CE152_XENLA
ID CE152_XENLA Reviewed; 1663 AA.
AC Q498G2;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Centrosomal protein of 152 kDa;
DE Short=Cep152;
GN Name=cep152;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24075808; DOI=10.1016/j.devcel.2013.08.021;
RA Klos Dehring D.A., Vladar E.K., Werner M.E., Mitchell J.W., Hwang P.,
RA Mitchell B.J.;
RT "Deuterosome-mediated centriole biogenesis.";
RL Dev. Cell 27:103-112(2013).
CC -!- FUNCTION: Necessary for centrosome duplication; the function seems also
CC to involve cep63, cdk5rap2 and wdr62 through a stepwise assembled
CC complex at the centrosome that recruits cdk2 required for centriole
CC duplication. Acts as a molecular scaffold facilitating the interaction
CC of plk4 and cenpj, 2 molecules involved in centriole formation (By
CC similarity). Also plays a key role in deuterosome-mediated centriole
CC amplification in multiciliated that can generate more than 100
CC centrioles (PubMed:24075808). Overexpression of cep152 can drive
CC amplification of centrioles (By similarity).
CC {ECO:0000250|UniProtKB:O94986, ECO:0000269|PubMed:24075808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:24075808}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O94986}. Note=Colocalizes with cdk5rap2, wdr62
CC and cep63 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). Localizes to the
CC deuterosome (PubMed:24075808). Localizes to pericentriolar material
CC (PCM) (By similarity). {ECO:0000250|UniProtKB:O94986,
CC ECO:0000269|PubMed:24075808}.
CC -!- SIMILARITY: Belongs to the CEP152 family. {ECO:0000305}.
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DR EMBL; BC100229; AAI00230.1; -; mRNA.
DR RefSeq; NP_001087086.1; NM_001093617.1.
DR AlphaFoldDB; Q498G2; -.
DR SMR; Q498G2; -.
DR GeneID; 446951; -.
DR KEGG; xla:446951; -.
DR CTD; 446951; -.
DR Xenbase; XB-GENE-988613; cep152.L.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 446951; Expressed in egg cell and 11 other tissues.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0098536; C:deuterosome; IDA:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; IDA:UniProtKB.
DR InterPro; IPR029598; Cep152.
DR PANTHER; PTHR10337:SF6; PTHR10337:SF6; 1.
PE 2: Evidence at transcript level;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..1663
FT /note="Centrosomal protein of 152 kDa"
FT /id="PRO_0000424821"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 266..516
FT /evidence="ECO:0000255"
FT COILED 571..664
FT /evidence="ECO:0000255"
FT COILED 696..796
FT /evidence="ECO:0000255"
FT COILED 843..886
FT /evidence="ECO:0000255"
FT COILED 946..977
FT /evidence="ECO:0000255"
FT COILED 1014..1047
FT /evidence="ECO:0000255"
FT COILED 1182..1288
FT /evidence="ECO:0000255"
SQ SEQUENCE 1663 AA; 192175 MW; 937FFE92D2D41CDD CRC64;
MSIDFDSGAL QTQQEDEEYD KEDYAREQEL QQLLTDLPHD MLDDSLSSSP EPSYSDCSGH
EISEKIPQWE HGANWGNDDL PNHQKPYKNG FTENQYCMGF VGKQDEHLRN QAGRDKMSNG
WDVLHANEDD PMFNGKYRYS KDHAYNSESN GQAFHGGDHY DAPGHCSSSE LYHLPDDFQP
YTNCQQVEHF PDSKKEHFQG FAVPEETSKI STEPFQVKYN PYQIKVARMD EMNQDPERRD
GNFDDLQREF LDTGENSTGN MQFVQLQVLY KARGRQLEEQ NNKLEESERQ IRYLNHQLAI
VKDQKDGLTI SLQESQSLLQ NSREMEIQLK GQLTALEKTV ESLTTNEEQL RKELNISKVA
MESFQQQLLD LRRSESIQRA REQHETVVSM LKKKHEEQVL ALQQKLDDVN AMLNEEKELC
SRLETRLKLS ERKEAESKLE KTDIINRLSK SLEESQKQCA NLLQSGSIQE ATQLRLQLQQ
VQSSKIINDG MNKALQEEVR ELQEQITMYE SAARLGAFVN SGEEQQLSDS YVELGIKNFN
WQKSRLGRIV ANNGVKNDLS SEEIILELKT ELERCLNSNK TKRKQIVQLQ AELKGHLLKN
EELKKSMEIA ERTARDSQIQ AENLANKVNN SPFYSSSSDR FREEIQKLQS EKQILQQENE
KHLLFIKEFT VNEEKLKASN QELCNEMRGM IQDFDQDKKE AIERCERTYE QHNEDIKAHL
LNELYEKFES EKELLSQGYE EKITLLQAQM NEIHREMAAV QECYIAVCKE KDALEENMRE
HFKKELQKSE EEVTAKAIQD VEMEWAQKLN QALQDAKTKS LQSFETQTIQ TDESSLAKSD
LNSDCIDELK VKLQNAIQEK EKAVHQAQLE LEERHHEETS KQVEVALTRA YGRWLQELTS
LPEYKARLKL EQEKWEKTNE RNVERQVSDA LYAAEIKWKM RSDKVDFTVR QKEFEEKIAS
MKRELELKAE ESQALLKAEI ATSRAQWNKE KHDEIQRLRE DNEKDYRVFL DEHRNKLTDT
LSTAKVEFEK QKNELIAQKD REMAERLDES LKQWALDESR RMRALENEIL SEVEQCMYEI
HDQLLDKSIV KDRLPSMKSN LDVTFLEKLK ACLQKSVKGI LYKVLANARQ DWKKKYDTES
NQETGIRGGE LEGSDDRKTA KMWYLDKDLG KTEKQPCCEH WVQQLEKSKK ECYEIRSKLE
KACRHLQQLV KEQKLKAEKY RKNHILTEEL KKQNSELQKK LELTVAPSPA CLEPVEGGSN
GCMMCNGNAL EEIRAQYIKA VDKIKNDMLR YIHESKGRAA ELLKSEVLRE RQETARKMRK
YYLTCLQQLL KDDGNNEGAE KKIINAASKL ATMAKVLETP VSQKYQSKSL NSDLPQNENF
LSETTQDQRS LQKPAHSHQN NNPLNQNIDQ QTIEELIKRH VREKSDGNKV TDAEGASAIN
ENSSFPTLRK SLVDNGNSQF VPSAPFQKLK TFSCIDSSTE GVLVTHQNKQ SALQSGTLYP
NSEHPKKKPG LQRFDLQETP VRDENGSNDW SCISSKSLFQ PHSAKGSLTQ LKMGPQNADV
EEHSSAVASC SLAEENHNTF SSGARNQHFF AQVAKRKDEN SGRKYSNKIQ EPSATGIHPE
SKLFSDVGQG NKLPSRKLLL DFTLSPQQDS GFDSPFPNLN NFN