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Protein

Collagen alpha-2(I) chain

Gene

COL1A2

Organism
Gallus gallus (Chicken)
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 bindingi1176CalciumBy similarity1
Metal bindingi1178CalciumBy similarity1
Metal bindingi1179Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1181Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1184CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-GGA-1442490 Collagen degradation
R-GGA-1474244 Extracellular matrix organization
R-GGA-1650814 Collagen biosynthesis and modifying enzymes
R-GGA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-GGA-2022090 Assembly of collagen fibrils and other multimeric structures
R-GGA-216083 Integrin cell surface interactions
R-GGA-2243919 Crosslinking of collagen fibrils
R-GGA-3000171 Non-integrin membrane-ECM interactions
R-GGA-3000178 ECM proteoglycans
R-GGA-430116 GP1b-IX-V activation signalling
R-GGA-75892 Platelet Adhesion to exposed collagen
R-GGA-76009 Platelet Aggregation (Plug Formation)
R-GGA-8874081 MET activates PTK2 signaling
R-GGA-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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 2

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
PropeptideiPRO_000000581523 – 77N-terminal propeptideBy similarityAdd BLAST55
ChainiPRO_000000581678 – 1117Collagen alpha-2(I) chainAdd BLAST1040
PropeptideiPRO_00000058171118 – 1363C-terminal propeptideBy similarityAdd BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Pyrrolidone carboxylic acidBy similarity1
Modified residuei78Pyrrolidone carboxylic acid2 Publications1 Publication1
Modified residuei83Allysine1 Publication1
Modified residuei1765-hydroxylysine; alternateBy similarity1
Glycosylationi176O-linked (Gal...) hydroxylysine; alternateBy similarity1
Modified residuei4404-hydroxyproline1 Publication1
Modified residuei4434-hydroxyproline1 Publication1
Disulfide bondi1158 ↔ 1190PROSITE-ProRule annotation
Disulfide bondi1198 ↔ 1361PROSITE-ProRule annotation
Glycosylationi1264N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1269 ↔ 1314PROSITE-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.1 Publication
The N-terminus of the mature protein is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02467
PRIDEiP02467

Miscellaneous databases

PMAP-CutDBiP02467

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSGALG00000009641

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

ComplexPortaliCPX-3102 Collagen type I trimer
STRINGi9031.ENSGALP00000015687

Structurei

3D structure databases

SMRiP02467
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1128 – 1363Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST236

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

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00900000140789
HOVERGENiHBG004933
InParanoidiP02467
OrthoDBiEOG091G03LV
PhylomeDBiP02467
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.

