DNA.
DR EMBL; V00401; CAA23695.1; -; mRNA.
DR EMBL; M10571; AAA48671.1; ALT_SEQ; mRNA.
DR EMBL; M17607; AAA48672.1; -; mRNA.
DR PIR; A27179; A27179.
DR PIR; A90458; CGCH1S.
DR PIR; I50629; I50629.
DR PIR; S07234; S07234.
DR ComplexPortal; CPX-3102; Collagen type I trimer.
DR IntAct; P02457; 1.
DR STRING; 9031.ENSGALP00000039595; -.
DR PRIDE; P02457; -.
DR VEuPathDB; HostDB:geneid_395069; -.
DR VEuPathDB; HostDB:geneid_395532; -.
DR VEuPathDB; HostDB:geneid_424526; -.
DR InParanoid; P02457; -.
DR OrthoDB; 337699at2759; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT PROPEP 23..151
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000269|PubMed:4313735"
FT /id="PRO_0000005716"
FT CHAIN 152..1207
FT /note="Collagen alpha-1(I) chain"
FT /evidence="ECO:0000303|PubMed:6927845"
FT /id="PRO_0000005717"
FT PROPEP 1208..1453
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000303|PubMed:6927845"
FT /id="PRO_0000005718"
FT DOMAIN 31..89
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1218..1453
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 96..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..201
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 909..924
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 SITE 1022
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:1125204"
FT SITE 1085
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 152
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4313735"
FT MOD_RES 160
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P02452"
FT MOD_RES 179
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4313735"
FT MOD_RES 182
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4313735"
FT MOD_RES 185
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4313735"
FT MOD_RES 194
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4313735"
FT MOD_RES 197
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4313735"
FT MOD_RES 200
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4313735"
FT MOD_RES 215
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 230
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 236
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 245
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 251
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 254
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 269
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 278
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 281
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 287
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1165248"
FT MOD_RES 296
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 302
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 317
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 323
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 332
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 335
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 362
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 365
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 377
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 383
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 392
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 398
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 401
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 416
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 419
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 425
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 428
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 440
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 449
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 464
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 470
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 479
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 485
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 494
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 497
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 503
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 512
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 518
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 524
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 533
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 536
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 545
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 554
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 560
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7093229"
FT MOD_RES 572
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 581
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 584
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 590
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 593
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 611
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 629
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 635
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 641
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 647
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 653
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 659
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 671
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 680
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 692
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 704
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 707
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 713
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125203"
FT MOD_RES 719
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 728
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 737
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 740
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 746
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 761
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 767
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 776
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 788
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 794
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 797
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 806
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 812
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 830
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 839
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 848
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 851
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 860
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 866
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 874
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 875
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 884
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 887
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 908
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 911
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 917
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 920
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 926
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 935
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 953
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 962
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 965
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 971
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 986
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:167810"
FT MOD_RES 992
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 998
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1007
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1013
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1022
FT /note="5-hydroxylysine; partial"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1034
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1037
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1040
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1067
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1085
FT /note="5-hydroxylysine; partial"
FT /evidence="ECO:0000269|PubMed:1125204"
FT MOD_RES 1097
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1109
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1112
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1115
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1133
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1148
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1153
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1154
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1168
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1169
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1171
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1172
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1174
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1175
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1178
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:728430"
FT MOD_RES 1181
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1197
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P02452"
FT CARBOHYD 254
FT /note="O-linked (Gal...) hydroxylysine; partial"
FT /evidence="ECO:0000269|PubMed:1165248"
FT CARBOHYD 1097
FT /note="O-linked (Gal...) hydroxylysine; partial"
FT /evidence="ECO:0000269|PubMed:728430"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 1248..1280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1254
FT /note="Interchain (with C-1271)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1271
FT /note="Interchain (with C-1254)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1288..1451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1359..1404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 1441
FT /note="Q -> H (in Ref. 12; AAA48671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1453 AA; 137755 MW; 61C617239E271A82 CRC64;
MFSFVDSRLL LLIAATVLLT RGEGEEDIQT GSCVQDGLTY NDKDVWKPEP CQICVCDSGN
ILCDEVICED TSDCPNAEIP FGECCPICPD VDASPVYPES AGVEGPKGDT GPRGDRGLPG
PPGRDGIPGQ PGLPGPPGPP GPPGLGGNFA PQMSYGYDEK SAGVAVPGPM GPAGPRGLPG
PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PAGPPGKNGD DGEAGKPGRP GQRGPPGPQG
ARGLPGTAGL PGMKGHRGFS GLDGAKGQPG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
RPGPSGPAGA RGNDGAPGAA GPPGPTGPAG PPGFPGAAGA KGETGPQGAR GSEGPQGSRG
EPGPPGPAGA AGPAGNPGAD GQPGAKGATG APGIAGAPGF PGARGPSGPQ GPSGAPGPKG
NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG PAGEEGKRGA RGEPGPAGLP GPAGERGAPG
SRGFPGADGI AGPKGPPGER GSPGAVGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG
KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGAAGE PGKPGERGAP GPPGAVGAAG
KDGEAGAQGP PGPTGPAGER GEQGPAGAPG FQGLPGPAGP PGEAGKPGEQ GVPGNAGAPG
PAGARGERGF PGERGVQGPP GPQGPRGANG APGNDGAKGD AGAPGAPGNE GPPGLEGMPG
ERGAAGLPGA KGDRGDPGPK GADGAPGKDG LRGLTGPIGP PGPAGAPGDK GEAGPPGPAG
PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGETGD AGAKGDAGPP GPAGPTGAPG
PAGZVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN IGLPGPPGPA GKZGSKGPRG
ETGPAGRPGE PGPAGPPGPP GEKGSPGADG PIGAPGTPGP QGIAGQRGVV GLPGQRGERG
FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE AGREGAPGAE GAPGRDGAAG
PKGDRGETGP AGPPGAPGAP GAPGPVGPAG KNGDRGETGP AGPAGPPGPA GARGPAGPQG
PRGDKGETGE QGDRGMKGHR GFSGLQGPPG PPGAPGEQGP SGASGPAGPR GPPGSAGAAG
KDGLNGLPGP IGPPGPRGRT GEVGPVGPPG PPGPPGPPGP PSGGFDLSFL PQPPQEKAHD
GGRYYRADDA NVMRDRDLEV DTTLKSLSQQ IENIRSPEGT RKNPARTCRD LKMCHGDWKS
GEYWIDPNQG CNLDAIKVYC NMETGETCVY PTQATIAQKN WYLSKNPKEK KHVWFGETMS
DGFQFEYGGE GSNPADVAIQ LTFLRLMSTE ATQNVTYHCK NSVAYMDHDT GNLKKALLLQ
GANEIEIRAE GNSRFTYGVT EDGCTSHTGA WGKTVIEYKT TKTSRLPIID LAPMDVGAPD
QEFGIDIGPV CFL
