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Protein

Collagen alpha-2(I) chain

Gene

COL1A2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1179CalciumBy similarity1
Metal bindingi1181CalciumBy similarity1
Metal bindingi1182Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1184Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1187CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-114604. GPVI-mediated activation cascade.
R-BTA-1442490. Collagen degradation.
R-BTA-1474244. Extracellular matrix organization.
R-BTA-1650814. Collagen biosynthesis and modifying enzymes.
R-BTA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-BTA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-BTA-202733. Cell surface interactions at the vascular wall.
R-BTA-216083. Integrin cell surface interactions.
R-BTA-2214320. Anchoring fibril formation.
R-BTA-2243919. Crosslinking of collagen fibrils.
R-BTA-3000171. Non-integrin membrane-ECM interactions.
R-BTA-3000178. ECM proteoglycans.
R-BTA-430116. GP1b-IX-V activation signalling.
R-BTA-75892. Platelet Adhesion to exposed collagen.
R-BTA-76009. Platelet Aggregation (Plug Formation).
R-BTA-8874081. MET activates PTK2 signaling.
R-BTA-8948216. Collagen chain trimerization.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(I) chain
Alternative name(s):
Alpha-2 type I collagen
Gene namesi
Name:COL1A2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 4

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei3550. Bos d alpha2I.0101.
896. Bos d alpha2I.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
PropeptideiPRO_000000579823 – 79N-terminal propeptide1 PublicationAdd BLAST57
ChainiPRO_000000579980 – 1117Collagen alpha-2(I) chainAdd BLAST1038
PropeptideiPRO_00000058001118 – 1364C-terminal propeptideBy similarityAdd BLAST247

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei80Pyrrolidone carboxylic acid1 Publication1
Modified residuei84Allysine1 Publication1
Modified residuei1004-hydroxyproline1 Publication1
Modified residuei1064-hydroxyproline1 Publication1
Modified residuei1154-hydroxyproline1 Publication1
Modified residuei1184-hydroxyproline1 Publication1
Modified residuei1214-hydroxyproline1 Publication1
Modified residuei1334-hydroxyproline1 Publication1
Modified residuei1364-hydroxyproline1 Publication1
Modified residuei1454-hydroxyproline1 Publication1
Modified residuei1514-hydroxyproline1 Publication1
Modified residuei1664-hydroxyproline1 Publication1
Modified residuei1694-hydroxyproline1 Publication1
Modified residuei1724-hydroxyproline1 Publication1
Modified residuei1755-hydroxylysine; alternate1 Publication1
Glycosylationi175O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei1904-hydroxyproline1 Publication1
Modified residuei1934-hydroxyproline1 Publication1
Modified residuei1965-hydroxylysine1 Publication1
Modified residuei1994-hydroxyproline1 Publication1
Modified residuei2024-hydroxyproline1 Publication1
Modified residuei2084-hydroxyproline1 Publication1
Modified residuei2174-hydroxyproline1 Publication1
Modified residuei2264-hydroxyproline1 Publication1
Modified residuei2534-hydroxyproline1 Publication1
Modified residuei2564-hydroxyproline1 Publication1
Modified residuei2594-hydroxyproline1 Publication1
Modified residuei2625-hydroxylysine1 Publication1
Modified residuei2714-hydroxyproline1 Publication1
Modified residuei2864-hydroxyproline1 Publication1
Modified residuei2954-hydroxyproline1 Publication1
Modified residuei3044-hydroxyproline1 Publication1
Modified residuei3075-hydroxylysine1 Publication1
Modified residuei3134-hydroxyproline1 Publication1
Modified residuei3194-hydroxyproline1 Publication1
Modified residuei3224-hydroxyproline1 Publication1
Modified residuei3284-hydroxyproline1 Publication1
Modified residuei3464-hydroxyproline1 Publication1
Modified residuei3525-hydroxylysine1 Publication1
Modified residuei3614-hydroxyproline1 Publication1
Modified residuei3674-hydroxyproline1 Publication1
Modified residuei3704-hydroxyproline1 Publication1
Modified residuei3914-hydroxyproline1 Publication1
Modified residuei3944-hydroxyproline1 Publication1
Modified residuei4004-hydroxyproline1 Publication1
Modified residuei4064-hydroxyproline1 Publication1
Modified residuei4394-hydroxyproline1 Publication1
Modified residuei4424-hydroxyproline1 Publication1
Disulfide bondi1161 ↔ 1193PROSITE-ProRule annotation
Disulfide bondi1201 ↔ 1362PROSITE-ProRule annotation
Glycosylationi1265N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1270 ↔ 1315PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02465.
PeptideAtlasiP02465.
PRIDEiP02465.