P02467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSFVDTRIL LLLAVTSYLA TSQHLFQASA GRKGPRGDKG PQGERGPPGP
60 70 80 90 100
PGRDGEDGPP GPPGPPGPPG LGGNFAAQYD PSKAADFGPG PMGLMGPRGP
110 120 130 140 150
PGASGPPGPP GFQGVPGEPG EPGQTGPQGP RGPPGPPGKA GEDGHPGKPG
160 170 180 190 200
RPGERGVAGP QGARGFPGTP GLPGFKGIRG HNGLDGQKGQ PGTPGTKGEP
210 220 230 240 250
GAPGENGTPG QPGARGLPGE RGRIGAPGPA GARGSDGSAG PTGPAGPIGA
260 270 280 290 300
AGPPGFPGAP GAKGEIGPAG NVGPTGPAGP RGEIGLPGSS GPVGPPGNPG
310 320 330 340 350
ANGLPGAKGA AGLPGVAGAP GLPGPRGIPG PPGPAGPSGA RGLVGEPGPA
360 370 380 390 400
GAKGESGNKG EPGAAGPPGP PGPSGEEGKR GSNGEPGSAG PPGPAGLRGV
410 420 430 440 450
PGSRGLPGAD GRAGVMGPAG NRGASGPVGA KGPNGDAGRP GEPGLMGPRG
460 470 480 490 500
LPGQPGSPGP AGKEGPVGFP GADGRVGPIG PAGNRGEPGN IGFPGPKGPT
510 520 530 540 550
GEPGKPGEKG NVGLAGPRGA PGPEGNNGAQ GPPGVTGNQG AKGETGPAGP
560 570 580 590 600
PGFQGLPGPS GPAGEAGKPG ERGLHGEFGV PGPAGPRGER GLPGESGAVG
610 620 630 640 650
PAGPIGSRGP SGPPGPDGNK GEPGNVGPAG APGPAGPGGI PGERGVAGVP
660 670 680 690 700
GGKGEKGAPG LRGDTGATGR DGARGLPGAI GAPGPAGGAG DRGEGGPAGP
710 720 730 740 750
AGPAGARGIP GERGEPGPVG PSGFAGPPGA AGQPGAKGER GPKGPKGETG
760 770 780 790 800
PTGAIGPIGA SGPPGPVGAA GPAGPRGDAG PPGMTGFPGA AGRVGPPGPA
810 820 830 840 850
GITGPPGPPG PAGKDGPRGL RGDVGPVGRT GEQGIAGPPG FAGEKGPSGE
860 870 880 890 900
AGAAGPPGTP GPQGILGAPG ILGLPGSRGE RGLPGIAGAT GEPGPLGVSG
910 920 930 940 950
PPGARGPSGP VGSPGPNGAP GEAGRDGNPG NDGPPGRDGA PGFKGERGAP
960 970 980 990 1000
GNPGPSGALG APGPHGQVGP SGKPGNRGDP GPVGPVGPAG AFGPRGLAGP
1010 1020 1030 1040 1050
QGPRGEKGEP GDKGHRGLPG LKGHNGLQGL PGLAGQHGDQ GPPGNNGPAG
1060 1070 1080 1090 1100
PRGPPGPSGP PGKDGRNGLP GPIGPAGVRG SHGSQGPAGP PGPPGPPGPP
1110 1120 1130 1140 1150
GPNGGGYEVG FDAEYYRADQ PSLRPKDYEV DATLKTLNNQ IETLLTPEGS
1160 1170 1180 1190 1200
KKNPARTCRD LRLSHPEWSS GFYWIDPNQG CTADAIRAYC DFATGETCIH
1210 1220 1230 1240 1250
ASLEDIPTKT WYVSKNPKDK KHIWFGETIN GGTQFEYNGE GVTTKDMATQ
1260 1270 1280 1290 1300
LAFMRLLANH ASQNITYHCK NSIAYMDEET GNLKKAVILQ GSNDVELRAE
1310 1320 1330 1340 1350
GNSRFTFSVL VDGCSKKNNK WGKTIIEYRT NKPSRLPILD IAPLDIGGAD
1360
QEFGLHIGPV CFK
Length:1,363
Mass (Da):128,995
Last modified:May 10, 2017 - v3
Checksum:i41FFEE5077B428B4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti428 – 430VGA → AGV AA sequence (PubMed:5544653).Curated3
Sequence conflicti974P → L in AAA48638 (PubMed:6159982).Curated1
Sequence conflicti1010P → H in AAA51615 (PubMed:6267043).Curated1
Sequence conflicti1055P → H in AAA51615 (PubMed:6267043).Curated1
Sequence conflicti1061P → H in AAA51615 (PubMed:6267043).Curated1
Sequence conflicti1262S → P in AAA51615 (PubMed:6267043).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN04000096 Genomic DNA No translation available.
M25963
, M25956, M25959, M25961, M25962 Genomic DNA Translation: AAA69960.1
M25965, M25964 Genomic DNA Translation: AAA69961.1
M25984
, M25957, M25966, M25967, M25969, M25970, M25971, M25972, M25973, M25974, M25976, M25977, M25978, M25979, M25980, M25981, M25982, M25983 Genomic DNA Translation: AAA69962.1
J00826, J00821, K00792 Genomic DNA Translation: AAA51611.1
J00830, J00829 Genomic DNA Translation: AAA51613.1
J00837 Genomic DNA Translation: AAA51614.1
J00812
, J00811, J00814, J00815 Genomic DNA Translation: AAA51615.1
X02657 mRNA Translation: CAA26493.1
K00794 Genomic DNA No translation available.
V00390 mRNA Translation: CAA23688.1
M17608 mRNA Translation: AAA48673.1
M10581 Genomic DNA Translation: AAA48637.1
M10540 Genomic DNA Translation: AAA48638.1
J00828, J00827 Genomic DNA Translation: AAA51612.1
J00832, J00831 Genomic DNA Translation: AAD22117.1
J00833 Genomic DNA No translation available.
J00822 Genomic DNA No translation available.
PIRiI50173
I50206 CGCH2S
S10847
UniGeneiGga.5097

Genome annotation databases

EnsembliENSGALT00000015703; ENSGALP00000015687; ENSGALG00000009641

Similar proteinsi

Entry informationi

Entry nameiCO1A2_CHICK
AccessioniPrimary (citable) accession number: P02467
Secondary accession number(s): F1P0H9
, P87491, P87492, Q90758, Q90792, Q90795, Q90797, Q92014
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 10, 2017
Last modified: June 20, 2018
This is version 133 of the entry and version 3 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

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