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Q01149

- CO1A2_MOUSE

UniProt

Q01149 - CO1A2_MOUSE

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Protein
Collagen alpha-2(I) chain
Gene
Col1a2, Cola2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1187 – 11871Calcium By similarity
Metal bindingi1189 – 11891Calcium By similarity
Metal bindingi1190 – 11901Calcium; via carbonyl oxygen By similarity
Metal bindingi1192 – 11921Calcium; via carbonyl oxygen By similarity
Metal bindingi1195 – 11951Calcium By similarity

GO - Molecular functioni

  1. SMAD binding Source: MGI
  2. extracellular matrix structural constituent Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: MGI
Complete GO annotation...

GO - Biological processi

  1. Rho protein signal transduction Source: Ensembl
  2. blood vessel development Source: Ensembl
  3. cellular response to amino acid stimulus Source: MGI
  4. collagen fibril organization Source: Ensembl
  5. protein heterotrimerization Source: MGI
  6. regulation of blood pressure Source: Ensembl
  7. skeletal system development Source: Ensembl
  8. skin morphogenesis Source: Ensembl
  9. transforming growth factor beta receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196515. Crosslinking of collagen fibrils.
REACT_196581. Scavenging by Class A Receptors.
REACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.
REACT_220092. GPVI-mediated activation cascade.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(I) chain
Alternative name(s):
Alpha-2 type I collagen
Gene namesi
Name:Col1a2
Synonyms:Cola2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:88468. Col1a2.

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: MGI
  2. collagen type I trimer Source: MGI
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Propeptidei23 – 8563N-terminal propeptide By similarity
PRO_0000005807Add
BLAST
Chaini86 – 11081023Collagen alpha-2(I) chain
PRO_0000005808Add
BLAST
Propeptidei1109 – 1372264C-terminal propeptide By similarity
PRO_0000005809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861Pyrrolidone carboxylic acid By similarity
Modified residuei90 – 901Allysine By similarity
Disulfide bondi1169 ↔ 1201 By similarity
Disulfide bondi1209 ↔ 1370 By similarity
Glycosylationi1273 – 12731N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1278 ↔ 1323 By similarity

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

MaxQBiQ01149.
PaxDbiQ01149.
PRIDEiQ01149.

PTM databases

PhosphoSiteiQ01149.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ01149.
BgeeiQ01149.
CleanExiMM_COL1A2.
GenevestigatoriQ01149.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ01149. 1 interaction.
MINTiMINT-4091346.

Structurei

3D structure databases

ProteinModelPortaliQ01149.
SMRiQ01149. Positions 1158-1371.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1139 – 1372234Fibrillar collagen NC1
Add
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.

Sequence similaritiesi

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiQ01149.
KOiK06236.
OMAiKNGDKGH.
OrthoDBiEOG7TJ3HH.
PhylomeDBiQ01149.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 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.