Miscellaneous databases

PMAP-CutDBiP02465.

Expressioni

Tissue specificityi

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Gene expression databases

BgeeiENSBTAG00000013472.

Interactioni

Subunit structurei

Trimers of one alpha 2(I) and two alpha 1(I) chains.

GO - Molecular functioni

Protein-protein interaction databases

IntActiP02465. 1 interactor.
MINTiMINT-1346303.
STRINGi9913.ENSBTAP00000033771.

Structurei

3D structure databases

SMRiP02465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1131 – 1364Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST234

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02465.
KOiK06236.
OMAiDITIGNG.
OrthoDBiEOG091G03LV.
TreeFamiTF344135.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
InterProiView protein in InterPro
IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR014716. Fibrinogen_a/b/g_C_1.
PfamiView protein in Pfam
PF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078. Fib_collagen_C. 1 hit.
SMARTiView protein in SMART
SM00038. COLFI. 1 hit.
PROSITEiView protein in PROSITE
PS51461. NC1_FIB. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSFVDTRTL LLLAVTSCLA TCQSLQEATA RKGPSGDRGP RGERGPPGPP
60 70 80 90 100
GRDGDDGIPG PPGPPGPPGP PGLGGNFAAQ FDAKGGGPGP MGLMGPRGPP
110 120 130 140 150
GASGAPGPQG FQGPPGEPGE PGQTGPAGAR GPPGPPGKAG EDGHPGKPGR
160 170 180 190 200
PGERGVVGPQ GARGFPGTPG LPGFKGIRGH NGLDGLKGQP GAPGVKGEPG
210 220 230 240 250
APGENGTPGQ TGARGLPGER GRVGAPGPAG ARGSDGSVGP VGPAGPIGSA
260 270 280 290 300
GPPGFPGAPG PKGELGPVGN PGPAGPAGPR GEVGLPGLSG PVGPPGNPGA
310 320 330 340 350
NGLPGAKGAA GLPGVAGAPG LPGPRGIPGP VGAAGATGAR GLVGEPGPAG
360 370 380 390 400
SKGESGNKGE PGAVGQPGPP GPSGEEGKRG STGEIGPAGP PGPPGLRGNP
410 420 430 440 450
GSRGLPGADG RAGVMGPAGS RGATGPAGVR GPNGDSGRPG EPGLMGPRGF
460 470 480 490 500
PGSPGNIGPA GKEGPVGLPG IDGRPGPIGP AGARGEPGNI GFPGPKGPSG
510 520 530 540 550
DPGKAGEKGH AGLAGARGAP GPDGNNGAQG PPGLQGVQGG KGEQGPAGPP
560 570 580 590 600
GFQGLPGPAG TAGEAGKPGE RGIPGEFGLP GPAGARGERG PPGESGAAGP
610 620 630 640 650
TGPIGSRGPS GPPGPDGNKG EPGVVGAPGT AGPSGPSGLP GERGAAGIPG
660 670 680 690 700
GKGEKGETGL RGDIGSPGRD GARGAPGAIG APGPAGANGD RGEAGPAGPA
710 720 730 740 750
GPAGPRGSPG ERGEVGPAGP NGFAGPAGAA GQPGAKGERG TKGPKGENGP
760 770 780 790 800
VGPTGPVGAA GPSGPNGPPG PAGSRGDGGP PGATGFPGAA GRTGPPGPSG
810 820 830 840 850
ISGPPGPPGP AGKEGLRGPR GDQGPVGRSG ETGASGPPGF VGEKGPSGEP
860 870 880 890 900
GTAGPPGTPG PQGLLGAPGF LGLPGSRGER GLPGVAGSVG EPGPLGIAGP
910 920 930 940 950
PGARGPPGNV GNPGVNGAPG EAGRDGNPGN DGPPGRDGQP GHKGERGYPG
960 970 980 990 1000
NAGPVGAAGA PGPQGPVGPV GKHGNRGEPG PAGAVGPAGA VGPRGPSGPQ
1010 1020 1030 1040 1050
GIRGDKGEPG DKGPRGLPGL KGHNGLQGLP GLAGHHGDQG APGAVGPAGP
1060 1070 1080 1090 1100
RGPAGPSGPA GKDGRIGQPG AVGPAGIRGS QGSQGPAGPP GPPGPPGPPG
1110 1120 1130 1140 1150
PSGGGYEFGF DGDFYRADQP RSPTSLRPKD YEVDATLKSL NNQIETLLTP
1160 1170 1180 1190 1200
EGSRKNPART CRDLRLSHPE WSSGYYWIDP NQGCTMDAIK VYCDFSTGET
1210 1220 1230 1240 1250
CIRAQPEDIP VKNWYRNSKA KKHVWVGETI NGGTQFEYNV EGVTTKEMAT
1260 1270 1280 1290 1300
QLAFMRLLAN HASQNITYHC KNSIAYMDEE TGNLKKAVIL QGSNDVELVA
1310 1320 1330 1340 1350
EGNSRFTYTV LVDGCSKKTN EWQKTIIEYK TNKPSRLPIL DIAPLDIGGA
1360
DQEIRLNIGP VCFK
Length:1,364
Mass (Da):129,064
Last modified:May 30, 2000 - v2
Checksum:i5593F4D6B9ED119A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti157V → P AA sequence (PubMed:173531).Curated1
Sequence conflicti187K → T AA sequence (PubMed:173531).Curated1
Sequence conflicti211T → K AA sequence (PubMed:173531).Curated1
Sequence conflicti298 – 300PGA → AGP AA sequence (PubMed:173531).Curated3
Sequence conflicti423 – 424AT → TA AA sequence (PubMed:4412529).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008683 mRNA. Translation: BAA25171.1.
BC149095 mRNA. Translation: AAI49096.1.
PIRiA90596. CGBO2S.
RefSeqiNP_776945.1. NM_174520.2.
UniGeneiBt.53485.

