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

 CO1A1_BOVIN             Reviewed;        1463 AA.
P02453; Q3MHM2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 3.
16-OCT-2019, entry version 154.
RecName: Full=Collagen alpha-1(I) chain;
AltName: Full=Alpha-1 type I collagen;
Flags: Precursor;
Name=COL1A1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 162-180, ALLYSINE AT LYS-170, AND PYROGLUTAMATE
FORMATION AT GLN-162.
PubMed=4115172; DOI=10.1111/j.1432-1033.1972.tb01831.x;
Rauterberg J., Timpl R., Furthmayr H.;
"Structural characterization of N-terminal antigenic determinants in
calf and human collagen.";
Eur. J. Biochem. 27:231-237(1972).
[3]
PROTEIN SEQUENCE OF 181-306, AND HYDROXYLATION AT LYS-264.
PubMed=1164916; DOI=10.1111/j.1432-1033.1975.tb03974.x;
Fietzek P.P., Kuehn K.;
"The covalent structure of collagen: amino-acid sequence of the
cyanogen-bromide peptides alpha-1-CB2, alpha-1-CB4 and alpha-1-CB5
from calf-skin collagen.";
Eur. J. Biochem. 52:77-82(1975).
[4]
PROTEIN SEQUENCE OF 580-728.
PubMed=4673951; DOI=10.1016/0014-5793(72)80545-3;
Fietzek P.P., Wendt P., Kell I., Kuehn K.;
"The covalent structure of collagen: amino acid sequence of alpha-1-
CB3 from calf skin collagen.";
FEBS Lett. 26:74-76(1972).
[5]
PROTEIN SEQUENCE OF 729-999.
PubMed=4359390; DOI=10.1111/j.1432-1033.1973.tb03072.x;
Fietzek P.P., Rexrodt F.W., Hopper K.E., Kuehn K.;
"The covalent structure of collagen. 2. The amino-acid sequence of
alpha-1-CB7 from calf-skin collagen.";
Eur. J. Biochem. 38:396-400(1973).
[6]
PROTEIN SEQUENCE OF 1000-1112.
PubMed=4343808; DOI=10.1111/j.1432-1033.1972.tb02084.x;
Wendt P., Mark K.V.D., Rexrodt F., Kuehn K.;
"The covalent structure of collagen. The amino-acid sequence of the
112-residues. Amino-terminal part of peptide alpha-1-CB6 from calf-
skin collagen.";
Eur. J. Biochem. 30:169-183(1972).
[7]
PROTEIN SEQUENCE OF 1113-1188.
PubMed=4343807; DOI=10.1111/j.1432-1033.1972.tb02083.x;
Fietzek P.P., Rexrodt F.W., Wendt P., Stark M., Kuehn K.;
"The covalent structure of collagen. Amino-acid sequence of peptide
alpha-1-CB6-C2.";
Eur. J. Biochem. 30:163-168(1972).
[8]
PROTEIN SEQUENCE OF 1196-1215, ALLYSINE AT LYS-1207, AND HYDROXYLATION
AT PRO-1163.
PubMed=11946479; DOI=10.1016/0014-5793(72)80167-4;
Rauterberg J., Fietzek P., Rexrodt F., Becker U., Stark M., Kuehn K.;
"The amino acid sequence of the carboxyterminal nonhelical cross link
region of the alpha 1 chain of calf skin collagen.";
FEBS Lett. 21:75-79(1972).
[9]
HYDROXYLATION AT PRO-1178; PRO-1179; PRO-1181; PRO-1182; PRO-1185 AND
PRO-1188, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25645914; DOI=10.1074/jbc.m114.634915;
Hudson D.M., Joeng K.S., Werther R., Rajagopal A., Weis M., Lee B.H.,
Eyre D.R.;
"Post-translationally abnormal collagens of prolyl 3-hydroxylase-2
null mice offer a pathobiological mechanism for the high myopia linked
to human LEPREL1 mutations.";
J. Biol. Chem. 290:8613-8622(2015).
[10]
INTERACTION WITH MFAP4.
PubMed=26601954; DOI=10.1074/jbc.m115.681775;
Pilecki B., Holm A.T., Schlosser A., Moeller J.B., Wohl A.P.,
Zuk A.V., Heumueller S.E., Wallis R., Moestrup S.K., Sengle G.,
Holmskov U., Sorensen G.L.;
"Characterization of microfibrillar-associated protein 4 (MFAP4) as a
tropoelastin- and fibrillin-binding protein involved in elastic fiber
formation.";
J. Biol. Chem. 291:1103-1114(2016).
-!- 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.
