CEP63_RAT
ID CEP63_RAT Reviewed; 538 AA.
AC Q4KLY0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Centrosomal protein of 63 kDa {ECO:0000305};
DE Short=Cep63;
GN Name=Cep63 {ECO:0000312|RGD:1561183};
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Kidney;
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).
CC -!- FUNCTION: Required for normal spindle assembly. Plays a key role in
CC mother-centriole-dependent centriole duplication; the function seems
CC also to involve CEP152, CDK5RAP2 and WDR62 through a stepwise assembled
CC complex at the centrosome that recruits CDK2 required for centriole
CC duplication. Also recruits CDK1 to centrosomes (By similarity). Plays a
CC role in DNA damage response. Following DNA damage, such as double-
CC strand breaks (DSBs), is removed from centrosomes; this leads to the
CC inactivation of spindle assembly and delay in mitotic progression (By
CC similarity). {ECO:0000250|UniProtKB:Q96MT8}.
CC -!- SUBUNIT: Interacts with CEP152 and CDK1; these interactions recruit
CC both ligands to centrosomes. Interacts with CDK2, CDK5RAP2, WDR62,
CC CEP90, KIAA0753/moonraker an CCDC14. CEP63, CDK5RAP2, CEP152, WDR62 are
CC proposed to form a stepwise assdembled complex at the centrosome
CC forming a ring near parental centrioles. Interacts with CCDC57; the
CC interaction is required for their location to proximal end of
CC centrioles (By similarity). {ECO:0000250|UniProtKB:Q96MT8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q3UPP8,
CC ECO:0000250|UniProtKB:Q96MT8}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q3UPP8,
CC ECO:0000250|UniProtKB:Q96MT8}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q96MT8}. Note=Colocalizes with CDK5RAP2, CEP152
CC and WDR62 in a discrete ring around the proximal end of the parental
CC centriole. At this site, a cohesive structure is predicted to engage
CC parental centrioles and procentrioles (By similarity).
CC {ECO:0000250|UniProtKB:Q3UPP8, ECO:0000250|UniProtKB:Q96MT8}.
CC -!- SIMILARITY: Belongs to the CEP63 family. {ECO:0000305}.
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DR EMBL; CH473954; EDL77401.1; -; Genomic_DNA.
DR EMBL; BC098948; AAH98948.1; -; mRNA.
DR EMBL; BC161815; AAI61815.1; -; mRNA.
DR RefSeq; NP_001032861.2; NM_001037772.1.
DR RefSeq; NP_001231734.1; NM_001244805.1.
DR AlphaFoldDB; Q4KLY0; -.
DR SMR; Q4KLY0; -.
DR STRING; 10116.ENSRNOP00000053371; -.
DR PaxDb; Q4KLY0; -.
DR GeneID; 300963; -.
DR KEGG; rno:300963; -.
DR UCSC; RGD:1561183; rat.
DR CTD; 80254; -.
DR RGD; 1561183; Cep63.
DR VEuPathDB; HostDB:ENSRNOG00000008410; -.
DR eggNOG; ENOG502QRYU; Eukaryota.
DR HOGENOM; CLU_027471_0_0_1; -.
DR InParanoid; Q4KLY0; -.
DR OrthoDB; 943593at2759; -.
DR PhylomeDB; Q4KLY0; -.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR PRO; PR:Q4KLY0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000008410; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q4KLY0; baseline and differential.
DR Genevisible; Q4KLY0; RN.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:0051298; P:centrosome duplication; ISO:RGD.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0045141; P:meiotic telomere clustering; ISO:RGD.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:RGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISO:RGD.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
DR InterPro; IPR029608; Cep63.
DR InterPro; IPR031470; Cep63/Deup1_N.
DR PANTHER; PTHR18875:SF7; PTHR18875:SF7; 2.
DR Pfam; PF17045; CEP63; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; DNA damage; Mitosis; Reference proteome.
FT CHAIN 1..538
FT /note="Centrosomal protein of 63 kDa"
FT /id="PRO_0000381806"
FT COILED 73..283
FT /evidence="ECO:0000255"
FT COILED 343..486
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96MT8"
SQ SEQUENCE 538 AA; 62680 MW; DDE750F775888D1D CRC64;
MEALLEGIQT RGHSGGFLTS CEAELQELMK QIDIMVAHKK SEWEGQTHAL ETCLDMRDRE
LKALRSQLDM KHKEVGILHQ QIEEQEKTKQ EMALEYKEEL MKLQEELSRL KRSYEKLQKK
QLREFRGNTK SLREDRSEIE RLTGKIEEFR QKSLDWEKQR LIYQQQVSSL EAQRKALAEQ
SEIIQAQLAN RKQKLESVEL SSQSEIQHLS SKLERAKDTI CANELEIERL NIRVKDLMGT
NVTILQEQRQ KEEKLRESEK LLEALQEEQK ELKASLQAQE SFILDAKMQE KLQTKLKAVD
TKHSVERSLE DCQVERKYSS SGQGVLDNVL SQLDISHSSE ELLQAEVTRL EGSLESVSTT
CKQLSQELME KYEELKRMEG HNNEYRTEIK KLKEQILQAD QTYSSALEGM KTEISQLTRE
LHQRDITIAS AKCSSSDMER QLKAEMQKAE EKAVEHKEIL SQLESLRLEN RRLSETVMKL
ELGLHECSMP VSPLGLIATR FLEEEELRSH HILERLDAHI EELKRESEKT VRQFTALV
