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Collagen alpha-1(I) chain (Alpha-1 type I collagen)

 CO1A1_CHICK             Reviewed;        1453 AA.
P02457;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
10-JUL-2007, sequence version 3.
20-JUN-2018, entry version 113.
RecName: Full=Collagen alpha-1(I) chain;
AltName: Full=Alpha-1 type I collagen;
Flags: Precursor;
Name=COL1A1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
PubMed=3678834; DOI=10.1016/0378-1119(87)90159-4;
Finer M.H., Boedtker H., Doty P.;
"Construction and characterization of cDNA clones encoding the 5' end
of the chicken pro alpha 1(I) collagen mRNA.";
Gene 56:71-78(1987).
[2]
NUCLEOTIDE SEQUENCE OF 1-144.
PubMed=2820966;
Finer M.H., Aho S., Gerstenfeld L.C., Boedtker H., Doty P.;
"Unusual DNA sequences located within the promoter region and the
first intron of the chicken pro-alpha 1(I) collagen gene.";
J. Biol. Chem. 262:13323-13332(1987).
[3]
PROTEIN SEQUENCE OF 152-206, PYROGLUTAMATE FORMATION AT GLN-152, AND
HYDROXYLATION AT PRO-179; PRO-182; PRO-185; PRO-194; PRO-197 AND
PRO-200.
PubMed=4313735; DOI=10.1021/bi00806a012;
Kang A.H., Gross J.;
"Amino acid sequence of cyanogen bromide peptides from the amino-
terminal region of chick skicollagen.";
Biochemistry 9:796-804(1970).
[4]
PROTEIN SEQUENCE OF 207-290, HYDROXYLATION AT PRO-215; PRO-230;
PRO-236; PRO-245; PRO-251; LYS-254; PRO-269; PRO-278; PRO-281 AND
PRO-287, AND GLYCOSYLATION AT LYS-254.
PubMed=1165248;
Kang A.H., Dixit S.N., Corbett C., Gross J.;
"The covalent structure of collagen. Amino acid sequence of alpha1-CB5
glycopeptide and alpha1-CB4 from chick skin collagen.";
J. Biol. Chem. 250:7428-7434(1975).
[5]
PROTEIN SEQUENCE OF 291-569, AND HYDROXYLATION AT PRO-296; PRO-302;
PRO-317; PRO-323; PRO-332; PRO-335; PRO-362; PRO-365; PRO-377;
PRO-383; PRO-392; PRO-398; PRO-401; PRO-416; LYS-419; PRO-425;
PRO-428; PRO-440; PRO-449; PRO-464; PRO-470; PRO-479; PRO-485;
LYS-494; PRO-497; PRO-503; PRO-512; PRO-518; PRO-524; PRO-533;
PRO-536; PRO-545; PRO-554 AND PRO-560.
PubMed=7093229; DOI=10.1021/bi00538a011;
Highberger J.H., Corbett C., Dixit S.N., Yu W., Seyer J.M., Kang A.H.,
Gross J.;
"Amino acid sequence of chick skin collagen alpha 1(I)-CB8 and the
complete primary structure of the helical portion of the chick skin
collagen alpha 1(I) chain.";
Biochemistry 21:2048-2055(1982).
[6]
PROTEIN SEQUENCE OF 570-718, AND HYDROXYLATION AT PRO-572; PRO-581;
PRO-584; PRO-590; PRO-593; PRO-611; PRO-629; PRO-635; PRO-641;
PRO-647; PRO-653; PRO-659; PRO-671; PRO-680; PRO-692; PRO-704; PRO-707
AND PRO-713.
PubMed=1125203; DOI=10.1021/bi00680a019;
Dixit S.N., Kang A.H., Gross J.;
"Covalent structure of collagen: amino acid sequence of alpha1-CB3 of
chick skin collagen.";
Biochemistry 14:1929-1933(1975).