Interacts with MRC2 (By similarity). Interacts with TRAM2 (By
similarity). Interacts with MFAP4 in a Ca (2+)-dependent manner
(PubMed:26601954). {ECO:0000250|UniProtKB:P02452,
ECO:0000250|UniProtKB:P02454, ECO:0000269|PubMed:26601954}.
-!- 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
hydroxylated in some or all of the chains.
{ECO:0000269|PubMed:1164916, ECO:0000269|PubMed:11946479}.
-!- PTM: Contains 3-hydroxyproline at a few sites. This modification
occurs on the first proline residue in the sequence motif Gly-Pro-
Hyp, where Hyp is 4-hydroxyproline. {ECO:0000269|PubMed:11946479}.
-!- 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:0000250|UniProtKB:P02457}.
-!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
glycan consists of a Glc-Gal disaccharide.
{ECO:0000250|UniProtKB:P11087}.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
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EMBL; BC105184; AAI05185.1; -; mRNA.
PIR; A91193; CGBO1S.
RefSeq; NP_001029211.1; NM_001034039.2.
SMR; P02453; -.
ComplexPortal; CPX-3101; Collagen type I trimer.
IntAct; P02453; 1.
STRING; 9913.ENSBTAP00000017420; -.
PaxDb; P02453; -.
PeptideAtlas; P02453; -.
PRIDE; P02453; -.
Ensembl; ENSBTAT00000017420; ENSBTAP00000017420; ENSBTAG00000013103.
GeneID; 282187; -.
KEGG; bta:282187; -.
CTD; 1277; -.
VGNC; VGNC:27560; COL1A1.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00940000156584; -.
HOGENOM; HOG000085654; -.
InParanoid; P02453; -.
KO; K06236; -.
OMA; NDSGTWV; -.
OrthoDB; 337699at2759; -.
TreeFam; TF344135; -.
Reactome; R-BTA-114604; GPVI-mediated activation cascade.
Reactome; R-BTA-1442490; Collagen degradation.
Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-BTA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-BTA-202733; Cell surface interactions at the vascular wall.
Reactome; R-BTA-216083; Integrin cell surface interactions.
Reactome; R-BTA-2243919; Crosslinking of collagen fibrils.
Reactome; R-BTA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-BTA-3000178; ECM proteoglycans.
Reactome; R-BTA-430116; GP1b-IX-V activation signalling.
Reactome; R-BTA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-BTA-8948216; Collagen chain trimerization.
PMAP-CutDB; P02453; -.
Proteomes; UP000009136; Chromosome 19.
Bgee; ENSBTAG00000013103; Expressed in 9 organ(s), highest expression level in colon.
GO; GO:0005584; C:collagen type I trimer; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl.
GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IBA:GO_Central.
GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0001503; P:ossification; IBA:GO_Central.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
GO; GO:0043588; P:skin development; IBA:GO_Central.
GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
GO; GO:0034505; P:tooth mineralization; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IEA:Ensembl.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR001007; VWF_dom.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 10.
Pfam; PF00093; VWC; 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; Phosphoprotein; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 161 N-terminal propeptide.
{ECO:0000269|PubMed:4115172}.
/FTId=PRO_0000236804.
CHAIN 162 1217 Collagen alpha-1(I) chain.
{ECO:0000305|PubMed:11946479}.
/FTId=PRO_0000059396.
PROPEP 1218 1463 C-terminal propeptide.
{ECO:0000305|PubMed:11946479}.
/FTId=PRO_0000236805.
DOMAIN 38 96 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 1228 1463 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 162 177 Nonhelical region (N-terminal).
REGION 178 1191 Triple-helical region.
REGION 1192 1215 Nonhelical region (C-terminal).
MOTIF 744 746 Cell attachment site. {ECO:0000255}.
MOTIF 1092 1094 Cell attachment site. {ECO:0000255}.
METAL 1276 1276 Calcium. {ECO:0000250}.
METAL 1278 1278 Calcium. {ECO:0000250}.
METAL 1279 1279 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1281 1281 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1284 1284 Calcium. {ECO:0000250}.
MOD_RES 162 162 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:4115172}.
