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Protein

Collagen alpha-2(I) chain

Gene

COL1A2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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

Organism-specific databases

VGNCiVGNC:27561 COL1A2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 residuei23Pyrrolidone carboxylic acidBy similarity1
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

ComplexPortaliCPX-3101 Collagen type I trimer
IntActiP02465, 1 interactor
MINTiP02465
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
GeneTreeiENSGT00900000140789
HOGENOMiHOG000085654
HOVERGENiHBG004933
InParanoidiP02465
KOiK06236
OMAiPEWSSGY
OrthoDBiEOG091G03LV
TreeFamiTF344135

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
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

Similar proteinsi

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: June 20, 2018
This is version 145 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

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