CCDC8_RAT
ID CCDC8_RAT Reviewed; 643 AA.
AC P62521; Q6P9Z5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Coiled-coil domain-containing protein 8;
GN Name=Ccdc8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC060520; AAH60520.1; -; mRNA.
DR RefSeq; NP_001009533.2; NM_001009533.2.
DR AlphaFoldDB; P62521; -.
DR iPTMnet; P62521; -.
DR PhosphoSitePlus; P62521; -.
DR PRIDE; P62521; -.
DR GeneID; 494320; -.
DR KEGG; rno:494320; -.
DR UCSC; RGD:1359717; rat.
DR CTD; 83987; -.
DR RGD; 1359717; Ccdc8.
DR InParanoid; P62521; -.
DR OrthoDB; 1181293at2759; -.
DR PhylomeDB; P62521; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR PRO; PR:P62521; -.
DR Proteomes; UP000002494; Unplaced.
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: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..643
FT /note="Coiled-coil domain-containing protein 8"
FT /id="PRO_0000089402"
FT REGION 93..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 603..609
FT /note="PxLPxI/L motif; mediates interaction with ANKRA2"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W5"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W5"
SQ SEQUENCE 643 AA; 69589 MW; 0028464DAE8E9632 CRC64;
MLQIGEDVDY LLIPREVRLA GGVWRVISKP ATKEAVFRER LIQFLQEEGR TLEDVARIIE
KSTPHPPQPP KKAKVPRVRR VPQMVTPPLR LVVGTYDSSN GSDSELSDFD TSKVKGNRGS
GKTRKVRKMP VSYLGSKFLG SDESEDDQEL VEAFLRRGEK KPSAPPPRRR VNLPVPMFEN
NLGPQPSKGD RWREYVSQVS WGKLKQRVRG WAPRSGSEVG QAQQSSIAER AGEMRHSHTS
PDLDDSSRNT GDLSDQTLIT RRWKPKIKWV SLRRCRKEQV PPLAHGTAEE PPEAAENQGA
GAAAEHGVEA AASQRPEAAA SPRAEAAANP RAEATANPRA EAAANPRAEA AASPRAEAAA
NPRAEAAANP RAEATANPRA EAAANPRAEA TANPRAEAAV NPRTEAAVNP RTEAAANPRA
EAAVNPRAEA TASPRAEAEV NQKTEATASP RAETAASPRV EAAASLRVEA AASPRAEATV
SPRAEAVATP RAETAASARV EAAANLRAGV LPDQRAEAID SQRAEGPVNQ STGATENQRV
EVLADQRAGV LHDQREEAGP QAILEASADS GSRARKQVKT VRFQTPGRFS WFHMRRKAFW
HTPRLPTLPK RGPRAGAGEA RSLRVLRADT RADMEHREQE EQL
