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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1179 – 11791CalciumBy similarity
Metal bindingi1181 – 11811CalciumBy similarity
Metal bindingi1182 – 11821Calcium; via carbonyl oxygenBy similarity
Metal bindingi1184 – 11841Calcium; via carbonyl oxygenBy similarity
Metal bindingi1187 – 11871CalciumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, 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-75892. Platelet Adhesion to exposed collagen.

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

Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Propeptidei23 – 7957N-terminal propeptide1 PublicationPRO_0000005798Add
BLAST
Chaini80 – 11001021Collagen alpha-2(I) chainPRO_0000005799Add
BLAST
Propeptidei1101 – 1364264C-terminal propeptidePRO_0000005800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801Pyrrolidone carboxylic acid
Modified residuei84 – 841AllysineCurated
Modified residuei175 – 17515-hydroxylysineCurated
Modified residuei196 – 19615-hydroxylysineCurated
Modified residuei262 – 26215-hydroxylysineCurated
Modified residuei307 – 30715-hydroxylysineCurated
Modified residuei352 – 35215-hydroxylysineCurated
Disulfide bondi1161 ↔ 1193PROSITE-ProRule annotation
Disulfide bondi1201 ↔ 1362PROSITE-ProRule annotation
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, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02465.
PeptideAtlasiP02465.
PRIDEiP02465.

Miscellaneous databases

PMAP-CutDBP02465.

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.

Protein-protein interaction databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1131 – 1364234Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

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
Contains 1 fibrillar collagen NC1 domain.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

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571V → P AA sequence (PubMed:173531).Curated
Sequence conflicti187 – 1871K → T AA sequence (PubMed:173531).Curated
Sequence conflicti211 – 2111T → K AA sequence (PubMed:173531).Curated
Sequence conflicti298 – 3003PGA → AGP AA sequence (PubMed:173531).Curated
Sequence conflicti423 – 4242AT → TA AA sequence (PubMed:4412529).Curated

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

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02465. 1 interaction.
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-75892. Platelet Adhesion to exposed collagen.

Miscellaneous databases

PMAP-CutDBP02465.

Gene expression databases

BgeeiENSBTAG00000013472.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO1A2_BOVIN
AccessioniPrimary (citable) accession number: P02465
Secondary accession number(s): A6QP13, O62649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2000
Last modified: September 7, 2016
This is version 131 of the entry and version 2 of the sequence. [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.