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Cell death protein 4

 CED4_CAEEL              Reviewed;         571 AA.
P30429; Q5BHI5;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 2.
20-JUN-2018, entry version 153.
RecName: Full=Cell death protein 4;
Name=ced-4; ORFNames=C35D10.9;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=1286611;
Yuan J., Horvitz H.R.;
"The Caenorhabditis elegans cell death gene ced-4 encodes a novel
protein and is expressed during the period of extensive programmed
cell death.";
Development 116:309-320(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION.
PubMed=3955651;
Ellis H.M., Horvitz H.R.;
"Genetic control of programmed cell death in the nematode C.
elegans.";
Cell 44:817-829(1986).
[4]
FUNCTION, AND ALTERNATIVE SPLICING.
PubMed=8706125; DOI=10.1016/S0092-8674(00)80092-6;
Shaham S., Horvitz H.R.;
"An alternatively spliced C. elegans ced-4 RNA encodes a novel cell
death inhibitor.";
Cell 86:201-208(1996).
[5]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH CED-9.
PubMed=9027313; DOI=10.1126/science.275.5303.1126;
Wu D., Wallen H.D., Nunez G.;
"Interaction and regulation of subcellular localization of CED-4 by
CED-9.";
Science 275:1126-1129(1997).
[6]
FUNCTION.
PubMed=9927601;
Gumienny T.L., Lambie E., Hartwieg E., Horvitz H.R., Hengartner M.O.;
"Genetic control of programmed cell death in the Caenorhabditis
elegans hermaphrodite germline.";
Development 126:1011-1022(1999).
[7]
INTERACTION WITH MAC-1, AND MUTAGENESIS OF ILE-280.
PubMed=10101135;
Wu D., Chen P.J., Chen S., Hu Y., Nunez G., Ellis R.E.;
"C. elegans MAC-1, an essential member of the AAA family of ATPases,
can bind CED-4 and prevent cell death.";
Development 126:2021-2031(1999).
[8]
FUNCTION, AND INTERACTION WITH FEM-1.
PubMed=10764728; DOI=10.1074/jbc.C000146200;
Chan S.L., Yee K.S., Tan K.M., Yu V.C.;
"The Caenorhabditis elegans sex determination protein FEM-1 is a CED-3
substrate that associates with CED-4 and mediates apoptosis in
mammalian cells.";
J. Biol. Chem. 275:17925-17928(2000).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10688797; DOI=10.1126/science.287.5457.1485;
Chen F., Hersh B.M., Conradt B., Zhou Z., Riemer D., Gruenbaum Y.,
Horvitz H.R.;
"Translocation of C. elegans CED-4 to nuclear membranes during
programmed cell death.";
Science 287:1485-1489(2000).
[10]
FUNCTION.
PubMed=11226309; DOI=10.1073/pnas.041613098;
Aballay A., Ausubel F.M.;
"Programmed cell death mediated by ced-3 and ced-4 protects
Caenorhabditis elegans from Salmonella typhimurium-mediated killing.";
Proc. Natl. Acad. Sci. U.S.A. 98:2735-2739(2001).
[11]
FUNCTION, AND INTERACTION WITH CED-9.
PubMed=15383288; DOI=10.1016/j.molcel.2004.08.022;
Yan N., Gu L., Kokel D., Chai J., Li W., Han A., Chen L., Xue D.,
Shi Y.;
"Structural, biochemical, and functional analyses of CED-9 recognition
by the proapoptotic proteins EGL-1 and CED-4.";
Mol. Cell 15:999-1006(2004).
[12]
FUNCTION.
PubMed=17329362; DOI=10.1242/dev.02818;
Maurer C.W., Chiorazzi M., Shaham S.;
"Timing of the onset of a developmental cell death is controlled by
transcriptional induction of the C. elegans ced-3 caspase-encoding
gene.";
Development 134:1357-1368(2007).
[13]
FUNCTION.
PubMed=21901106; DOI=10.1371/journal.pgen.1002238;
Rutkowski R., Dickinson R., Stewart G., Craig A., Schimpl M.,
Keyse S.M., Gartner A.;
"Regulation of Caenorhabditis elegans p53/CEP-1-dependent germ cell
apoptosis by Ras/MAPK signaling.";
PLoS Genet. 7:E1002238-E1002238(2011).
[14]
FUNCTION.