MOD_RES 170 170 Allysine. {ECO:0000269|PubMed:4115172}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 189 189 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 192 192 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 195 195 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 204 204 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 207 207 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 210 210 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 225 225 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 240 240 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 246 246 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 255 255 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 261 261 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 264 264 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:1164916}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 276 276 5-hydroxylysine. {ECO:0000255}.
MOD_RES 285 285 5-hydroxylysine. {ECO:0000255}.
MOD_RES 288 288 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 291 291 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 297 297 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 306 306 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 312 312 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 333 333 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 342 342 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 345 345 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 372 372 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 375 375 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 387 387 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 393 393 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 402 402 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 408 408 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 411 411 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 426 426 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 429 429 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 435 435 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 438 438 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 450 450 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 459 459 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 474 474 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 480 480 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 489 489 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 495 495 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 504 504 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 513 513 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 522 522 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 528 528 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 534 534 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 543 543 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 546 546 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 555 555 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 564 564 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 570 570 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 582 582 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 591 591 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 600 600 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 603 603 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 621 621 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 639 639 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 645 645 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 651 651 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 657 657 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 663 663 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 669 669 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 681 681 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 690 690 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 702 702 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 714 714 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 717 717 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 723 723 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 729 729 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 738 738 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 750 750 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 756 756 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 771 771 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 777 777 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 798 798 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 804 804 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 807 807 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 816 816 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 822 822 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 840 840 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 849 849 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 858 858 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 861 861 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 870 870 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 876 876 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 884 884 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 885 885 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 894 894 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 897 897 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 918 918 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 927 927 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 936 936 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 945 945 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 963 963 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 972 972 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 975 975 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 981 981 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 996 996 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1002 1002 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1008 1008 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1017 1017 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1023 1023 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1032 1032 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1044 1044 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1047 1047 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1050 1050 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1095 1095 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1107 1107 5-hydroxylysine; alternate.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1119 1119 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1122 1122 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1125 1125 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1143 1143 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1158 1158 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1163 1163 3-hydroxyproline.
{ECO:0000269|PubMed:11946479}.
MOD_RES 1164 1164 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1178 1178 3-hydroxyproline.
{ECO:0000269|PubMed:25645914}.
MOD_RES 1179 1179 4-hydroxyproline.
{ECO:0000269|PubMed:25645914}.
MOD_RES 1181 1181 3-hydroxyproline.
{ECO:0000269|PubMed:25645914}.
MOD_RES 1182 1182 4-hydroxyproline.
{ECO:0000269|PubMed:25645914}.
MOD_RES 1184 1184 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1185 1185 4-hydroxyproline.
{ECO:0000269|PubMed:25645914}.
MOD_RES 1188 1188 4-hydroxyproline.
{ECO:0000269|PubMed:25645914}.
MOD_RES 1191 1191 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1207 1207 Allysine. {ECO:0000269|PubMed:11946479}.
CARBOHYD 264 264 O-linked (Gal...) hydroxylysine;
alternate.
{ECO:0000250|UniProtKB:P02457}.
CARBOHYD 1107 1107 O-linked (Gal...) hydroxylysine;
alternate.
{ECO:0000250|UniProtKB:P02457}.
DISULFID 1258 1290 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1264 1264 Interchain (with C-1281).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1281 1281 Interchain (with C-1264).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1298 1461 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1369 1414 {ECO:0000255|PROSITE-ProRule:PRU00793}.
CONFLICT 687 687 Q -> E (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 790 792 Missing (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 794 794 A -> T (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 1043 1043 P -> A (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1046 1046 A -> P (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1074 1074 A -> I (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1077 1077 I -> V (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1080 1080 V -> A (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1206 1206 E -> QZ (in Ref. 8; AA sequence).
{ECO:0000305}.
