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UniProtKB - P02466 (CO1A2_RAT)
Protein
Collagen alpha-2(I) chain
Gene
Col1a2
Organism
Rattus norvegicus (Rat)
Status
Functioni
Type I collagen is a member of group I collagen (fibrillar forming collagen).
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 1187 | CalciumBy similarity | 1 | |
Metal bindingi | 1189 | CalciumBy similarity | 1 | |
Metal bindingi | 1190 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1192 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1195 | CalciumBy similarity | 1 |
GO - Molecular functioni
- extracellular matrix structural constituent Source: GO_Central
- identical protein binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- platelet-derived growth factor binding Source: RGD
- protease binding Source: RGD
- protein-macromolecule adaptor activity Source: RGD
- SMAD binding Source: RGD
GO - Biological processi
- blood vessel development Source: RGD
- bone mineralization Source: RGD
- cellular response to amino acid stimulus Source: RGD
- cellular response to organic substance Source: RGD
- cellular response to retinoic acid Source: RGD
- cellular response to thyroid hormone stimulus Source: RGD
- collagen fibril organization Source: RGD
- collagen metabolic process Source: RGD
- extracellular matrix assembly Source: RGD
- extracellular matrix organization Source: GO_Central
- protein heterotrimerization Source: RGD
- regulation of blood pressure Source: RGD
- response to norepinephrine Source: RGD
- Rho protein signal transduction Source: RGD
- skeletal system development Source: RGD
- skin morphogenesis Source: RGD
- transforming growth factor beta receptor signaling pathway Source: RGD
Keywordsi
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-RNO-114604, GPVI-mediated activation cascade R-RNO-1442490, Collagen degradation R-RNO-1474244, Extracellular matrix organization R-RNO-1650814, Collagen biosynthesis and modifying enzymes R-RNO-198933, Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell R-RNO-2022090, Assembly of collagen fibrils and other multimeric structures R-RNO-202733, Cell surface interactions at the vascular wall R-RNO-216083, Integrin cell surface interactions R-RNO-2243919, Crosslinking of collagen fibrils R-RNO-3000171, Non-integrin membrane-ECM interactions R-RNO-3000178, ECM proteoglycans R-RNO-430116, GP1b-IX-V activation signalling R-RNO-75892, Platelet Adhesion to exposed collagen R-RNO-76009, Platelet Aggregation (Plug Formation) R-RNO-8874081, MET activates PTK2 signaling R-RNO-8948216, Collagen chain trimerization |
Names & Taxonomyi
Protein namesi | Recommended name: Collagen alpha-2(I) chainAlternative name(s): Alpha-2 type I collagen |
Gene namesi | Name:Col1a2 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 621351, Col1a2 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix PROSITE-ProRule annotation
Extracellular region or secreted
- extracellular region Source: Reactome
- extracellular space Source: RGD
Other locations
- collagen trimer Source: RGD
- collagen type I trimer Source: RGD
- extracellular matrix Source: GO_Central
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 22 | 1 PublicationAdd BLAST | 22 | |
PropeptideiPRO_0000005812 | 23 – 85 | N-terminal propeptideBy similarityAdd BLAST | 63 | |
ChainiPRO_0000005813 | 86 – 1125 | Collagen alpha-2(I) chainAdd BLAST | 1040 | |
PropeptideiPRO_0000005814 | 1126 – 1372 | C-terminal propeptideBy similarityAdd BLAST | 247 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 23 | Pyrrolidone carboxylic acidBy similarity | 1 | |
Modified residuei | 86 | Pyrrolidone carboxylic acid1 Publication | 1 | |
Modified residuei | 90 | Allysine1 Publication | 1 | |
Modified residuei | 183 | 5-hydroxylysine; alternateBy similarity | 1 | |
Glycosylationi | 183 | O-linked (Gal...) hydroxylysine; alternateBy similarity | 1 | |
Disulfide bondi | 1169 ↔ 1201 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1209 ↔ 1370 | PROSITE-ProRule annotation | ||
Glycosylationi | 1273 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1278 ↔ 1323 | PROSITE-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 acidProteomic databases
PaxDbi | P02466 |
PRIDEi | P02466 |
PTM databases
GlyGeni | P02466, 2 sites |
iPTMneti | P02466 |
PhosphoSitePlusi | P02466 |
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.
