CCDC9_MOUSE
ID CCDC9_MOUSE Reviewed; 543 AA.
AC Q8VC31;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Coiled-coil domain-containing protein 9;
GN Name=Ccdc9;
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 [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 [2]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-106; ARG-120; ARG-126 AND
RP ARG-128, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probable component of the exon junction complex (EJC), a
CC multiprotein complex that associates immediately upstream of the exon-
CC exon junction on mRNAs and serves as a positional landmark for the
CC intron exon structure of genes and directs post-transcriptional
CC processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA
CC decay (NMD) or translation. {ECO:0000250|UniProtKB:Q9Y3X0}.
CC -!- SUBUNIT: Probable component of the exon junction complex (EJC); the
CC association is RNA-dependent. {ECO:0000250|UniProtKB:Q9Y3X0}.
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DR EMBL; BC021915; AAH21915.1; -; mRNA.
DR CCDS; CCDS39784.2; -.
DR RefSeq; NP_758501.2; NM_172297.1.
DR AlphaFoldDB; Q8VC31; -.
DR SMR; Q8VC31; -.
DR BioGRID; 232567; 44.
DR STRING; 10090.ENSMUSP00000114088; -.
DR iPTMnet; Q8VC31; -.
DR PhosphoSitePlus; Q8VC31; -.
DR EPD; Q8VC31; -.
DR MaxQB; Q8VC31; -.
DR PaxDb; Q8VC31; -.
DR PRIDE; Q8VC31; -.
DR ProteomicsDB; 281421; -.
DR Ensembl; ENSMUST00000041010; ENSMUSP00000035597; ENSMUSG00000041375.
DR GeneID; 243846; -.
DR KEGG; mmu:243846; -.
DR CTD; 26093; -.
DR MGI; MGI:1921443; Ccdc9.
DR eggNOG; ENOG502QUM9; Eukaryota.
DR GeneTree; ENSGT00530000063950; -.
DR InParanoid; Q8VC31; -.
DR OrthoDB; 602532at2759; -.
DR BioGRID-ORCS; 243846; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ccdc9; mouse.
DR PRO; PR:Q8VC31; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VC31; protein.
DR GO; GO:0035145; C:exon-exon junction complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR InterPro; IPR029336; DUF4594.
DR PANTHER; PTHR15635; PTHR15635; 1.
DR Pfam; PF15266; DUF4594; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..543
FT /note="Coiled-coil domain-containing protein 9"
FT /id="PRO_0000089404"
FT REGION 38..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 147..183
FT /evidence="ECO:0000255"
FT COILED 422..452
FT /evidence="ECO:0000255"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 106
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 120
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 126
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 128
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 129
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 131
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 133
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3X0"
SQ SEQUENCE 543 AA; 61445 MW; 370D0E337E89E70B CRC64;
MATTLDLKSK EEKDAELDKR IEALRRKNEA LIRRYQEIEE DRKKAELEGV AVTAPRKSRS
MEKENMAVEE KSLGPSRRTP GTPRPPGASR GGRTHPQQGG RAGVGRASQG WEDGAGEQLR
GGPGGRGRRG RGRGSPHLLG AGDNSTSDRK SKEWEERRRQ NIEKMNEEME KIAEYERNQR
EGVLEPNPVR NFLDDPRRRG GPLEESERDR REGSRRHGRN WGGSDFERVR SGLEQERQGR
RAGLGSGGDM TMSMTGRERS EYLRWKQERE KIDQERLQRH RKPTGQWRRE WDAEKTDGMF
KDGPAPTHEL SHRYDDQAWA RPPKPPTFGE FLSQHKAEVS SRRRRKNSRP QAKVAPRAYS
DHDNRWETRE EAVSSAPESS QSISLEETPT QASETPAPAH RPPEEDGEED VGEEEEGEEE
GEDEEDEEWE DVSEDVTEEE EEEEEEFEED EEGPKDQEAA TVPDHQPEAE PAGKPTCEQV
DPVPAGSQEL LSPVPVEPPI PFSPSEDHQP VSDWGEEMEL NSPGTAHLPG THSSGEAWPF
ANA
