CCDC8_MOUSE
ID CCDC8_MOUSE Reviewed; 685 AA.
AC D3YZV8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Coiled-coil domain-containing protein 8 homolog;
GN Name=Ccdc8;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, and Spleen;
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: Core component of the 3M complex, a complex required to
CC regulate microtubule dynamics and genome integrity. It is unclear how
CC the 3M complex regulates microtubules, it could act by controlling the
CC level of a microtubule stabilizer. Required for localization of CUL7 to
CC the centrosome. {ECO:0000250|UniProtKB:Q9H0W5}.
CC -!- SUBUNIT: Component of the 3M complex, composed of core components CUL7,
CC CCDC8 and OBSL1. Interacts (via PxLPxI/L motif) with ANKRA2 (via
CC ankyrin repeats); may link the 3M complex to histone deacetylases
CC including HDAC4 and HDAC5. {ECO:0000250|UniProtKB:Q9H0W5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H0W5}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9H0W5}.
CC -!- DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of
CC ANKRA2. {ECO:0000250|UniProtKB:Q9H0W5}.
CC -!- MISCELLANEOUS: Despite its name, does not contain a coiled coil domain.
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DR EMBL; AC148976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466654; EDL42062.1; -; Genomic_DNA.
DR CCDS; CCDS52044.1; -.
DR RefSeq; NP_001095005.1; NM_001101535.1.
DR AlphaFoldDB; D3YZV8; -.
DR BioGRID; 241620; 1.
DR STRING; 10090.ENSMUSP00000092399; -.
DR iPTMnet; D3YZV8; -.
DR PhosphoSitePlus; D3YZV8; -.
DR jPOST; D3YZV8; -.
DR MaxQB; D3YZV8; -.
DR PaxDb; D3YZV8; -.
DR PeptideAtlas; D3YZV8; -.
DR PRIDE; D3YZV8; -.
DR ProteomicsDB; 265606; -.
DR Antibodypedia; 31453; 152 antibodies from 23 providers.
DR Ensembl; ENSMUST00000094805; ENSMUSP00000092399; ENSMUSG00000041117.
DR GeneID; 434130; -.
DR KEGG; mmu:434130; -.
DR UCSC; uc012fak.1; mouse.
DR CTD; 83987; -.
DR MGI; MGI:3612184; Ccdc8.
DR VEuPathDB; HostDB:ENSMUSG00000041117; -.
DR eggNOG; ENOG502S9UD; Eukaryota.
DR GeneTree; ENSGT01030000234522; -.
DR HOGENOM; CLU_025577_0_0_1; -.
DR InParanoid; D3YZV8; -.
DR OMA; RRVFWHT; -.
DR OrthoDB; 1181293at2759; -.
DR PhylomeDB; D3YZV8; -.
DR TreeFam; TF335054; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 434130; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ccdc8; mouse.
DR PRO; PR:D3YZV8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; D3YZV8; protein.
DR Bgee; ENSMUSG00000041117; Expressed in humerus cartilage element and 133 other tissues.
DR Genevisible; D3YZV8; MM.
DR GO; GO:1990393; C:3M complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR InterPro; IPR026523; PNMA.
DR Pfam; PF14893; PNMA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..685
FT /note="Coiled-coil domain-containing protein 8 homolog"
FT /id="PRO_0000415807"
FT REGION 93..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 647..653
FT /note="PxLPxI/L motif; mediates interaction with ANKRA2"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W5"
FT COMPBIAS 93..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W5"
SQ SEQUENCE 685 AA; 73938 MW; 72CBA6C436127E02 CRC64;
MLQIGEDVDY LLIPREVRLA GGVWRVISKP ATKEAEFRER LIQFLQEEGR TLEDVARIIE
KSTPHPPQPR KRTKELRVRR VPQMVTPPLR LVVGTYDSSN GSDSELSDFD TSKVKGNRSS
SGRTRKVRKM PVSYLGSKFL GSDVESEDDQ ELVEAFLRRG EKPSAPPPRR RVNLPVPMFE
NNLGPQPSKA DRWREYVSQV SWGKLKQRVK GWAPRSGSEV GQTQQASTAA ERAGEMRHSQ
ASSDDDSSRN TGDRSDQMLG TRRWKPKIKW VSLRRCRKEQ VPPFAQGTGM PAEEHPEAAE
NQGAEAAANQ RAEPLASPRA EAAASPRAET AADPRVEAVA SPRAEAAASP RAEAVADPRA
EAAASPRAEA AASPRTEAAA SLRAEAVASP RAEAAASPRA EAAADPRAEA AASPIAEAAA
NQKAELVDSP RAETAADPRA EAAASPRAEA VADPRVEAAA SPIAEAAANQ KAELVDSPRA
ETAADPRAEA AASPRAEAAA DPRAEVAASP RAEAAASPRA EAEASPRAEA AASPKAEAEA
NLRVEAAAYL RAGVPPDQRA EAIDSQRAEG PANQRTGATE NQRVEVLADQ RAGVLHDQRE
EAGPQGIQEA SAGSGSRAQK QVKTVRFQTP GRFSWFRMRR RVFWHTPRLP TLPRRVPRAG
EARSLRVLRA DIRADVEHRE QEEQL