GO - Molecular functioni
- identical protein binding Source: RGD
- platelet-derived growth factor binding Source: RGD
- protease binding Source: RGD
- SMAD binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 249912, 2 interactors |
ComplexPortali | CPX-3104, Collagen type I trimer |
DIPi | DIP-37338N |
IntActi | P02466, 2 interactors |
STRINGi | 10116.ENSRNOP00000016423 |
Structurei
3D structure databases
AlphaFoldDBi | P02466 |
SMRi | P02466 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P02466 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1139 – 1372 | Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST | 234 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 28 – 1135 | DisorderedSequence analysisAdd BLAST | 1108 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 783 – 785 | Cell attachment siteSequence analysis | 3 | |
Motifi | 828 – 830 | Cell attachment siteSequence analysis | 3 | |
Motifi | 1011 – 1013 | Cell attachment siteSequence analysis | 3 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 58 – 78 | Pro residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 254 – 268 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1094 – 1108 | Pro residuesSequence analysisAdd BLAST | 15 |
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, SignalPhylogenomic databases
eggNOGi | KOG3544, Eukaryota |
InParanoidi | P02466 |
OrthoDBi | 1406711at2759 |
PhylomeDBi | P02466 |
Family and domain databases
InterProi | View protein in InterPro IPR008160, Collagen IPR000885, Fib_collagen_C |
Pfami | View protein in Pfam PF01410, COLFI, 1 hit PF01391, Collagen, 7 hits |
SMARTi | View protein in SMART SM00038, COLFI, 1 hit |
PROSITEi | View protein in PROSITE PS51461, NC1_FIB, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
P02466-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1LS40 | F1LS40_RAT | Collagen alpha-2(I) chain | Col1a2 | 1,372 | Annotation score: | ||
A0A0G2K5E8 | A0A0G2K5E8_RAT | Collagen alpha-2(I) chain | NEWGENE_621351 Col1a2 | 1,288 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 132 | T → P AA sequence (PubMed:4636752).Curated | 1 | |
Sequence conflicti | 137 | S → P AA sequence (PubMed:4636752).Curated | 1 | |
Sequence conflicti | 431 – 432 | ST → TS AA sequence (PubMed:5544653).Curated | 2 | |
Sequence conflicti | 494 | E → Z AA sequence (PubMed:4435743).Curated | 1 | |
Sequence conflicti | 497 | N → A AA sequence (PubMed:4435743).Curated | 1 | |
Sequence conflicti | 825 | R → K AA sequence (PubMed:4763308).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF121217 mRNA Translation: AAD41775.1 |
RefSeqi | NP_445808.1, NM_053356.1 |
Genome annotation databases
GeneIDi | 84352 |
KEGGi | rno:84352 |
UCSCi | RGD:621351, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF121217 mRNA Translation: AAD41775.1 |
RefSeqi | NP_445808.1, NM_053356.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3HQV | fiber diffraction | 5.16 | B | 86-1113 | [»] | |
3HR2 | fiber diffraction | 5.16 | B | 86-1113 | [»] | |
AlphaFoldDBi | P02466 | |||||
SMRi | P02466 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 249912, 2 interactors |
ComplexPortali | CPX-3104, Collagen type I trimer |
DIPi | DIP-37338N |
IntActi | P02466, 2 interactors |
STRINGi | 10116.ENSRNOP00000016423 |
PTM databases
GlyGeni | P02466, 2 sites |
iPTMneti | P02466 |
PhosphoSitePlusi | P02466 |
Proteomic databases
PaxDbi | P02466 |
PRIDEi | P02466 |
Genome annotation databases
GeneIDi | 84352 |
KEGGi | rno:84352 |
UCSCi | RGD:621351, rat |
Organism-specific databases
CTDi | 1278 |
RGDi | 621351, Col1a2 |
Phylogenomic databases
eggNOGi | KOG3544, Eukaryota |
InParanoidi | P02466 |
OrthoDBi | 1406711at2759 |
PhylomeDBi | P02466 |
Enzyme and pathway databases
Reactomei | R-RNO-114604, GPVI-mediated activation cascade R-RNO-1442490, Collagen degradation R-RNO-1474244, Extracellular matrix organization R-RNO-1650814, Collagen biosynthesis and modifying enzymes R-RNO-198933, Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell R-RNO-2022090, Assembly of collagen fibrils and other multimeric structures R-RNO-202733, Cell surface interactions at the vascular wall R-RNO-216083, Integrin cell surface interactions R-RNO-2243919, Crosslinking of collagen fibrils R-RNO-3000171, Non-integrin membrane-ECM interactions R-RNO-3000178, ECM proteoglycans R-RNO-430116, GP1b-IX-V activation signalling R-RNO-75892, Platelet Adhesion to exposed collagen R-RNO-76009, Platelet Aggregation (Plug Formation) R-RNO-8874081, MET activates PTK2 signaling R-RNO-8948216, Collagen chain trimerization |
Miscellaneous databases
EvolutionaryTracei | P02466 |
PROi | PR:P02466 |
Family and domain databases
InterProi | View protein in InterPro IPR008160, Collagen IPR000885, Fib_collagen_C |
Pfami | View protein in Pfam PF01410, COLFI, 1 hit PF01391, Collagen, 7 hits |
SMARTi | View protein in SMART SM00038, COLFI, 1 hit |
PROSITEi | View protein in PROSITE PS51461, NC1_FIB, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CO1A2_RAT | |
Accessioni | P02466Primary (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: | May 25, 2022 | |
This is version 159 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families