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


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Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1584: Type II diabetes mellitus
WP231: TNF alpha Signaling Pathway
WP537: Translation Factors
WP1487: TNF-alpha and mucus production in lung epythelium
WP1047: TNF-alpha NF-kB Signaling Pathway
WP1772: Apoptosis Modulation and Signaling
WP1120: Ovarian Infertility Genes
WP1904: RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
WP622: Long-Day Flowering Time Pathway
WP1566: Citrate cycle (TCA cycle)
WP262: EBV LMP1 signaling
WP1209: EBV LMP1 signaling
WP210: Cytoplasmic Ribosomal Proteins
WP215: noncanonical wnt pathway
WP885: Ovarian Infertility Genes
WP34: Ovarian Infertility Genes
WP1655: Geraniol degradation
WP457: TNF-alpha NF-kB Signaling Pathway
WP1340: Ovarian Infertility Genes
WP1434: Osteopontin Signaling
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP566: canonical wnt - zebrafish
WP1883: Platelet Adhesion to exposed collagen
WP1531: Vitamin D synthesis

Related Genes :
[COL1A1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[Col1a1 Cola1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[Col1a1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[COL1A1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[COL1A1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[COL2A1] Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin]
[COL1A2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[Col4a1 Cg25C DCg1 CG4145] Collagen alpha-1(IV) chain (Collagen type IV alpha 1)
[COL1A1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[COL2A1] Collagen alpha-1(II) chain (Alpha-1 type II collagen)
[Col2a1] Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin]
[Col2a1] Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin]
[Col1a2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[COL1A2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[Col1a2 Cola2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[COL2A1] Collagen alpha-1(II) chain (Alpha-1 type II collagen) (Fragment)
[COL19A1] Collagen alpha-1(XIX) chain (Collagen alpha-1(Y) chain)
[COL1A2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[COL7A1] Collagen alpha-1(VII) chain (Long-chain collagen) (LC collagen)
[COL6A5 COL29A1 VWA4] Collagen alpha-5(VI) chain (Collagen alpha-1(XXIX) chain) (von Willebrand factor A domain-containing protein 4)
[Col26a1 Col26a Emid2 Emu2] Collagen alpha-1(XXVI) chain (Alpha-1 type XXVI collagen) (EMI domain-containing protein 2) (Emilin and multimerin domain-containing protein 2) (Emu2)
[COL8A1 C3orf7] Collagen alpha-1(VIII) chain (Endothelial collagen) [Cleaved into: Vastatin]
[COL25A1] Collagen alpha-1(XXV) chain (Alzheimer disease amyloid-associated protein) (AMY) (CLAC-P) [Cleaved into: Collagen-like Alzheimer amyloid plaque component (CLAC)]
[Col14a1] Collagen alpha-1(XIV) chain
[Col7a1] Collagen alpha-1(VII) chain (Long-chain collagen) (LC collagen)
[COL17A1 BP180 BPAG2] Collagen alpha-1(XVII) chain (180 kDa bullous pemphigoid antigen 2) (Bullous pemphigoid antigen 2) [Cleaved into: 120 kDa linear IgA disease antigen (120 kDa linear IgA dermatosis antigen) (Linear IgA disease antigen 1) (LAD-1); 97 kDa linear IgA disease antigen (97 kDa linear IgA bullous dermatosis antigen) (97 kDa LAD antigen) (97-LAD) (Linear IgA bullous disease antigen of 97 kDa) (LABD97)]
[COL12A1 COL12A1L] Collagen alpha-1(XII) chain
[COL4A1] Collagen alpha-1(IV) chain [Cleaved into: Arresten]
[COL3A1] Collagen alpha-1(III) chain
[Col4a1] Collagen alpha-1(IV) chain [Cleaved into: Arresten]

Bibliography :
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[31679460] RNA-binding protein ZFP36/TTP protects against ferroptosis by regulating autophagy signaling pathway in hepatic stellate cells.
[31660146] Fermented black radish ( L. var. ) attenuates methionine and choline deficient diet-induced nonalcoholic fatty liver disease in mice.
[31637903] The role of miR-145 in promoting the fibrosis of pulmonary fibroblasts.
[31612672] [Roles of transforming growth factor - β1 and heat shock protein 47 in progression of -induced hepatic fibrosis].
[31611968] Exploration of estrogen receptor-associated hub genes and potential molecular mechanisms in non-smoking females with lung adenocarcinoma using integrated bioinformatics analysis.
[31443264] Extract Promotes In Vitro Differentiation and Functionality of Human Primary Osteoblasts.
[31428151] Circular RNA hsa_circRNA_0007334 is Predicted to Promote MMP7 and COL1A1 Expression by Functioning as a miRNA Sponge in Pancreatic Ductal Adenocarcinoma.
[31385019] Association between sphingosine-1-phosphate-induced signal transduction via mitogen-activated protein kinase pathways and keloid formation.
[31377650] COL1A1 affects apoptosis by regulating oxidative stress and autophagy in bovine cumulus cells.