Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Collagen alpha-2(I) chain

Gene

Col1a2

Organism
Rattus norvegicus (Rat)
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 bindingi1187CalciumBy similarity1
Metal bindingi1189CalciumBy similarity1
Metal bindingi1190Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1192Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1195CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cellular response to organic substance Source: RGD
  • cellular response to retinoic acid Source: RGD
  • cellular response to thyroid hormone stimulus Source: RGD
  • extracellular matrix organization Source: Reactome
  • response to norepinephrine Source: RGD
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-3000178. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(I) chain
Alternative name(s):
Alpha-2 type I collagen
Gene namesi
Name:Col1a2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621351. Col1a2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
PropeptideiPRO_000000581223 – 85N-terminal propeptideBy similarityAdd BLAST63
ChainiPRO_000000581386 – 1108Collagen alpha-2(I) chainAdd BLAST1023
PropeptideiPRO_00000058141109 – 1372C-terminal propeptideBy similarityAdd BLAST264

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei86Pyrrolidone carboxylic acidCurated1
Modified residuei90Allysine1
Disulfide bondi1169 ↔ 1201PROSITE-ProRule annotation
Disulfide bondi1209 ↔ 1370PROSITE-ProRule annotation
Glycosylationi1273N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1278 ↔ 1323PROSITE-ProRule annotation

Post-translational modificationi

Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02466.
PRIDEiP02466.

PTM databases

iPTMnetiP02466.
PhosphoSitePlusiP02466.

Miscellaneous databases

PMAP-CutDBP02466.

Expressioni

Tissue specificityi

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. Expressed in flagella of epididymal sperm.1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi249912. 1 interactor.
DIPiDIP-37338N.
IntActiP02466. 1 interactor.
STRINGi10116.ENSRNOP00000016423.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HQVfiber diffraction5.16B86-1113[»]
3HR2fiber diffraction5.16B86-1113[»]
SMRiP02466.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02466.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1139 – 1372Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST234

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi783 – 785Cell attachment siteSequence analysis3
Motifi828 – 830Cell attachment siteSequence analysis3
Motifi1011 – 1013Cell attachment siteSequence analysis3

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.
ENOG410ZZWR. LUCA.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02466.
KOiK06236.
PhylomeDBiP02466.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 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.