PubMed=22629231; DOI=10.1371/journal.pbio.1001331;
Pinan-Lucarre B., Gabel C.V., Reina C.P., Hulme S.E.,
Shevkoplyas S.S., Slone R.D., Xue J., Qiao Y., Weisberg S.,
Roodhouse K., Sun L., Whitesides G.M., Samuel A., Driscoll M.;
"The core apoptotic executioner proteins CED-3 and CED-4 promote
initiation of neuronal regeneration in Caenorhabditis elegans.";
PLoS Biol. 10:E1001331-E1001331(2012).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23106139; DOI=10.1111/jnc.12072;
VanDuyn N., Settivari R., LeVora J., Zhou S., Unrine J., Nass R.;
"The metal transporter SMF-3/DMT-1 mediates aluminum-induced dopamine
neuron degeneration.";
J. Neurochem. 124:147-157(2013).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25432023; DOI=10.7554/eLife.04265;
Weaver B.P., Zabinsky R., Weaver Y.M., Lee E.S., Xue D., Han M.;
"CED-3 caspase acts with miRNAs to regulate non-apoptotic gene
expression dynamics for robust development in C. elegans.";
Elife 3:E04265-E04265(2014).
[17]
FUNCTION.
PubMed=26074078; DOI=10.1016/j.celrep.2015.05.031;
Meng L., Mulcahy B., Cook S.J., Neubauer M., Wan A., Jin Y., Yan D.;
"The cell death pathway regulates synapse elimination through cleavage
of gelsolin in Caenorhabditis elegans neurons.";
Cell Rep. 11:1737-1748(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF ISOFORM A IN COMPLEX WITH
ATP; MAGNESIUM AND CED-9, FUNCTION, AND MUTAGENESIS OF VAL-252;
ARG-255; MET-256 AND 272-ASP-ASP-273.
PubMed=16208361; DOI=10.1038/nature04002;
Yan N., Chai J., Lee E.S., Gu L., Liu Q., He J., Wu J.W., Kokel D.,
Li H., Hao Q., Xue D., Shi Y.;
"Structure of the CED-4-CED-9 complex provides insights into
programmed cell death in Caenorhabditis elegans.";
Nature 437:831-837(2005).
[19]
X-RAY CRYSTALLOGRAPHY (3.53 ANGSTROMS) IN COMPLEX WITH CED-3;
MAGNESIUM AND ATP, AND FUNCTION.
PubMed=20434985; DOI=10.1016/j.cell.2010.03.017;
Qi S., Pang Y., Hu Q., Liu Q., Li H., Zhou Y., He T., Liang Q.,
Liu Y., Yuan X., Luo G., Li H., Wang J., Yan N., Shi Y.;
"Crystal structure of the Caenorhabditis elegans apoptosome reveals an
octameric assembly of CED-4.";
Cell 141:446-457(2010).
[20]
X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) IN COMPLEX WITH CED-3 AND ATP
(ISOFORM A), FUNCTION, AND MUTAGENESIS OF ALA-416.
PubMed=24065769; DOI=10.1101/gad.224428.113;
Huang W., Jiang T., Choi W., Qi S., Pang Y., Hu Q., Xu Y., Gong X.,
Jeffrey P.D., Wang J., Shi Y.;
"Mechanistic insights into CED-4-mediated activation of CED-3.";
Genes Dev. 27:2039-2048(2013).
-!- FUNCTION: Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic
signaling cascade required for the initiation of programmed cell
death in cells fated to die during embryonic and postembryonic
development (PubMed:3955651). During oogenesis, required for
germline apoptosis downstream of ced-9 and upstream of ced-3 but
independently of egl-1 (PubMed:9927601). May regulate germline
apoptosis in response to DNA damage, probably downstream of let-
60/ras and mpk-1 pathway (PubMed:21901106). Regulates CEP neuron
apoptosis in response to high Al(3+) levels (PubMed:23106139).
During male tail morphogenesis, promotes apoptosis of the tail-
spike cell upstream of ced-3 but independently of egl-1 and ced-9
(PubMed:17329362). May play a role in sex-specific cell apoptosis,
probably by promoting ced-3-mediated cleavage of sex-determining
protein fem-1 (PubMed:10764728). During larval development,
required for the elimination of transient presynaptic components
downstream of egl-1 and ced-9 and upstream of ced-3 apoptotic
pathway (PubMed:26074078). Downstream of calreticulin crt-1 and
upstream of ced-3 and independently of egl-1 and ced-9, plays a
role in the initial steps of axonal regrowth following axotomy
(PubMed:22629231). Together with ain-1, a component of the miRNA-
induced-silencing complex (miRISC), and probably upstream of ced-
3, regulates temporal cell fate patterning during larval
development (PubMed:25432023). May play a role in resistance to
S.typhimurium-mediated infection (PubMed:11226309).