[7]
PROTEIN SEQUENCE OF 719-989, AND HYDROXYLATION AT PRO-719; PRO-728;
PRO-737; LYS-740; PRO-746; PRO-761; PRO-767; PRO-776; PRO-788;
PRO-794; PRO-797; PRO-806; PRO-812; PRO-830; PRO-839; PRO-848;
LYS-851; PRO-860; PRO-866; PRO-875; PRO-884; PRO-887; PRO-908;
PRO-911; PRO-917; PRO-920; PRO-926; PRO-935; PRO-953; PRO-962;
PRO-965; PRO-971 AND PRO-986.
PubMed=167810; DOI=10.1021/bi00684a013;
Highberger J.H., Corbett C., Kang A.H., Gross J.;
"The amino acid sequence of chick skin collagen alpha1-CB7.";
Biochemistry 14:2872-2881(1975).
[8]
PROTEIN SEQUENCE OF 990-1096, HYDROXYLATION AT PRO-992; PRO-998;
PRO-1007; PRO-1013; LYS-1022; PRO-1034; PRO-1037; PRO-1040; PRO-1067
AND LYS-1085, AND LACK OF GLYCOSYLATION AT LYS-1022 AND LYS-1085.
PubMed=1125204; DOI=10.1021/bi00680a020;
Dixit S.N., Seyer J.M., Oronsky A.O., Corbett C., Kang A.H., Gross J.;
"Covalent structure of collagen: amino acid sequence of alpha1-CB6A of
chick skin collagen.";
Biochemistry 14:1933-1938(1975).
[9]
PROTEIN SEQUENCE OF 1097-1187, HYDROXYLATION AT LYS-1097; PRO-1109;
PRO-1112; PRO-1115; PRO-1133; PRO-1148; PRO-1153; PRO-1154; PRO-1169;
PRO-1172; PRO-1175 AND PRO-1178, AND GLYCOSYLATION AT LYS-1097.
PubMed=728430; DOI=10.1021/bi00619a018;
Dixit S.N., Seyer J.M., Kang A.H., Gross J.;
"Covalent structure of collagen: amino acid sequence of chick skin
collagen alpha1(1)-CB6B.";
Biochemistry 17:5719-5722(1978).
[10]
PROTEIN SEQUENCE OF 1200-1205.
PubMed=5047697; DOI=10.1016/0006-291X(72)90408-1;
Eyre D.R., Glimcher M.J.;
"Evidence for a previously undetected sequence at the carboxyterminus
of the alpha 1 chain of chicken bone collagen.";
Biochem. Biophys. Res. Commun. 48:720-726(1972).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 981-1453, AND C-TERMINAL PROPEPTIDE
CLEAVAGE SITE.
PubMed=6927845; DOI=10.1021/bi00507a054;
Fuller F., Boedtker H.;
"Sequence determination and analysis of the 3' region of chicken pro-
alpha 1(I) and pro-alpha 2(I) collagen messenger ribonucleic acids
including the carboxy-terminal propeptide sequences.";
Biochemistry 20:996-1006(1981).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1453.
PubMed=6987088; DOI=10.1016/0014-5793(80)80761-7;
Showalter A.M., Pesciotta D.M., Eikenberry E.F., Yamamoto T.,
Pastan I., Decrombrugghe B., Fietzek P.P., Olsen B.R.;
"Nucleotide sequence of a collagen cDNA-fragment coding for the
carboxyl end of pro alpha 1(I)-chains.";
FEBS Lett. 111:61-65(1980).
-!- FUNCTION: Type I collagen is a member of group I collagen
(fibrillar forming collagen).
-!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and
bones. In bones the fibrils are mineralized with calcium
hydroxyapatite.
-!- DOMAIN: The C-terminal propeptide, also known as COLFI domain,
have crucial roles in tissue growth and repair by controlling both
the intracellular assembly of procollagen molecules and the
extracellular assembly of collagen fibrils. It binds a calcium ion
which is essential for its function (By similarity).