Genome annotation databases

EnsembliENSBTAT00000033863; ENSBTAP00000033771; ENSBTAG00000013472.
GeneIDi282188.
KEGGibta:282188.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008683 mRNA. Translation: BAA25171.1.
BC149095 mRNA. Translation: AAI49096.1.
PIRiA90596. CGBO2S.
RefSeqiNP_776945.1. NM_174520.2.
UniGeneiBt.53485.

3D structure databases

SMRiP02465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02465. 1 interactor.
MINTiMINT-1346303.
STRINGi9913.ENSBTAP00000033771.

Protein family/group databases

Allergomei3550. Bos d alpha2I.0101.
896. Bos d alpha2I.

Proteomic databases

PaxDbiP02465.
PeptideAtlasiP02465.
PRIDEiP02465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000033863; ENSBTAP00000033771; ENSBTAG00000013472.
GeneIDi282188.
KEGGibta:282188.

Organism-specific databases

CTDi1278.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02465.
KOiK06236.
OMAiDITIGNG.
OrthoDBiEOG091G03LV.
TreeFamiTF344135.

Enzyme and pathway databases

ReactomeiR-BTA-114604. GPVI-mediated activation cascade.
R-BTA-1442490. Collagen degradation.
R-BTA-1474244. Extracellular matrix organization.
R-BTA-1650814. Collagen biosynthesis and modifying enzymes.
R-BTA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-BTA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-BTA-202733. Cell surface interactions at the vascular wall.
R-BTA-216083. Integrin cell surface interactions.
R-BTA-2214320. Anchoring fibril formation.
R-BTA-2243919. Crosslinking of collagen fibrils.
R-BTA-3000171. Non-integrin membrane-ECM interactions.
R-BTA-3000178. ECM proteoglycans.
R-BTA-430116. GP1b-IX-V activation signalling.
R-BTA-75892. Platelet Adhesion to exposed collagen.
R-BTA-76009. Platelet Aggregation (Plug Formation).
R-BTA-8874081. MET activates PTK2 signaling.
R-BTA-8948216. Collagen chain trimerization.

Miscellaneous databases

PMAP-CutDBiP02465.

Gene expression databases

BgeeiENSBTAG00000013472.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
InterProiView protein in InterPro
IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR014716. Fibrinogen_a/b/g_C_1.
PfamiView protein in Pfam
PF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078. Fib_collagen_C. 1 hit.
SMARTiView protein in SMART
SM00038. COLFI. 1 hit.
PROSITEiView protein in PROSITE
PS51461. NC1_FIB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCO1A2_BOVIN
AccessioniPrimary (citable) accession number: P02465
Secondary accession number(s): A6QP13, O62649
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2000
Last modified: May 10, 2017
This is version 136 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.