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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.
07-JUN-2017, entry version 141.
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]
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: Proline residues at the third position of the tripeptide
repeating unit (G-X-Y) are hydroxylated in some or all of the
chains. Pro-1163 is the only 3-hydroxyproline and the only
hydroxylated proline in position X. {ECO:0000269|PubMed:1164916,
ECO:0000269|PubMed:11946479}.
-!- PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to
the oxygen atom of a post-translationally added hydroxyl group.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BC105184; AAI05185.1; -; mRNA.
PIR; A91193; CGBO1S.
RefSeq; NP_001029211.1; NM_001034039.2.
UniGene; Bt.23316; -.
ProteinModelPortal; P02453; -.
SMR; P02453; -.
IntAct; P02453; 1.
STRING; 9913.ENSBTAP00000017420; -.
PaxDb; P02453; -.
PeptideAtlas; P02453; -.
PRIDE; P02453; -.
Ensembl; ENSBTAT00000017420; ENSBTAP00000017420; ENSBTAG00000013103.
GeneID; 282187; -.
KEGG; bta:282187; -.
CTD; 1277; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00840000129673; -.
HOGENOM; HOG000085654; -.
HOVERGEN; HBG004933; -.
InParanoid; P02453; -.
KO; K06236; -.
OMA; FQFEYGS; -.
OrthoDB; EOG091G03LV; -.
TreeFam; TF344135; -.
Reactome; R-BTA-114604; GPVI-mediated activation cascade.
Reactome; R-BTA-1442490; Collagen degradation.
Reactome; R-BTA-1474244; Extracellular matrix organization.
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-2214320; Anchoring fibril formation.
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-76009; Platelet Aggregation (Plug Formation).
Reactome; R-BTA-8874081; MET activates PTK2 signaling.
Reactome; R-BTA-8948216; Collagen chain trimerization.
PMAP-CutDB; P02453; -.
Proteomes; UP000009136; Chromosome 19.
Bgee; ENSBTAG00000013103; -.
GO; GO:0005584; C:collagen type I trimer; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
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; IEA:Ensembl.
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:0048706; P:embryonic skeletal system development; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
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: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:0070208; P:protein heterotrimerization; IEA:Ensembl.
GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
GO; GO:0034505; P:tooth mineralization; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IEA:Ensembl.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
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; 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 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 708 708 5-hydroxylysine. {ECO:0000255}.
MOD_RES 780 780 5-hydroxylysine. {ECO:0000255}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 861 861 5-hydroxylysine. {ECO:0000255}.
MOD_RES 933 933 5-hydroxylysine. {ECO:0000255}.
MOD_RES 1095 1095 5-hydroxylysine. {ECO:0000255}.
MOD_RES 1107 1107 5-hydroxylysine. {ECO:0000255}.
MOD_RES 1163 1163 3-hydroxyproline.
{ECO:0000269|PubMed:11946479}.
MOD_RES 1207 1207 Allysine. {ECO:0000269|PubMed:11946479}.
CARBOHYD 264 264 O-linked (Gal...) hydroxylysine;
alternate.
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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