{ECO:0000250}.
-!- PTM: Contains mostly 4-hydroxyproline. Proline residues at the
third position of the tripeptide repeating unit (G-X-Y) are 4-
hydroxylated in some or all of the chains.
{ECO:0000269|PubMed:1125203, ECO:0000269|PubMed:167810,
ECO:0000269|PubMed:4313735, ECO:0000269|PubMed:7093229,
ECO:0000269|PubMed:728430}.
-!- PTM: Contains 3-hydroxyproline. This modification occurs on the
first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp
is 4-hydroxyproline. {ECO:0000269|PubMed:728430}.
-!- PTM: Lysine residues at the third position of the tripeptide
repeating unit (G-X-Y) are 5-hydroxylated in some or all of the
chains. {ECO:0000269|PubMed:1125204, ECO:0000269|PubMed:1165248,
ECO:0000269|PubMed:728430}.
-!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
glycan consists of a Glc-Gal disaccharide.
{ECO:0000269|PubMed:1165248, ECO:0000269|PubMed:728430}.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
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EMBL; M17839; AAA48704.1; -; Genomic_DNA.
EMBL; M17838; AAA48704.1; JOINED; Genomic_DNA.
EMBL; V00401; CAA23695.1; -; mRNA.
EMBL; M10571; AAA48671.1; ALT_SEQ; mRNA.
EMBL; M17607; AAA48672.1; -; mRNA.
PIR; A27179; A27179.
PIR; A90458; CGCH1S.
PIR; I50629; I50629.
PIR; S07234; S07234.
UniGene; Gga.2073; -.
UniGene; Gga.43371; -.
ComplexPortal; CPX-3102; Collagen type I trimer.
IntAct; P02457; 1.
PRIDE; P02457; -.
HOVERGEN; HBG004933; -.
InParanoid; P02457; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR001007; VWF_dom.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 10.
Pfam; PF00093; VWC; 1.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
SMART; SM00214; VWC; 1.
PROSITE; PS51461; NC1_FIB; 1.
PROSITE; PS01208; VWFC_1; 1.
PROSITE; PS50184; VWFC_2; 1.
1: Evidence at protein level;
Calcium; Collagen; Complete proteome; Direct protein sequencing;
Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 22
PROPEP 23 151 N-terminal propeptide.
{ECO:0000269|PubMed:4313735}.
/FTId=PRO_0000005716.
CHAIN 152 1207 Collagen alpha-1(I) chain.
{ECO:0000303|PubMed:6927845}.
/FTId=PRO_0000005717.
PROPEP 1208 1453 C-terminal propeptide.
{ECO:0000303|PubMed:6927845}.
/FTId=PRO_0000005718.
DOMAIN 31 89 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 1218 1453 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
METAL 1266 1266 Calcium. {ECO:0000250}.
METAL 1268 1268 Calcium. {ECO:0000250}.
METAL 1269 1269 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1271 1271 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1274 1274 Calcium. {ECO:0000250}.
SITE 1022 1022 Not glycosylated.
{ECO:0000269|PubMed:1125204}.
SITE 1085 1085 Not glycosylated.
{ECO:0000269|PubMed:1125204}.
MOD_RES 152 152 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:4313735}.
MOD_RES 160 160 Allysine. {ECO:0000250|UniProtKB:P02452}.
MOD_RES 179 179 4-hydroxyproline.
{ECO:0000269|PubMed:4313735}.
MOD_RES 182 182 4-hydroxyproline.
{ECO:0000269|PubMed:4313735}.
MOD_RES 185 185 4-hydroxyproline.
{ECO:0000269|PubMed:4313735}.
MOD_RES 194 194 4-hydroxyproline.
{ECO:0000269|PubMed:4313735}.
MOD_RES 197 197 4-hydroxyproline.
{ECO:0000269|PubMed:4313735}.
MOD_RES 200 200 4-hydroxyproline.
{ECO:0000269|PubMed:4313735}.