{ECO:0000269|PubMed:10764728, ECO:0000269|PubMed:11226309,
ECO:0000269|PubMed:17329362, ECO:0000269|PubMed:21901106,
ECO:0000269|PubMed:22629231, ECO:0000269|PubMed:23106139,
ECO:0000269|PubMed:25432023, ECO:0000269|PubMed:26074078,
ECO:0000269|PubMed:3955651, ECO:0000269|PubMed:9927601}.
-!- FUNCTION: Isoform a: Plays a major role in programmed cell death
(PubMed:1286611, PubMed:8706125). egl-1 binds to and directly
inhibits the activity of ced-9, releasing the cell death activator
ced-4 from a ced-9/ced-4 containing protein complex and allowing
ced-4 to induce caspase ced-3 autoproteolytic cleavage and
activation (PubMed:15383288, PubMed:16208361, PubMed:20434985,
PubMed:24065769). Also forms an holoenzyme with processed ced-3
enhancing ced-3 activity (PubMed:20434985).
{ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:1286611,
ECO:0000269|PubMed:15383288, ECO:0000269|PubMed:16208361,
ECO:0000269|PubMed:20434985, ECO:0000269|PubMed:24065769,
ECO:0000269|PubMed:8706125}.
-!- FUNCTION: Isoform b: Prevents programmed cell death.
{ECO:0000269|PubMed:8706125}.
-!- SUBUNIT: Associates as an asymmetric homodimer with ced-9
(PubMed:16208361, PubMed:9027313, PubMed:15383288). Upon release
from ced-9, forms an octamer, known as the apoptosome, and
interacts with ced-3; the interaction results in ced-3
autoproteolytic cleavage and activation (PubMed:20434985,
PubMed:24065769). The octamer (a tetramer of an asymmetric dimer)
also interacts with two processed ced-3 to form a stable
holoenzyme (PubMed:20434985). Interacts with sex-determining
protein fem-1 (PubMed:10764728). May form a complex composed of
ced-3, ced-4 and mac-1 or of ced-9, ced-4 and mac-1
(PubMed:10101135). Within the complex, interacts with ced-4
(PubMed:10101135). {ECO:0000269|PubMed:10101135,
ECO:0000269|PubMed:10764728, ECO:0000269|PubMed:15383288,
ECO:0000269|PubMed:16208361, ECO:0000269|PubMed:20434985,
ECO:0000269|PubMed:24065769, ECO:0000269|PubMed:9027313}.
-!- INTERACTION:
Q07817-1:BCL2L1 (xeno); NbExp=2; IntAct=EBI-536271, EBI-287195;
P42573:ced-3; NbExp=13; IntAct=EBI-536271, EBI-494247;
P41958:ced-9; NbExp=17; IntAct=EBI-494118, EBI-494110;
Q9NAG4:mac-1; NbExp=8; IntAct=EBI-536271, EBI-2005767;
Q20924:sun-1; NbExp=3; IntAct=EBI-494118, EBI-15599048;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10688797,
ECO:0000269|PubMed:9027313}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}. Note=In
non cell death induced cells, ced-9 is required for mitochondrial
localization. Perinuclear in cell death induced cells.
{ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=b; Synonyms=Long;
IsoId=P30429-1; Sequence=Displayed;
Note=Minor transcript.;
Name=a; Synonyms=Short;
IsoId=P30429-2; Sequence=VSP_013199;
Note=Major transcript.;
-!- DEVELOPMENTAL STAGE: Abundantly expressed during embryogenesis and
to a lesser extent in larvae and adults (PubMed:1286611).
Expression starts at the 100-cell stage and persists through
embryogenesis (at protein level) (PubMed:9027313). Not expressed
in larvae and adults (at protein level) (PubMed:9027313).
{ECO:0000269|PubMed:1286611, ECO:0000269|PubMed:9027313}.
-!- DISRUPTION PHENOTYPE: Mutants exhibit a block in almost all
programmed cell deaths that normally occur during development
(PubMed:1286611). RNAi-mediated knockdown causes a defect in egg
laying in a small proportion of animals (PubMed:25432023). Also
causes a moderate increase in CEP neuron survival in response to
high Al(3+) levels (PubMed:23106139). In an ain-1 mutant
background, enhances the proportion of animals arrested at the
larval stage, with egg-laying defects and with a ruptured vulva
(PubMed:25432023). {ECO:0000269|PubMed:1286611,
ECO:0000269|PubMed:23106139, ECO:0000269|PubMed:25432023}.
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EMBL; X69016; CAA48781.1; -; Genomic_DNA.
EMBL; FO080789; CCD66781.1; -; Genomic_DNA.
EMBL; FO080789; CCD66782.1; -; Genomic_DNA.
PIR; S72566; S72566.
RefSeq; NP_001021202.1; NM_001026031.2. [P30429-2]
RefSeq; NP_001021203.1; NM_001026032.1. [P30429-1]
UniGene; Cel.10679; -.
PDB; 2A5Y; X-ray; 2.60 A; B/C=1-571.
PDB; 3LQQ; X-ray; 3.53 A; A/B=1-571.
PDB; 3LQR; X-ray; 3.90 A; A/B=1-571.
PDB; 4M9S; X-ray; 3.21 A; A/B/C/D=1-571.
PDB; 4M9X; X-ray; 3.34 A; A/B=1-571.
PDB; 4M9Y; X-ray; 4.20 A; A/B=1-571.
PDB; 4M9Z; X-ray; 3.40 A; A/B/C/D=1-571.
PDBsum; 2A5Y; -.
PDBsum; 3LQQ; -.
PDBsum; 3LQR; -.
PDBsum; 4M9S; -.
PDBsum; 4M9X; -.
PDBsum; 4M9Y; -.
PDBsum; 4M9Z; -.
ProteinModelPortal; P30429; -.
SMR; P30429; -.
BioGrid; 40877; 5.
ComplexPortal; CPX-1358; ced-3-ced-4-mac-1 complex.
ComplexPortal; CPX-1359; ced-4-ced-9-mac-1 complex.
ComplexPortal; CPX-1360; ced-3-ced-4 caspase complex.
ComplexPortal; CPX-399; ced-9-ced-4 complex.
DIP; DIP-1016N; -.
IntAct; P30429; 7.
STRING; 6239.C35D10.9b; -.
EPD; P30429; -.
PaxDb; P30429; -.
PeptideAtlas; P30429; -.
PRIDE; P30429; -.
EnsemblMetazoa; C35D10.9b.1; C35D10.9b.1; WBGene00000418. [P30429-1]
EnsemblMetazoa; C35D10.9b.2; C35D10.9b.2; WBGene00000418. [P30429-1]
GeneID; 175643; -.
KEGG; cel:CELE_C35D10.9; -.
UCSC; C35D10.9b; c. elegans. [P30429-1]
CTD; 175643; -.
WormBase; C35D10.9a; CE01203; WBGene00000418; ced-4. [P30429-2]
WormBase; C35D10.9b; CE38154; WBGene00000418; ced-4. [P30429-1]
eggNOG; KOG4658; Eukaryota.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000111533; -.
InParanoid; P30429; -.
KO; K20105; -.
OMA; AIMESYK; -.
OrthoDB; EOG091G05PL; -.
PhylomeDB; P30429; -.
EvolutionaryTrace; P30429; -.
PRO; PR:P30429; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00000418; -.
GO; GO:0008303; C:caspase complex; IMP:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:WormBase.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
GO; GO:0043531; F:ADP binding; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IDA:WormBase.
GO; GO:0051432; F:BH1 domain binding; IPI:WormBase.
GO; GO:0051434; F:BH3 domain binding; IPI:WormBase.
GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0061133; F:endopeptidase activator activity; IDA:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; IDA:WormBase.
GO; GO:0030042; P:actin filament depolymerization; IMP:UniProtKB.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:1902742; P:apoptotic process involved in development; IMP:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
GO; GO:0048598; P:embryonic morphogenesis; IGI:WormBase.
GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:WormBase.
GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IMP:UniProtKB.
GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IDA:WormBase.
GO; GO:0010954; P:positive regulation of protein processing; IDA:UniProtKB.
GO; GO:1905808; P:positive regulation of synapse disassembly; IMP:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0008361; P:regulation of cell size; IGI:WormBase.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:WormBase.
GO; GO:0040034; P:regulation of development, heterochronic; IGI:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IGI:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR016854; Apop_reg_Ced-4.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002182; NB-ARC.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00619; CARD; 1.
Pfam; PF00931; NB-ARC; 1.
PIRSF; PIRSF027202; Apop_reg_Ced-4; 1.
SMART; SM00114; CARD; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50209; CARD; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; ATP-binding;
Complete proteome; Cytoplasm; Magnesium; Metal-binding; Mitochondrion;
Nucleotide-binding; Reference proteome.
CHAIN 1 571 Cell death protein 4.
/FTId=PRO_0000089470.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
DOMAIN 133 439 NB-ARC. {ECO:0000255}.
NP_BIND 162 167 ATP. {ECO:0000244|PDB:2A5Y,
ECO:0000244|PDB:3LQQ,
ECO:0000244|PDB:3LQR,
ECO:0000244|PDB:4M9S,
ECO:0000244|PDB:4M9X,
ECO:0000244|PDB:4M9Y,
ECO:0000244|PDB:4M9Z,
ECO:0000269|PubMed:16208361,
ECO:0000269|PubMed:20434985,
ECO:0000269|PubMed:24065769}.
METAL 166 166 Magnesium. {ECO:0000269|PubMed:16208361,
ECO:0000269|PubMed:20434985}.
BINDING 131 131 ATP; via carbonyl oxygen.
{ECO:0000244|PDB:2A5Y,
ECO:0000244|PDB:3LQQ,
ECO:0000244|PDB:3LQR,
ECO:0000244|PDB:4M9S,
ECO:0000244|PDB:4M9X,
ECO:0000244|PDB:4M9Y,
ECO:0000244|PDB:4M9Z,
ECO:0000269|PubMed:16208361,
ECO:0000269|PubMed:20434985,
ECO:0000269|PubMed:24065769}.
BINDING 171 171 ATP. {ECO:0000244|PDB:4M9S,
ECO:0000269|PubMed:24065769}.
VAR_SEQ 212 234 ARVVSDTDDSHSITDFINRVLSR -> K (in isoform
a). {ECO:0000305}.
/FTId=VSP_013199.
MUTAGEN 252 252 V->D: Loss of dimerization without
affecting interaction with ced-9, loss of
ced-3 activation and severe reduction in
the number of cell corpses in embryos in
a ced-1 mutant background; when
associated with E-255 and E-256.
{ECO:0000269|PubMed:16208361}.
MUTAGEN 255 255 R->E: Severe reduction in the number of
cell corpses in embryos in a ced-1 mutant
background. Loss of dimerization without
affecting interaction with ced-9, loss of
ced-3 activation and severe reduction in
the number of cell corpses in embryos in
a ced-1 mutant background; when
associated with E-252 and E-256.
{ECO:0000269|PubMed:16208361}.
MUTAGEN 256 256 M->E: Loss of dimerization without
affecting interaction with ced-9, loss of
ced-3 activation and severe reduction in
the number of cell corpses in embryos in
a ced-1 mutant background; when
associated with E-252 and E-255.
{ECO:0000269|PubMed:16208361}.
MUTAGEN 272 273 DD->AA: Severe reduction in the number of
cell corpses in embryos in a ced-1 mutant
background.
{ECO:0000269|PubMed:16208361}.
MUTAGEN 280 280 I->N: In n1948; no effect on the
interaction with mac-1.
{ECO:0000269|PubMed:10101135}.
MUTAGEN 416 416 A->W: Reduced interaction with ced-3.
{ECO:0000269|PubMed:24065769}.
HELIX 4 20 {ECO:0000244|PDB:2A5Y}.
HELIX 23 26 {ECO:0000244|PDB:2A5Y}.
HELIX 27 32 {ECO:0000244|PDB:2A5Y}.
HELIX 38 45 {ECO:0000244|PDB:2A5Y}.
STRAND 47 49 {ECO:0000244|PDB:2A5Y}.
HELIX 50 64 {ECO:0000244|PDB:2A5Y}.
STRAND 66 68 {ECO:0000244|PDB:2A5Y}.
HELIX 69 77 {ECO:0000244|PDB:2A5Y}.
HELIX 81 96 {ECO:0000244|PDB:2A5Y}.
HELIX 101 104 {ECO:0000244|PDB:2A5Y}.
TURN 105 108 {ECO:0000244|PDB:2A5Y}.
