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Q01149 (CO1A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-2(I) chain
Alternative name(s):
Alpha-2 type I collagen
Gene names
Name:Col1a2
Synonyms:Cola2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Secreted › extracellular space › extracellular matrix By similarity.

Tissue specificity

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

Domain

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.

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 8563N-terminal propeptide By similarity
PRO_0000005807
Chain86 – 11081023Collagen alpha-2(I) chain
PRO_0000005808
Propeptide1109 – 1372264C-terminal propeptide By similarity
PRO_0000005809

Regions

Domain1139 – 1372234Fibrillar collagen NC1

Sites

Metal binding11871Calcium By similarity
Metal binding11891Calcium By similarity
Metal binding11901Calcium; via carbonyl oxygen By similarity
Metal binding11921Calcium; via carbonyl oxygen By similarity
Metal binding11951Calcium By similarity

Amino acid modifications

Modified residue861Pyrrolidone carboxylic acid By similarity
Modified residue901Allysine By similarity
Glycosylation12731N-linked (GlcNAc...) Potential
Disulfide bond1169 ↔ 1201 By similarity
Disulfide bond1209 ↔ 1370 By similarity
Disulfide bond1278 ↔ 1323 By similarity

Experimental info

Sequence conflict151V → A in AAA37331. Ref.4
Sequence conflict11671R → TT in CAA41205. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q01149 [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: 0D17DF5D6C1452D1

FASTA1,372129,557
        10         20         30         40         50         60 
MLSFVDTRTL LLLAVTSCLA TCQYLQSGSV RKGPTGDRGP RGQRGPAGPR GRDGVDGPMG 

        70         80         90        100        110        120 
PPGPPGSPGP PGSPAPPGLT GNFAAQYSDK GVSSGPGPMG LMGPRGPPGA VGAPGPQGFQ 

       130        140        150        160        170        180 
GPAGEPGEPG QTGPAGPRGP AGSPGKAGED GHPGKPGRPG ERGVVGPQGA RGFPGTPGLP 

       190        200        210        220        230        240 
GFKGVKGHSG MDGLKGQPGA QGVKGEPGAP GENGTPGQAG ARGLPGERGR VGAPGPAGAR 

       250        260        270        280        290        300 
GSDGSVGPVG PAGPIGSAGP PGFPGAPGPK GELGPVGNPG PAGPAGPRGE VGLPGLSGPV 

       310        320        330        340        350        360 
GPPGNPGTNG LTGAKGATGL PGVAGAPGLP GPRGIPGPAG AAGATGARGL VGEPGPAGSK 

       370        380        390        400        410        420 
GESGNKGEPG SVGAQGPPGP SGEEGKRGSP GEAGSAGPAG PPGLRGSPGS RGLPGADGRA 

       430        440        450        460        470        480 
GVMGPPGNRG STGPAGIRGP NGDAGRPGEP GLMGPRGLPG SPGNVGPSGK EGPVGLPGID 

       490        500        510        520        530        540 
GRPGPIGPAG PRGEAGNIGF PGPKGPSGDP GKPGERGHPG LAGARGAPGP DGNNGAQGPP 

       550        560        570        580        590        600 
GPQGVQGGKG EQGPAGPPGF QGLPGPSGTT GEVGKPGERG LPGEFGLPGP AGPRGERGTP 

       610        620        630        640        650        660 
GESGAAGPSG PIGSRGPSGA PGPDGNKGEA GAVGAPGSAG ASGPGGLPGE RGAAGIPGGK 

       670        680        690        700        710        720 
GEKGETGLRG DTGNTGRDGA RGIPGAVGAP GPAGASGDRG EAGAAGPSGP AGPRGSPGER 

       730        740        750        760        770        780 
GEVGPAGPNG FAGPAGAAGQ PGAKGEKGTK GPKGENGIVG PTGSVGAAGP SGPNGPPGPV 

       790        800        810        820        830        840 
GSRGDGGPPG MTGFPGAAGR TGPPGPSGIA GPPGPPGAAG KEGIRGPRGD QGPVGRTGET 

       850        860        870        880        890        900 
GASGPPGFVG EKGPSGEPGT AGAPGTAGPQ GLLGAPGILG LPGSRGERGL PGIAGALGEP 

       910        920        930        940        950        960 
GPLGISGPPG ARGPPGAVGS PGVNGAPGEA GRDGNPGSDG PPGRDGQPGH KGERGYPGSI 

       970        980        990       1000       1010       1020 
GPTGAAGAPG PHGSVGPAGK HGNRGEPGPA GSVGPVGAVG PRGPSGPQGI RGDKGEPGDK 

      1030       1040       1050       1060       1070       1080 
GHRGLPGLKG YSGLQGLPGL AGLHGDQGAP GPVGPAGPRG PAGPSGPVGK DGRSGQPGPV 

      1090       1100       1110       1120       1130       1140 
GPAGVRGSQG SQGPAGPPGP PGPPGPPGVS GGGYDFGFEG DFYRADQPRS QPSLRPKDYE 

      1150       1160       1170       1180       1190       1200 
VDATLKSLNN QIETLLTPEG SRKNPARTCR DLRLSHPEWN SDYYWIDPNQ GCTMDAIKVY 

      1210       1220       1230       1240       1250       1260 
CDFSTGETCI QAQPVNTPAK NSYSRAQANK HVWLGETING GSQFEYNVEG VSSKEMATQL 

      1270       1280       1290       1300       1310       1320 
AFMRLLANRA SQNITYHCKN SIAYLDEETG SLNKAVLLQG SNDVELVAEG NSRFTYSVLV 

      1330       1340       1350       1360       1370 
DGCSKKTNEW GKTIIEYKTN KPSRLPFLDI APLDIGGADQ EFRVEVGPVC FK

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X58251 mRNA. Translation: CAA41205.1.
BC007158 mRNA. Translation: AAH07158.1.
BC042503 mRNA. Translation: AAH42503.2.
K01832 Genomic DNA. Translation: AAA37331.1.
IPIIPI00222188.
PIRA43291.
RefSeqNP_031769.2. NM_007743.2.
UniGeneMm.277792.

3D structure databases

ProteinModelPortalQ01149.
SMRQ01149. Positions 1158-1371.
ModBaseSearch...

PTM databases

PhosphoSiteQ01149.

Proteomic databases

PaxDbQ01149.
PRIDEQ01149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031668; ENSMUSP00000031668; ENSMUSG00000029661.
GeneID12843.
KEGGmmu:12843.

Organism-specific databases

CTD1278.
MGIMGI:88468. Col1a2.

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085654.
HOVERGENHBG004933.
InParanoidQ01149.
KOK06236.
OMATGPIGSA.
OrthoDBEOG412M65.

Gene expression databases

ArrayExpressQ01149.
BgeeQ01149.
CleanExMM_COL1A2.
GenevestigatorQ01149.
GermOnlineENSMUSG00000029661. Mus musculus.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL1A2. mouse.
NextBio282380.
SOURCESearch...

Entry information

Entry nameCO1A2_MOUSE
AccessionPrimary (citable) accession number: Q01149
Secondary accession number(s): Q8CGA5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: August 29, 2001
Last modified: May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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