CES2_CAEEL
ID CES2_CAEEL Reviewed; 211 AA.
AC Q94126;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Transcription factor ces-2 {ECO:0000305};
DE AltName: Full=Cell death specification protein 2 {ECO:0000312|WormBase:ZK909.4};
GN Name=ces-2; ORFNames=ZK909.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF ALA-129.
RC STRAIN=Bristol N2;
RX PubMed=8700229; DOI=10.1038/382545a0;
RA Metzstein M.M., Hengartner M.O., Tsung N., Ellis R., Horvitz H.R.;
RT "Transcriptional regulator of programmed cell death encoded by
RT Caenorhabditis elegans gene ces-2.";
RL Nature 382:545-547(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-129.
RX PubMed=12231624; DOI=10.1101/gad.996302;
RA Wang X., Chamberlin H.M.;
RT "Multiple regulatory changes contribute to the evolution of the
RT Caenorhabditis lin-48 ovo gene.";
RL Genes Dev. 16:2345-2349(2002).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INTERACTION WITH ATF-2.
RX PubMed=16310763; DOI=10.1016/j.ydbio.2005.10.029;
RA Wang X., Jia H., Chamberlin H.M.;
RT "The bZip proteins CES-2 and ATF-2 alter the timing of transcription for a
RT cell-specific target gene in C. elegans.";
RL Dev. Biol. 289:456-465(2006).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=19686386; DOI=10.1111/j.1471-4159.2009.06323.x;
RA Janssen T., Husson S.J., Meelkop E., Temmerman L., Lindemans M.,
RA Verstraelen K., Rademakers S., Mertens I., Nitabach M., Jansen G.,
RA Schoofs L.;
RT "Discovery and characterization of a conserved pigment dispersing factor-
RT like neuropeptide pathway in Caenorhabditis elegans.";
RL J. Neurochem. 111:228-241(2009).
CC -!- FUNCTION: Transcription factor (PubMed:8700229, PubMed:16310763).
CC Required to activate programmed cell death in the sister cells of the
CC serotoninergic neurosecretory motor (NSM) neurons (PubMed:8700229).
CC Negatively regulates the activity of ces-1 which in turn negatively
CC regulates the activities of cell-killing genes (PubMed:8700229). Binds
CC to the DNA sequence 5'-RTTACGTAAY-3' (PubMed:8700229). Involved in the
CC development of the excretory duct cell, by positively modulating
CC embryonic transcription of putative transcription factor lin-48, acting
CC in concert with NFIL3 transcription factor homolog atf-2
CC (PubMed:16310763, PubMed:12231624). Positively modulates expression of
CC neuropeptide pigment dispersing factor homologs pdf-1 and pdf-2
CC (PubMed:19686386). {ECO:0000269|PubMed:16310763,
CC ECO:0000269|PubMed:19686386, ECO:0000269|PubMed:8700229}.
CC -!- SUBUNIT: Interacts with NFIL3 transcription factor homolog atf-2.
CC {ECO:0000269|PubMed:16310763}.
CC -!- INTERACTION:
CC Q94126; Q21361: atf-2; NbExp=4; IntAct=EBI-328155, EBI-317743;
CC Q94126; Q8IG69: cebp-2; NbExp=3; IntAct=EBI-328155, EBI-2914231;
CC Q94126; Q94126: ces-2; NbExp=2; IntAct=EBI-328155, EBI-328155;
CC Q94126; Q9XUK2: zip-3; NbExp=2; IntAct=EBI-328155, EBI-322774;
CC Q94126; Q9NAE4: zip-7; NbExp=4; IntAct=EBI-328155, EBI-332523;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Expression begins in the embryo and diminishes in
CC larvae (PubMed:16310763). Expressed in the excretory duct cell, as well
CC as other cells, at larval L3 stage (PubMed:16310763).
CC {ECO:0000269|PubMed:16310763}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes morphological
CC defects in excretory duct cells. Reduces expression of transcription
CC factor lin-48. {ECO:0000269|PubMed:12231624}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; U60979; AAC47277.1; -; Genomic_DNA.
DR EMBL; Z82096; CAB05032.1; -; Genomic_DNA.
DR PIR; T28098; T28098.
DR RefSeq; NP_493610.1; NM_061209.5.
DR AlphaFoldDB; Q94126; -.
DR SMR; Q94126; -.
DR BioGRID; 38746; 19.
DR DIP; DIP-27195N; -.
DR IntAct; Q94126; 20.
DR STRING; 6239.ZK909.4; -.
DR EPD; Q94126; -.
DR PaxDb; Q94126; -.
DR EnsemblMetazoa; ZK909.4.1; ZK909.4.1; WBGene00000469.
DR GeneID; 173365; -.
DR KEGG; cel:CELE_ZK909.4; -.
DR UCSC; ZK909.4; c. elegans.
DR CTD; 173365; -.
DR WormBase; ZK909.4; CE15479; WBGene00000469; ces-2.
DR eggNOG; KOG3119; Eukaryota.
DR HOGENOM; CLU_1327470_0_0_1; -.
DR InParanoid; Q94126; -.
DR OMA; CENNHEE; -.
DR OrthoDB; 1500131at2759; -.
DR SignaLink; Q94126; -.
DR PRO; PR:Q94126; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000469; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:WormBase.
DR GO; GO:0007568; P:aging; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:WormBase.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR040223; PAR_bZIP.
DR PANTHER; PTHR11988; PTHR11988; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Apoptosis; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..211
FT /note="Transcription factor ces-2"
FT /id="PRO_0000076638"
FT DOMAIN 116..179
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 83..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..140
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 144..172
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 184..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 129
FT /note="A->T: In n732; defects in programmed cell death in
FT the sister cells of the serotoninergic neurosecretory motor
FT (NSM) neurons. Morphological defects in excretory duct
FT cells. Reduced expression of transcription factor lin-48."
FT /evidence="ECO:0000269|PubMed:12231624,
FT ECO:0000269|PubMed:8700229"
SQ SEQUENCE 211 AA; 23133 MW; A791D04893FC67A0 CRC64;
MDFHRALSAL FTNQAAVQPL LGSLGFPFND GTSILTTALA AQSGGKKLDT PLGILPFDSL
PTTNLLTPTK KIKLEDELCA SPVSSRSSTV SSSHFSSPQR SPSRKMSVPI PEEKKDSAYF
ERRRKNNDAA KRSRDARRQK EEQIASKAHA LERENMQLRG KVSSLEQEAA QLRFLLFSKI
SPANSEVSCE SNDSTETNDS NDSKSDSTIE V