P02466-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSFVDTRTL LLLAVTSCLA TCQSLQMGSV RKGPTGDRGP RGQRGPAGPR
60 70 80 90 100
GRDGVDGPVG PPGPPGAPGP PGPPGPPGLT GNFAAQYSDK GVSAGPGPMG
110 120 130 140 150
LMGPRGPPGA VGAPGPQGFQ GPAGEPGEPG QTGPAGSRGP AGPPGKAGED
160 170 180 190 200
GHPGKPGRPG ERGVVGPQGA RGFPGTPGLP GFKGIRGHNG LDGLKGQPGA
210 220 230 240 250
QGVKGEPGAP GENGTPGQAG ARGLPGERGR VGAPGPAGAR GSDGSVGPVG
260 270 280 290 300
PAGPIGSAGP PGFPGAPGPK GELGPVGNPG PAGPAGPRGE AGLPGLSGPV
310 320 330 340 350
GPPGNPGANG LTGAKGATGL PGVAGAPGLP GPRGIPGPVG AAGATGPRGL
360 370 380 390 400
VGEPGPAGSK GETGNKGEPG SAGAQGPPGP SGEEGKRGSP GEPGSAGPAG
410 420 430 440 450
PPGLRGSPGS RGLPGADGRA GVMGPPGNRG STGPAGVRGP NGDAGRPGEP
460 470 480 490 500
GLMGPRGLPG SPGNVGPAGK EGPVGLPGID GRPGPIGPAG PRGEAGNIGF
510 520 530 540 550
PGPKGPSGDP GKPGEKGHPG LAGARGAPGP DGNNGAQGPP GPQGVQGGKG
560 570 580 590 600
EQGPAGPPGF QGLPGPSGTA GEVGKPGERG LPGEFGLPGP AGPRGERGPP
610 620 630 640 650
GESGAAGPSG PIGIRGPSGA PGPDGNKGEA GAVGAPGSAG ASGPGGLPGE
660 670 680 690 700
RGAAGIPGGK GEKGETGLRG EIGNPGRDGA RGAPGAIGAP GPAGASGDRG
710 720 730 740 750
EAGAAGPSGP AGPRGSPGER GEVGPAGPNG FAGPAGSAGQ PGAKGEKGTK
760 770 780 790 800
GPKGENGIVG PTGPVGAAGP SGPNGPPGPA GSRGDGGPPG MTGFPGAAGR
810 820 830 840 850
TGPPGPSGIT GPPGPPGAAG KEGIRGPRGD QGPVGRTGEI GASGPPGFAG
860 870 880 890 900
EKGPSGEPGT TGPPGTAGPQ GLLGAPGILG LPGSRGERGQ PGIAGALGEP
910 920 930 940 950
GPLGIAGPPG ARGPPGAVGS PGVNGAPGEA GRDGNPGSDG PPGRDGQPGH
960 970 980 990 1000
KGERGYPGNI GPTGAAGAPG PHGSVGPAGK HGNRGEPGPA GSVGPVGAVG
1010 1020 1030 1040 1050
PRGPSGPQGI RGDKGEPGDK GARGLPGLKG HNGLQGLPGL AGLHGDQGAP
1060 1070 1080 1090 1100
GPVGPAGPRG PAGPSGPIGK DGRSGHPGPV GPAGVRGSQG SQGPAGPPGP
1110 1120 1130 1140 1150
PGPPGPPGVS GGGYDFGFEG GFYRADQPRS QPSLRPKDYE VDATLKSLNN
1160 1170 1180 1190 1200
QIETLLTPEG SRKNPARTCR DLRLSHPEWK SDYYWIDPNQ GCTMDAIKVY
1210 1220 1230 1240 1250
CDFSTGETCI QAQPVNTPAK NAYSRAQANK HVWLGETING GSQFEYNAEG
1260 1270 1280 1290 1300
VSSKEMATQL AFMRLLANRA SQNITYHCKN SIAYLDEETG RLNKAVILQG
1310 1320 1330 1340 1350
SNDVELVAEG NSRFTYTVLV DGCSKKTNEW DKTVIEYKTN KPSRLPFLDI
1360 1370
APLDIGGTNQ EFRVEVGPVC FK
Length:1,372
Mass (Da):129,564
Last modified:August 29, 2001 - v3
Checksum:iB069371A8DB20A72
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti132T → P AA sequence (PubMed:4636752).Curated1
Sequence conflicti137S → P AA sequence (PubMed:4636752).Curated1
Sequence conflicti431 – 432ST → TS AA sequence (PubMed:5544653).Curated2
Sequence conflicti494E → Z AA sequence (PubMed:4435743).Curated1
Sequence conflicti497N → A AA sequence (PubMed:4435743).Curated1
Sequence conflicti825R → K AA sequence (PubMed:4763308).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121217 mRNA. Translation: AAD41775.1.
RefSeqiNP_445808.1. NM_053356.1.
UniGeneiRn.107239.

Genome annotation databases

GeneIDi84352.
KEGGirno:84352.
UCSCiRGD:621351. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121217 mRNA. Translation: AAD41775.1.
RefSeqiNP_445808.1. NM_053356.1.
UniGeneiRn.107239.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HQVfiber diffraction5.16B86-1113[»]
3HR2fiber diffraction5.16B86-1113[»]
SMRiP02466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249912. 1 interactor.
DIPiDIP-37338N.
IntActiP02466. 1 interactor.
STRINGi10116.ENSRNOP00000016423.

PTM databases

iPTMnetiP02466.
PhosphoSitePlusiP02466.

Proteomic databases

PaxDbiP02466.
PRIDEiP02466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84352.
KEGGirno:84352.
UCSCiRGD:621351. rat.

Organism-specific databases

CTDi1278.
RGDi621351. Col1a2.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410ZZWR. LUCA.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02466.
KOiK06236.
PhylomeDBiP02466.

Enzyme and pathway databases

ReactomeiR-RNO-3000178. ECM proteoglycans.

Miscellaneous databases

EvolutionaryTraceiP02466.
PMAP-CutDBP02466.
PROiP02466.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 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_RAT
AccessioniPrimary (citable) accession number: P02466
Secondary accession number(s): Q9R1E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 29, 2001
Last modified: November 2, 2016
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.