CO1A2_MOUSE
ID CO1A2_MOUSE Reviewed; 1372 AA.
AC Q01149; Q8CGA5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Collagen alpha-2(I) chain;
DE AltName: Full=Alpha-2 type I collagen;
DE Flags: Precursor;
GN Name=Col1a2; Synonyms=Cola2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Calvaria;
RX PubMed=1505972; DOI=10.1016/0888-7543(92)90065-z;
RA Phillips C.L., Morgan A.L., Lever L.W., Wenstrup R.J.;
RT "Sequence analysis of a full-length cDNA for the murine pro alpha 2(I)
RT collagen chain: comparison of the derived primary structure with human pro
RT alpha 2(I) collagen.";
RL Genomics 13:1345-1346(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-110.
RC TISSUE=Calvaria;
RX PubMed=1748823; DOI=10.1111/1523-1747.ep12491894;
RA Phillips C.L., Lever L.W., Pinnell S.R., Quarles L.D., Wenstrup R.J.;
RT "Construction of a full-length murine pro alpha 2(I) collagen cDNA by the
RT polymerase chain reaction.";
RL J. Invest. Dermatol. 97:980-984(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX PubMed=3039494; DOI=10.1073/pnas.84.16.5590;
RA Rossi P., de Crombrugghe B.;
RT "Identification of a cell-specific transcriptional enhancer in the first
RT intron of the mouse alpha 2 (type I) collagen gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5590-5594(1987).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen).
CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones.
CC In bones the fibrils are mineralized with calcium hydroxyapatite.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function. {ECO:0000250}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; X58251; CAA41205.1; -; mRNA.
DR EMBL; BC007158; AAH07158.1; -; mRNA.
DR EMBL; BC042503; AAH42503.2; -; mRNA.
DR EMBL; K01832; AAA37331.1; -; Genomic_DNA.
DR CCDS; CCDS39420.1; -.
DR PIR; A43291; A43291.
DR RefSeq; NP_031769.2; NM_007743.3.
DR AlphaFoldDB; Q01149; -.
DR SMR; Q01149; -.
DR BioGRID; 198832; 12.
DR ComplexPortal; CPX-2956; Collagen type I trimer.
DR STRING; 10090.ENSMUSP00000031668; -.
DR GlyGen; Q01149; 2 sites.
DR iPTMnet; Q01149; -.
DR PhosphoSitePlus; Q01149; -.
DR CPTAC; non-CPTAC-3310; -.
DR jPOST; Q01149; -.
DR PaxDb; Q01149; -.
DR PeptideAtlas; Q01149; -.
DR PRIDE; Q01149; -.
DR ProteomicsDB; 279128; -.
DR Antibodypedia; 15754; 448 antibodies from 35 providers.
DR DNASU; 12843; -.
DR Ensembl; ENSMUST00000031668; ENSMUSP00000031668; ENSMUSG00000029661.
DR GeneID; 12843; -.
DR KEGG; mmu:12843; -.
DR UCSC; uc009avm.1; mouse.
DR CTD; 1278; -.
DR MGI; MGI:88468; Col1a2.
DR VEuPathDB; HostDB:ENSMUSG00000029661; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155639; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; Q01149; -.
DR OMA; SFYWIDP; -.
DR OrthoDB; 1406711at2759; -.
DR PhylomeDB; Q01149; -.
DR TreeFam; TF344135; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474244; Extracellular matrix organization.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2214320; Anchoring fibril formation.
DR Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
DR Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-MMU-76009; Platelet Aggregation (Plug Formation).
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12843; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Col1a2; mouse.
DR PRO; PR:Q01149; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q01149; protein.
DR Bgee; ENSMUSG00000029661; Expressed in vault of skull and 264 other tissues.
DR ExpressionAtlas; Q01149; baseline and differential.
DR Genevisible; Q01149; MM.
DR GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR GO; GO:0005584; C:collagen type I trimer; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; IPI:MGI.
DR GO; GO:0001568; P:blood vessel development; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0030199; P:collagen fibril organization; ISO:MGI.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0085029; P:extracellular matrix assembly; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0070208; P:protein heterotrimerization; IDA:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; ISO:MGI.