Q01149-1 [UniParc]FASTAAdd to Basket

« Hide

MLSFVDTRTL LLLAVTSCLA TCQYLQSGSV RKGPTGDRGP RGQRGPAGPR     50
GRDGVDGPMG PPGPPGSPGP PGSPAPPGLT GNFAAQYSDK GVSSGPGPMG 100
LMGPRGPPGA VGAPGPQGFQ GPAGEPGEPG QTGPAGPRGP AGSPGKAGED 150
GHPGKPGRPG ERGVVGPQGA RGFPGTPGLP GFKGVKGHSG MDGLKGQPGA 200
QGVKGEPGAP GENGTPGQAG ARGLPGERGR VGAPGPAGAR GSDGSVGPVG 250
PAGPIGSAGP PGFPGAPGPK GELGPVGNPG PAGPAGPRGE VGLPGLSGPV 300
GPPGNPGTNG LTGAKGATGL PGVAGAPGLP GPRGIPGPAG AAGATGARGL 350
VGEPGPAGSK GESGNKGEPG SVGAQGPPGP SGEEGKRGSP GEAGSAGPAG 400
PPGLRGSPGS RGLPGADGRA GVMGPPGNRG STGPAGIRGP NGDAGRPGEP 450
GLMGPRGLPG SPGNVGPSGK EGPVGLPGID GRPGPIGPAG PRGEAGNIGF 500
PGPKGPSGDP GKPGERGHPG LAGARGAPGP DGNNGAQGPP GPQGVQGGKG 550
EQGPAGPPGF QGLPGPSGTT GEVGKPGERG LPGEFGLPGP AGPRGERGTP 600
GESGAAGPSG PIGSRGPSGA PGPDGNKGEA GAVGAPGSAG ASGPGGLPGE 650
RGAAGIPGGK GEKGETGLRG DTGNTGRDGA RGIPGAVGAP GPAGASGDRG 700
EAGAAGPSGP AGPRGSPGER GEVGPAGPNG FAGPAGAAGQ PGAKGEKGTK 750
GPKGENGIVG PTGSVGAAGP SGPNGPPGPV GSRGDGGPPG MTGFPGAAGR 800
TGPPGPSGIA GPPGPPGAAG KEGIRGPRGD QGPVGRTGET GASGPPGFVG 850
EKGPSGEPGT AGAPGTAGPQ GLLGAPGILG LPGSRGERGL PGIAGALGEP 900
GPLGISGPPG ARGPPGAVGS PGVNGAPGEA GRDGNPGSDG PPGRDGQPGH 950
KGERGYPGSI GPTGAAGAPG PHGSVGPAGK HGNRGEPGPA GSVGPVGAVG 1000
PRGPSGPQGI RGDKGEPGDK GHRGLPGLKG YSGLQGLPGL AGLHGDQGAP 1050
GPVGPAGPRG PAGPSGPVGK DGRSGQPGPV GPAGVRGSQG SQGPAGPPGP 1100
PGPPGPPGVS GGGYDFGFEG DFYRADQPRS QPSLRPKDYE VDATLKSLNN 1150
QIETLLTPEG SRKNPARTCR DLRLSHPEWN SDYYWIDPNQ GCTMDAIKVY 1200
CDFSTGETCI QAQPVNTPAK NSYSRAQANK HVWLGETING GSQFEYNVEG 1250
VSSKEMATQL AFMRLLANRA SQNITYHCKN SIAYLDEETG SLNKAVLLQG 1300
SNDVELVAEG NSRFTYSVLV DGCSKKTNEW GKTIIEYKTN KPSRLPFLDI 1350
APLDIGGADQ EFRVEVGPVC FK 1372
Length:1,372
Mass (Da):129,557
Last modified:August 29, 2001 - v2
Checksum:i0D17DF5D6C1452D1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151V → A in AAA37331. 1 Publication
Sequence conflicti1167 – 11671R → TT in CAA41205. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58251 mRNA. Translation: CAA41205.1.
BC007158 mRNA. Translation: AAH07158.1.
BC042503 mRNA. Translation: AAH42503.2.
K01832 Genomic DNA. Translation: AAA37331.1.
CCDSiCCDS39420.1.
PIRiA43291.
RefSeqiNP_031769.2. NM_007743.2.
UniGeneiMm.277792.

Genome annotation databases

EnsembliENSMUST00000031668; ENSMUSP00000031668; ENSMUSG00000029661.
GeneIDi12843.
KEGGimmu:12843.
UCSCiuc009avm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58251 mRNA. Translation: CAA41205.1 .
BC007158 mRNA. Translation: AAH07158.1 .
BC042503 mRNA. Translation: AAH42503.2 .
K01832 Genomic DNA. Translation: AAA37331.1 .
CCDSi CCDS39420.1.
PIRi A43291.
RefSeqi NP_031769.2. NM_007743.2.
UniGenei Mm.277792.

3D structure databases

ProteinModelPortali Q01149.
SMRi Q01149. Positions 1158-1371.
ModBasei Search...

Protein-protein interaction databases

IntActi Q01149. 1 interaction.
MINTi MINT-4091346.

PTM databases

PhosphoSitei Q01149.

Proteomic databases

MaxQBi Q01149.
PaxDbi Q01149.
PRIDEi Q01149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031668 ; ENSMUSP00000031668 ; ENSMUSG00000029661 .
GeneIDi 12843.
KEGGi mmu:12843.
UCSCi uc009avm.1. mouse.

Organism-specific databases

CTDi 1278.
MGIi MGI:88468. Col1a2.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi Q01149.
KOi K06236.
OMAi KNGDKGH.
OrthoDBi EOG7TJ3HH.
PhylomeDBi Q01149.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_196515. Crosslinking of collagen fibrils.
REACT_196581. Scavenging by Class A Receptors.
REACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.
REACT_220092. GPVI-mediated activation cascade.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

ChiTaRSi COL1A2. mouse.
NextBioi 282380.
PROi Q01149.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01149.
Bgeei Q01149.
CleanExi MM_COL1A2.
Genevestigatori Q01149.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a full-length cDNA for the murine pro alpha 2(I) collagen chain: comparison of the derived primary structure with human pro alpha 2(I) collagen."
    Phillips C.L., Morgan A.L., Lever L.W., Wenstrup R.J.
    Genomics 13:1345-1346(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Calvaria.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. "Construction of a full-length murine pro alpha 2(I) collagen cDNA by the polymerase chain reaction."
    Phillips C.L., Lever L.W., Pinnell S.R., Quarles L.D., Wenstrup R.J.
    J. Invest. Dermatol. 97:980-984(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-110.
    Tissue: Calvaria.
  4. "Identification of a cell-specific transcriptional enhancer in the first intron of the mouse alpha 2 (type I) collagen gene."
    Rossi P., de Crombrugghe B.
    Proc. Natl. Acad. Sci. U.S.A. 84:5590-5594(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.

Entry informationi

Entry nameiCO1A2_MOUSE
AccessioniPrimary (citable) accession number: Q01149
Secondary accession number(s): Q8CGA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: August 29, 2001
Last modified: September 3, 2014
This is version 127 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi