EGL1_CAEEL
ID EGL1_CAEEL Reviewed; 106 AA.
AC O61667; Q7JLC9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Programmed cell death activator egl-1;
DE AltName: Full=Egg-laying defective protein 1;
GN Name=egl-1 {ECO:0000312|EMBL:AAC39023.1, ECO:0000312|WormBase:F23B12.9};
GN ORFNames=F23B12.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC39023.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CED-9, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC39023.1};
RX PubMed=9604928; DOI=10.1016/s0092-8674(00)81182-4;
RA Conradt B., Horvitz H.R.;
RT "The C. elegans protein EGL-1 is required for programmed cell death and
RT interacts with the Bcl-2-like protein CED-9.";
RL Cell 93:519-529(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB82213.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB82213.2};
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=10688797; DOI=10.1126/science.287.5457.1485;
RA Chen F., Hersh B.M., Conradt B., Zhou Z., Riemer D., Gruenbaum Y.,
RA Horvitz H.R.;
RT "Translocation of C. elegans CED-4 to nuclear membranes during programmed
RT cell death.";
RL Science 287:1485-1489(2000).
RN [4]
RP FUNCTION.
RX PubMed=12874127; DOI=10.1242/dev.00597;
RA Thellmann M., Hatzold J., Conradt B.;
RT "The Snail-like CES-1 protein of C. elegans can block the expression of the
RT BH3-only cell-death activator gene egl-1 by antagonizing the function of
RT bHLH proteins.";
RL Development 130:4057-4071(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25432023; DOI=10.7554/elife.04265;
RA Weaver B.P., Zabinsky R., Weaver Y.M., Lee E.S., Xue D., Han M.;
RT "CED-3 caspase acts with miRNAs to regulate non-apoptotic gene expression
RT dynamics for robust development in C. elegans.";
RL Elife 3:E04265-E04265(2014).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26074078; DOI=10.1016/j.celrep.2015.05.031;
RA Meng L., Mulcahy B., Cook S.J., Neubauer M., Wan A., Jin Y., Yan D.;
RT "The cell death pathway regulates synapse elimination through cleavage of
RT gelsolin in Caenorhabditis elegans neurons.";
RL Cell Rep. 11:1737-1748(2015).
RN [7]
RP FUNCTION.
RX PubMed=20713707; DOI=10.1073/pnas.1010023107;
RA Hirose T., Galvin B.D., Horvitz H.R.;
RT "Six and Eya promote apoptosis through direct transcriptional activation of
RT the proapoptotic BH3-only gene egl-1 in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15479-15484(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 46-102 IN COMPLEX WITH CED-9, AND
RP FUNCTION.
RX PubMed=15383288; DOI=10.1016/j.molcel.2004.08.022;
RA Yan N., Gu L., Kokel D., Chai J., Li W., Han A., Chen L., Xue D., Shi Y.;
RT "Structural, biochemical, and functional analyses of CED-9 recognition by
RT the proapoptotic proteins EGL-1 and CED-4.";
RL Mol. Cell 15:999-1006(2004).
CC -!- FUNCTION: Plays a major role in programmed cell death (PCD or
CC apoptosis) by negatively regulating ced-9 (PubMed:9604928,
CC PubMed:10688797, PubMed:15383288). Binds to and directly inhibits the
CC activity of ced-9, releasing the cell death activator ced-4 from a ced-
CC 9/ced-4 containing protein complex and allowing ced-4 to activate the
CC cell-killing caspase ced-3 (PubMed:9604928, PubMed:10688797,
CC PubMed:15383288). Required to activate programmed cell death in the
CC sister cells of the serotonergic neurosecretory motor (NSM) neurons
CC during embryogenesis (PubMed:12874127). Required to activate programmed
CC cell death in the sister cells of the M4 motor neuron and I1 pharyngeal
CC neuron during embryogenesis (PubMed:20713707). During larval
CC development, required for the elimination of transient presynaptic
CC components upstream of ced-9, ced-4 and ced-3 apoptotic pathway
CC (PubMed:26074078). Together with ain-1, a component of the miRNA-
CC induced-silencing complex (miRISC), and probably upstream of ced-3 and
CC ced-4, regulates temporal cell fate patterning during larval
CC development (PubMed:25432023). {ECO:0000269|PubMed:10688797,
CC ECO:0000269|PubMed:12874127, ECO:0000269|PubMed:15383288,
CC ECO:0000269|PubMed:20713707, ECO:0000269|PubMed:25432023,
CC ECO:0000269|PubMed:26074078, ECO:0000269|PubMed:9604928}.