HELIX 112 121 {ECO:0000244|PDB:2A5Y}.
HELIX 134 147 {ECO:0000244|PDB:2A5Y}.
STRAND 150 158 {ECO:0000244|PDB:2A5Y}.
HELIX 165 175 {ECO:0000244|PDB:2A5Y}.
TURN 181 183 {ECO:0000244|PDB:2A5Y}.
STRAND 184 191 {ECO:0000244|PDB:2A5Y}.
STRAND 196 198 {ECO:0000244|PDB:4M9X}.
HELIX 199 211 {ECO:0000244|PDB:2A5Y}.
TURN 234 236 {ECO:0000244|PDB:2A5Y}.
STRAND 239 241 {ECO:0000244|PDB:4M9S}.
HELIX 250 261 {ECO:0000244|PDB:2A5Y}.
STRAND 267 274 {ECO:0000244|PDB:2A5Y}.
HELIX 277 285 {ECO:0000244|PDB:2A5Y}.
STRAND 289 296 {ECO:0000244|PDB:2A5Y}.
HELIX 297 302 {ECO:0000244|PDB:2A5Y}.
STRAND 307 311 {ECO:0000244|PDB:2A5Y}.
HELIX 317 326 {ECO:0000244|PDB:2A5Y}.
HELIX 336 348 {ECO:0000244|PDB:2A5Y}.
HELIX 352 359 {ECO:0000244|PDB:2A5Y}.
STRAND 364 366 {ECO:0000244|PDB:2A5Y}.
HELIX 367 380 {ECO:0000244|PDB:2A5Y}.
HELIX 381 384 {ECO:0000244|PDB:4M9S}.
STRAND 389 395 {ECO:0000244|PDB:2A5Y}.
HELIX 396 405 {ECO:0000244|PDB:2A5Y}.
HELIX 409 414 {ECO:0000244|PDB:2A5Y}.
HELIX 417 419 {ECO:0000244|PDB:2A5Y}.
HELIX 429 435 {ECO:0000244|PDB:2A5Y}.
HELIX 450 458 {ECO:0000244|PDB:2A5Y}.
TURN 459 461 {ECO:0000244|PDB:2A5Y}.
STRAND 462 464 {ECO:0000244|PDB:2A5Y}.
STRAND 466 469 {ECO:0000244|PDB:2A5Y}.
STRAND 471 473 {ECO:0000244|PDB:2A5Y}.
STRAND 475 477 {ECO:0000244|PDB:2A5Y}.
HELIX 480 487 {ECO:0000244|PDB:2A5Y}.
HELIX 493 499 {ECO:0000244|PDB:2A5Y}.
TURN 503 505 {ECO:0000244|PDB:2A5Y}.
TURN 510 512 {ECO:0000244|PDB:4M9Z}.
HELIX 555 558 {ECO:0000244|PDB:4M9S}.
HELIX 559 562 {ECO:0000244|PDB:2A5Y}.
SEQUENCE 571 AA; 65336 MW; 6BE9893946B79E6C CRC64;
MLCEIECRAL STAHTRLIHD FEPRDALTYL EGKNIFTEDH SELISKMSTR LERIANFLRI
YRRQASELGP LIDFFNYNNQ SHLADFLEDY IDFAINEPDL LRPVVIAPQF SRQMLDRKLL
LGNVPKQMTC YIREYHVDRV IKKLDEMCDL DSFFLFLHGR AGSGKSVIAS QALSKSDQLI
GINYDSIVWL KDSGTAPKST FDLFTDILLM LARVVSDTDD SHSITDFINR VLSRSEDDLL
NFPSVEHVTS VVLKRMICNA LIDRPNTLFV FDDVVQEETI RWAQELRLRC LVTTRDVEIS
NAASQTCEFI EVTSLEIDEC YDFLEAYGMP MPVGEKEEDV LNKTIELSSG NPATLMMFFK
SCEPKTFEKM AQLNNKLESR GLVGVECITP YSYKSLAMAL QRCVEVLSDE DRSALAFAVV
MPPGVDIPVK LWSCVIPVDI CSNEEEQLDD EVADRLKRLS KRGALLSGKR MPVLTFKIDH
IIHMFLKHVV DAQTIANGIS ILEQRLLEIG NNNVSVPERH IPSHFQKFRR SSASEMYPKT
TEETVIRPED FPKFMQLHQK FYDSLKNFAC C


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