ID   A2ACT7_MOUSE            Unreviewed;       680 AA.
AC   A2ACT7;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   SubName: Full=Collagen, type IX, alpha 3 {ECO:0000313|Ensembl:ENSMUSP00000128718.2};
GN   Name=Col9a3 {ECO:0000313|Ensembl:ENSMUSP00000128718.2,
GN   ECO:0000313|MGI:MGI:894686};
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 {ECO:0000313|Ensembl:ENSMUSP00000128718.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000128718.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000128718.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000128718.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000128718.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; NP_034066.2; NM_009936.2.
DR   ComplexPortal; CPX-2970; Collagen type IX trimer.
DR   STRING; 10090.ENSMUSP00000128718; -.
DR   PaxDb; 10090-ENSMUSP00000128718; -.
DR   ProteomicsDB; 342670; -.
DR   DNASU; 12841; -.
DR   Ensembl; ENSMUST00000103059.2; ENSMUSP00000099348.2; ENSMUSG00000027570.16.
DR   Ensembl; ENSMUST00000132527.9; ENSMUSP00000128718.2; ENSMUSG00000027570.16.
DR   GeneID; 12841; -.
DR   UCSC; uc008ojl.1; mouse.
DR   AGR; MGI:894686; -.
DR   CTD; 1299; -.
DR   MGI; MGI:894686; Col9a3.
DR   VEuPathDB; HostDB:ENSMUSG00000027570; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000161930; -.
DR   HOGENOM; CLU_001074_18_2_1; -.
DR   OMA; MINEQIA; -.
DR   OrthoDB; 5363474at2759; -.
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   BioGRID-ORCS; 12841; 6 hits in 79 CRISPR screens.
DR   ChiTaRS; Col9a3; mouse.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000027570; Expressed in humerus cartilage element and 244 other cell types or tissues.
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:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0008585; P:female gonad development; IEP:UniProtKB.
DR   GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR37456:SF5; -; 1.
DR   PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR   Pfam; PF01391; Collagen; 6.
PE   1: Evidence at protein level;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Proteomics identification {ECO:0007829|MaxQB:A2ACT7,
KW   ECO:0007829|ProteomicsDB:A2ACT7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..680
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015086012"
FT   REGION          20..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..159
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..186
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..570
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   680 AA;  63475 MW;  E898FA049A4D9D2E CRC64;
     MTGAPALALL LLGQLLTATS AQKVGPRGPP GPQGPPGKPG KDGIDGEAGP PGLPGLPGPK
     GTSGKPGKPG EAGLPGLPGV DGLTGRDGPA GPKGAPGERG SLGPPGPPGL GGKGLPGPPG
     EAGVSGLPGG IGLRGPPGPS GLPGLPGLPG PPGPPGNPGV LPEGATDLQC PAICPPGPPG
     PPGMPGFKGP TGYKGEQGEV GKDGEKGSPG PPGPPGIPGT VGLQGPRGLR GLPGPLGPPG
     DRGPIGFRGP PGTPGAPGKV GDRGERGPEG FRGPKGDLGR PGPKGIPGMA GPGGEPGMPG
     KDGKDGVPGL DGEKGEAGRN GGQGEKGPNG LPGLPGRAGS KGEKGEPGRT GELGEAGPSG
     EPGIPGDVGV PGERGEAGHR GSVGALGPQG PPGAPGIRGF QGQKGSTGDP GLPGPQGLRG
     DVGDRGPGGA TGPKGDQGIA GSDGLPGDKG ELGPNGPVGQ KGESGSRGEL GPKGIQGPNG
     TSGVQGVPGP PGPLGLQGVQ GVPGITGKPG VPGKEASEQR IRELCGGMIS EQIAQLAAHL
     RKPLAPGSIG RPGPAGPPGP PGPPGSIGHP GARGPPGYRG PTGELGDPGP RGSQGDRGDK
     GATGAGLDGP AGDQGYQGPQ GVPGISKDGR DGAHGEPGLP GDPGLPGAAG AQGTPGICDT
     SACQGAVLGG GGEKSGPRSS
//