MOD_RES 215 215 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 230 230 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 236 236 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 245 245 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 251 251 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 254 254 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:1165248}.
MOD_RES 269 269 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 278 278 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 281 281 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 287 287 4-hydroxyproline.
{ECO:0000269|PubMed:1165248}.
MOD_RES 296 296 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 302 302 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 317 317 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 323 323 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 332 332 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 335 335 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 362 362 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 365 365 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 377 377 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 383 383 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 392 392 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 398 398 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 401 401 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 416 416 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 419 419 5-hydroxylysine.
{ECO:0000269|PubMed:7093229}.
MOD_RES 425 425 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 428 428 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 440 440 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 449 449 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 464 464 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 470 470 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 479 479 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 485 485 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 494 494 5-hydroxylysine.
{ECO:0000269|PubMed:7093229}.
MOD_RES 497 497 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 503 503 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 512 512 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 518 518 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 524 524 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 533 533 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 536 536 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 545 545 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 554 554 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 560 560 4-hydroxyproline.
{ECO:0000269|PubMed:7093229}.
MOD_RES 572 572 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 581 581 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 584 584 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 590 590 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 593 593 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 611 611 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 629 629 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 635 635 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 641 641 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 647 647 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 653 653 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 659 659 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 671 671 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 680 680 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 692 692 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 704 704 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 707 707 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 713 713 4-hydroxyproline.
{ECO:0000269|PubMed:1125203}.
MOD_RES 719 719 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 728 728 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 737 737 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 740 740 5-hydroxylysine.
{ECO:0000269|PubMed:167810}.
MOD_RES 746 746 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 761 761 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 767 767 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 776 776 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 788 788 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 794 794 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 797 797 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 806 806 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 812 812 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 830 830 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 839 839 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 848 848 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 851 851 5-hydroxylysine.
{ECO:0000269|PubMed:167810}.
MOD_RES 860 860 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 866 866 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 874 874 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 875 875 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 884 884 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 887 887 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 908 908 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 911 911 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 917 917 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 920 920 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 926 926 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 935 935 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 953 953 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 962 962 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 965 965 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 971 971 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 986 986 4-hydroxyproline.
{ECO:0000269|PubMed:167810}.
MOD_RES 992 992 4-hydroxyproline.
{ECO:0000269|PubMed:1125204}.
MOD_RES 998 998 4-hydroxyproline.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1007 1007 4-hydroxyproline.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1013 1013 4-hydroxyproline.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1022 1022 5-hydroxylysine; partial.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1034 1034 4-hydroxyproline.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1037 1037 4-hydroxyproline.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1040 1040 4-hydroxyproline.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1067 1067 4-hydroxyproline.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1085 1085 5-hydroxylysine; partial.
{ECO:0000269|PubMed:1125204}.
MOD_RES 1097 1097 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:728430}.
MOD_RES 1109 1109 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1112 1112 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1115 1115 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1133 1133 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1148 1148 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1153 1153 3-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1154 1154 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1168 1168 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1169 1169 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1171 1171 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1172 1172 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1174 1174 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1175 1175 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1178 1178 4-hydroxyproline.
{ECO:0000269|PubMed:728430}.
MOD_RES 1181 1181 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1197 1197 Allysine. {ECO:0000250|UniProtKB:P02452}.
CARBOHYD 254 254 O-linked (Gal...) hydroxylysine; partial.
{ECO:0000269|PubMed:1165248}.
CARBOHYD 1097 1097 O-linked (Gal...) hydroxylysine; partial.
{ECO:0000269|PubMed:728430}.
CARBOHYD 1354 1354 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 1248 1280 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1254 1254 Interchain (with C-1271).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1271 1271 Interchain (with C-1254).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1288 1451 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1359 1404 {ECO:0000255|PROSITE-ProRule:PRU00793}.
CONFLICT 1441 1441 Q -> H (in Ref. 12; AAA48671).
{ECO:0000305}.
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


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