DR GO; GO:0043589; P:skin morphogenesis; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 6.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Metal-binding; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P02466"
FT PROPEP 23..85
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005807"
FT CHAIN 86..1125
FT /note="Collagen alpha-2(I) chain"
FT /id="PRO_0000005808"
FT PROPEP 1126..1372
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005809"
FT DOMAIN 1139..1372
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 28..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 90
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 183
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 183
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 1273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1169..1201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1209..1370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1278..1323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 15
FT /note="V -> A (in Ref. 4; AAA37331)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="R -> TT (in Ref. 1; CAA41205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1372 AA; 129557 MW; 0D17DF5D6C1452D1 CRC64;
MLSFVDTRTL LLLAVTSCLA TCQYLQSGSV RKGPTGDRGP RGQRGPAGPR GRDGVDGPMG
PPGPPGSPGP PGSPAPPGLT GNFAAQYSDK GVSSGPGPMG LMGPRGPPGA VGAPGPQGFQ
GPAGEPGEPG QTGPAGPRGP AGSPGKAGED GHPGKPGRPG ERGVVGPQGA RGFPGTPGLP
GFKGVKGHSG MDGLKGQPGA QGVKGEPGAP GENGTPGQAG ARGLPGERGR VGAPGPAGAR
GSDGSVGPVG PAGPIGSAGP PGFPGAPGPK GELGPVGNPG PAGPAGPRGE VGLPGLSGPV
GPPGNPGTNG LTGAKGATGL PGVAGAPGLP GPRGIPGPAG AAGATGARGL VGEPGPAGSK
GESGNKGEPG SVGAQGPPGP SGEEGKRGSP GEAGSAGPAG PPGLRGSPGS RGLPGADGRA
GVMGPPGNRG STGPAGIRGP NGDAGRPGEP GLMGPRGLPG SPGNVGPSGK EGPVGLPGID
GRPGPIGPAG PRGEAGNIGF PGPKGPSGDP GKPGERGHPG LAGARGAPGP DGNNGAQGPP
GPQGVQGGKG EQGPAGPPGF QGLPGPSGTT GEVGKPGERG LPGEFGLPGP AGPRGERGTP
GESGAAGPSG PIGSRGPSGA PGPDGNKGEA GAVGAPGSAG ASGPGGLPGE RGAAGIPGGK
GEKGETGLRG DTGNTGRDGA RGIPGAVGAP GPAGASGDRG EAGAAGPSGP AGPRGSPGER
GEVGPAGPNG FAGPAGAAGQ PGAKGEKGTK GPKGENGIVG PTGSVGAAGP SGPNGPPGPV
GSRGDGGPPG MTGFPGAAGR TGPPGPSGIA GPPGPPGAAG KEGIRGPRGD QGPVGRTGET
GASGPPGFVG EKGPSGEPGT AGAPGTAGPQ GLLGAPGILG LPGSRGERGL PGIAGALGEP
GPLGISGPPG ARGPPGAVGS PGVNGAPGEA GRDGNPGSDG PPGRDGQPGH KGERGYPGSI
GPTGAAGAPG PHGSVGPAGK HGNRGEPGPA GSVGPVGAVG PRGPSGPQGI RGDKGEPGDK
GHRGLPGLKG YSGLQGLPGL AGLHGDQGAP GPVGPAGPRG PAGPSGPVGK DGRSGQPGPV
GPAGVRGSQG SQGPAGPPGP PGPPGPPGVS GGGYDFGFEG DFYRADQPRS QPSLRPKDYE
VDATLKSLNN QIETLLTPEG SRKNPARTCR DLRLSHPEWN SDYYWIDPNQ GCTMDAIKVY
CDFSTGETCI QAQPVNTPAK NSYSRAQANK HVWLGETING GSQFEYNVEG VSSKEMATQL
AFMRLLANRA SQNITYHCKN SIAYLDEETG SLNKAVLLQG SNDVELVAEG NSRFTYSVLV
DGCSKKTNEW GKTIIEYKTN KPSRLPFLDI APLDIGGADQ EFRVEVGPVC FK