CC -!- SUBUNIT: Interacts with ced-9; the interaction results in ced-4 release
CC from the ced-4/ced-9 complex. {ECO:0000269|PubMed:15383288,
CC ECO:0000269|PubMed:9604928}.
CC -!- INTERACTION:
CC O61667; P41958: ced-9; NbExp=7; IntAct=EBI-495949, EBI-494110;
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:26074078}.
CC Note=Localizes to RMED/V synaptic regions in L1 larvae.
CC {ECO:0000269|PubMed:26074078}.
CC -!- DISRUPTION PHENOTYPE: Mutants block programmed cell death
CC (PubMed:9604928). In an ain-1 mutant background, enhances the
CC proportion of animals arrested at the larval stage, with egg-laying
CC defects and with a ruptured vulva (PubMed:25432023).
CC {ECO:0000269|PubMed:25432023, ECO:0000269|PubMed:9604928}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39023.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF057309; AAC39023.1; ALT_INIT; mRNA.
DR EMBL; BX284605; CAB82213.2; -; Genomic_DNA.
DR PIR; T43032; T43032.
DR RefSeq; NP_506575.2; NM_074174.3.
DR PDB; 1TY4; X-ray; 2.20 A; C/D=46-102.
DR PDBsum; 1TY4; -.
DR AlphaFoldDB; O61667; -.
DR SMR; O61667; -.
DR BioGRID; 44947; 1.
DR ComplexPortal; CPX-398; ced-9-egl-1 complex.
DR ELM; O61667; -.
DR IntAct; O61667; 2.
DR STRING; 6239.F23B12.9; -.
DR PaxDb; O61667; -.
DR EnsemblMetazoa; F23B12.9.1; F23B12.9.1; WBGene00001170.
DR GeneID; 179943; -.
DR KEGG; cel:CELE_F23B12.9; -.
DR UCSC; F23B12.9; c. elegans.
DR CTD; 179943; -.
DR WormBase; F23B12.9; CE35714; WBGene00001170; egl-1.
DR eggNOG; ENOG502TIVM; Eukaryota.
DR HOGENOM; CLU_2123374_0_0_1; -.
DR InParanoid; O61667; -.
DR OMA; DAEMMSY; -.
DR EvolutionaryTrace; O61667; -.
DR PRO; PR:O61667; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001170; Expressed in pharyngeal muscle cell (C elegans) and 12 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IMP:UniProtKB.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:WormBase.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:1902742; P:apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:WormBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:WormBase.
DR GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IGI:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:WormBase.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:1905808; P:positive regulation of synapse pruning; IMP:UniProtKB.
DR GO; GO:0040034; P:regulation of development, heterochronic; IGI:UniProtKB.
DR DisProt; DP01407; -.
DR InterPro; IPR021543; EGL-1.
DR Pfam; PF11430; EGL-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Reference proteome; Synapse.
FT CHAIN 1..106
FT /note="Programmed cell death activator egl-1"
FT /id="PRO_0000086944"
FT HELIX 65..84
FT /evidence="ECO:0007829|PDB:1TY4"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1TY4"
SQ SEQUENCE 106 AA; 11916 MW; 2329D2DB0F019636 CRC64;
MLMLTFASTS SDLLPMSNVF DVQSSVFYNE KNMFYSSSQD FSSCEDSSQF ADDSGFFDDS
EISSIGYEIG SKLAAMCDDF DAQMMSYSAH ASDRSLFHRL LDFFAF
