CEP1_CAEBR
ID CEP1_CAEBR Reviewed; 658 AA.
AC A8WW61;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Transcription factor cep-1 {ECO:0000250|UniProtKB:Q20646};
GN Name=cep-1 {ECO:0000312|WormBase:CBG04081};
GN ORFNames=CBG04081 {ECO:0000312|WormBase:CBG04081};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP24870.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP24870.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
RN [2] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=15707894; DOI=10.1016/j.cell.2004.12.009;
RA Schumacher B., Hanazawa M., Lee M.-H., Nayak S., Volkmann K., Hofmann E.R.,
RA Hengartner M.O., Schedl T., Gartner A.;
RT "Translational repression of C. elegans p53 by GLD-1 regulates DNA damage-
RT induced apoptosis.";
RL Cell 120:357-368(2005).
RN [3] {ECO:0000305}
RP DNA-BINDING.
RX PubMed=17581633; DOI=10.1038/sj.emboj.7601764;
RA Ou H.D., Loehr F., Vogel V., Maentele W., Doetsch V.;
RT "Structural evolution of C-terminal domains in the p53 family.";
RL EMBO J. 26:3463-3473(2007).
CC -!- FUNCTION: Transcriptional activator that binds the same DNA consensus
CC sequence as p53. Has a role in normal development to ensure proper
CC meiotic chromosome segregation. Promotes apoptosis under conditions of
CC cellular and genotoxic stress in response to DNA damage, hypoxia, or
CC starvation. However, not required for DNA repair in response to UV-C or
CC to regulate cell-cycle progression. Regulates germline apoptosis in
CC response to DNA damage. Required for induction of ced-13 in response to
CC DNA damage. Its pro-apoptotic activity is inhibited when bound to ape-1
CC in vitro (By similarity). Regulates germline proliferation by
CC activating phg-1. Regulates DNA damage-induced apoptosis by inducing
CC transcription of the programmed cell death activator egl-1. Negatively
CC regulates lifespan. {ECO:0000250|UniProtKB:Q20646}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q20646};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q20646};
CC -!- SUBUNIT: Homodimer. Interacts (via C-terminus domain) with prmt-5; not
CC methylated by prmt-5. Interacts with cbp-1 (via HAT domain); cep-1
CC transcriptional activity may be inhibited by interaction with
CC methylated cbp-1. Component of a complex that contains prmt-5 and cbp-1
CC (By similarity). Interacts with ape-1; the interaction inhibits pro-
CC apoptotic activity of cep-1 (By similarity).
CC {ECO:0000250|UniProtKB:Q20646}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q20646}.
CC -!- INDUCTION: By DNA damage. {ECO:0000250|UniProtKB:Q20646, ECO:0000305}.
CC -!- PTM: Phosphorylated in response to IR-induced DNA damage which is
CC thought to be mediated by akt-1. {ECO:0000250|UniProtKB:Q20646}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000255}.
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DR EMBL; HE600906; CAP24870.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WW61; -.
DR SMR; A8WW61; -.
DR STRING; 6238.CBG04081; -.
DR PRIDE; A8WW61; -.
DR EnsemblMetazoa; CBG04081.1; CBG04081.1; WBGene00026824.
DR WormBase; CBG04081; CBP32131; WBGene00026824; Cbr-cep-1.
DR eggNOG; ENOG502TH76; Eukaryota.
DR HOGENOM; CLU_425295_0_0_1; -.
DR InParanoid; A8WW61; -.
DR OMA; VAYPRRD; -.
DR OrthoDB; 1351862at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblMetazoa.
DR GO; GO:0005654; C:nucleoplasm; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IEA:EnsemblMetazoa.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; ISS:UniProtKB.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0045132; P:meiotic chromosome segregation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IEA:EnsemblMetazoa.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; IEA:EnsemblMetazoa.
DR CDD; cd08367; P53; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR011615; p53_DNA-bd.
DR InterPro; IPR015367; Trans_fact_CEP1_DNA-bd.
DR Pfam; PF09287; CEP1-DNA_bind; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
PE 1: Evidence at protein level;
KW Activator; Apoptosis; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Tumor suppressor; Zinc.
FT CHAIN 1..658
FT /note="Transcription factor cep-1"
FT /id="PRO_0000374067"
FT DNA_BIND 238..428
FT /evidence="ECO:0000255"
FT REGION 450..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..564
FT /note="Required for tertiary structure stability of the
FT protein"
FT /evidence="ECO:0000250|UniProtKB:Q20646"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q20646"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q20646"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q20646"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q20646"
SQ SEQUENCE 658 AA; 76245 MW; 3A853567F1175E19 CRC64;
MNTEATDSQL SVLIKKEKIV PDSQEVDGNT TRELGDNTLD EIINGQFSPL MSQNSENELE
KHLRSTPGIE GVFESLLHNE IQEPDITHLS LMSTHPSESG RQPELIKTRT RTPRIVNDGP
LQQTSRSELL DLNALFDTEE SALMNQSIES ETTLTQFLGG SQPIDYLRER TKEEQDKRNQ
MRQEEKLIKK MQKAQVEKAR SEMFSERNHE FEPMECDNDE EDVFRAVKED SSNREKEEEW
LTFEVKKERA SKVSDFEFET VVNDGIYLWA KMKCNIPFIV KWNVSSCHKQ LFLKVRLVNY
MASDNIENSI RVPSNLAKCH NHRMTEEKTP RESFFYVVKS GEHWTPQINS KKDQCFVAKL
APGTTQVLFD LIFKCQRSCL DLAERRKRMC LAVFLEDENG NELLHDVIKQ LLIVGYPRRD
WKNFCEKRGD FKFSEKSLLV QTTNNIFADQ SSLHSGPSSP EKVTDTSQMF QSTSSSSRKR
AASDVKFVAS AVPSSDQQSY PMRLHGCESR RMEMSFYRKF KENEDSLSNK RPRSQYGLQR
QVKLSEKEYS KFVAFFAKEG ENEISKYASA HCLTPAQASR LDPSDKIEKF LAFVGDESAA
DNFRKHGLFT MLDLDKYFQV YDSAFETIGV DSSKMEKYYD LFLHYHRVQE NIRYNQPK
