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CO9A2_MOUSE
ID   CO9A2_MOUSE             Reviewed;         688 AA.
AC   Q07643;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Collagen alpha-2(IX) chain;
DE   Flags: Precursor;
GN   Name=Col9a2;
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 [GENOMIC DNA].
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=8106484; DOI=10.1016/s0021-9258(17)37655-x;
RA   Perala M., Elima K., Metsaranta M., Rosati R., de Crombrugghe B.,
RA   Vuorio E.;
RT   "The exon structure of the mouse alpha 2(IX) collagen gene shows unexpected
RT   divergence from the chick gene.";
RL   J. Biol. Chem. 269:5064-5071(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 521-668.
RC   STRAIN=C57BL/6J;
RX   PubMed=1543751; DOI=10.1016/0167-4781(92)90465-c;
RA   Elima K., Metsaeranta M., Kallio J., Peraelae M., Eerola I., Garofalo S.,
RA   de Crombrugghe B., Vuorio E.;
RT   "Specific hybridization probes for mouse alpha 2(IX) and alpha 1(X)
RT   collagen mRNAs.";
RL   Biochim. Biophys. Acta 1130:78-80(1992).
CC   -!- FUNCTION: Structural component of hyaline cartilage and vitreous of the
CC       eye.
CC   -!- SUBUNIT: Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha
CC       3(IX) chain (By similarity). The chains are linked to each other by
CC       interchain disulfide bonds (By similarity). Trimers are also cross-
CC       linked via hydroxylysines (By similarity).
CC       {ECO:0000250|UniProtKB:C0HLN2}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- PTM: Covalently linked to the telopeptides of type II collagen by
CC       lysine-derived cross-links.
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 fibril-associated collagens with interrupted
CC       helices (FACIT) family. {ECO:0000305}.
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DR   EMBL; Z22923; CAA80503.1; -; Genomic_DNA.
DR   EMBL; X63014; CAA44742.1; -; mRNA.
DR   CCDS; CCDS18599.1; -.
DR   PIR; A53330; A53330.
DR   AlphaFoldDB; Q07643; -.
DR   SMR; Q07643; -.
DR   ComplexPortal; CPX-2970; Collagen type IX trimer.
DR   STRING; 10090.ENSMUSP00000030372; -.
DR   GlyGen; Q07643; 2 sites.
DR   PhosphoSitePlus; Q07643; -.
DR   MaxQB; Q07643; -.
DR   PaxDb; Q07643; -.
DR   PRIDE; Q07643; -.
DR   ProteomicsDB; 283550; -.
DR   MGI; MGI:88466; Col9a2.
DR   eggNOG; KOG3544; Eukaryota.
DR   InParanoid; Q07643; -.
DR   PhylomeDB; Q07643; -.
DR   Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-MMU-186797; Signaling by PDGF.
DR   Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   Reactome; R-MMU-419037; NCAM1 interactions.
DR   Reactome; R-MMU-8948216; Collagen chain trimerization.
DR   ChiTaRS; Col9a2; mouse.
DR   PRO; PR:Q07643; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q07643; protein.
DR   GO; GO:0005594; C:collagen type IX trimer; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01391; Collagen; 6.
PE   2: Evidence at transcript level;
KW   Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Hydroxylation; Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..688
FT                   /note="Collagen alpha-2(IX) chain"
FT                   /id="PRO_0000005838"
FT   REGION          25..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          26..162
FT                   /note="Triple-helical region 4 (COL4)"
FT   REGION          163..179
FT                   /note="Nonhelical region 4 (NC4)"
FT   REGION          180..518
FT                   /note="Triple-helical region 3 (COL3)"
FT   REGION          183..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..548
FT                   /note="Nonhelical region 3 (NC3)"
FT   REGION          549..631
FT                   /note="Triple-helical region 2 (COL2)"
FT   REGION          553..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..633
FT                   /note="Nonhelical region 2 (NC2)"
FT   REGION          634..663
FT                   /note="Triple-helical region 1 (COL1)"
FT   REGION          664..688
FT                   /note="Nonhelical region 1 (NC1)"
FT   COMPBIAS        27..43
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..130
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..157
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..570
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         159
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P12108"
FT   MOD_RES         182
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:P12108"
FT   CARBOHYD        168
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P12108"
FT   CARBOHYD        182
FT                   /note="O-linked (Gal...) hydroxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:P12108"
FT   DISULFID        173
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   DISULFID        177
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   VARIANT         525
FT                   /note="V -> M (in strain: C57BL/6)"
FT   VARIANT         610
FT                   /note="H -> R (in strain: C57BL/6)"
FT   VARIANT         666
FT                   /note="A -> G (in strain: C57BL/6)"
SQ   SEQUENCE   688 AA;  65321 MW;  7C7A73D2CD2A039F CRC64;
     MTAVPAPRSL FVLLQVLWLA LAQIRGPPGE PGPPGPPGPP GVPGSDGIDG DKGPPGKVGP
     PGSKGEPGKP GPDGPDGKPG IDGLMGAKGE PGPVGTPGVK GQPGLPGPPG LPGPGFAGPP
     GPPGPVGLPG EIGTPGPKGD PGPEGPSGPP GPPGKPGRPG TIQGLEGSAD FLCPTNCPAG
     VKGPQGLQGV KGHPGKRGIL GDPGRQGKPG PKGDVGASGE QGIPGPPGPQ GIRGYPGMAG
     PKGEMGPRGY KGMVGSIGAA GPPGEEGPRG PPGEAGEKGD VGSQGARGPQ GITGPKGITG
     PPGIDGKDGT PGIPGMKGSA GQVGRPGSPG HQGLAGVPGQ PGTKGGPGDK GEPGQQGLPG
     VSGPPGKEGE PGPRGEIGPQ GIMGQKGDQG ERGPVGQPGP QGRQGPKGEQ GPPGIPGPQG
     LPGIKGDKGS PGKTGPRGGV GDPGVAGLPG EKGEKGQSGE PGLKGQQGVR GETGYPGPSG
     DIGAPGVQGY PGLPGPRGLV GDRGVPGQPG RQGVVGRAAS DQHIVDVVLK MIQEQLAEVA
     VSAKREALGA AGMVGLPGPP GPPGYPGKQG PNGHPGPRGI PGIVGAVGQI GNTGPKGKRG
     EKGDRGEMGH GHPGMPGPPG IPGLPGRPGQ AINGKDGDRG SPGAPGEAGR PGRPGPVGLP
     GFCEPAACLG ASAYTSARLT EPGSIKGP
 
 
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