ID  P30429;
PN  Cell death protein 4;
GN  ced;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: 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}.
DR  UNIPROT: P30429;
DR  UNIPROT: Q5BHI5;
DR  PDB: 2A5Y;
DR  PDB: 3LQQ;
DR  PDB: 3LQR;
DR  PDB: 4M9S;
DR  PDB: 4M9X;
DR  PDB: 4M9Y;
DR  PDB: 4M9Z;
DR  Pfam: PF00619;
DR  Pfam: PF00931;
DR  PROSITE: PS50209;
DE  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}. [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 a 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}. [Isoform b]: Prevents programmed cell death. {ECO:0000269|PubMed:8706125}.
DE  Reference Proteome: Yes;
DE  Interaction: P41958; IntAct: EBI-494126; Score: 0.84
DE  Interaction: Q07817; IntAct: EBI-494146; Score: 0.40
DE  Interaction: P42573; IntAct: EBI-494268; Score: 0.86
DE  Interaction: O61667; IntAct: EBI-11688070; Score: 0.35
DE  Interaction: P30429; IntAct: EBI-2655126; Score: 0.44
DE  Interaction: Q20924; IntAct: EBI-15599089; Score: 0.56
DE  Interaction: Q14790; IntAct: EBI-16211709; Score: 0.40
DE  Interaction: Q9NAG4; IntAct: EBI-16587288; Score: 0.57
GO  GO:0008303;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0051432;
GO  GO:0051434;
GO  GO:0089720;
GO  GO:0008656;
GO  GO:0061133;
GO  GO:0042802;
GO  GO:0000287;
GO  GO:0016505;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0048598;
GO  GO:0046716;
GO  GO:0043066;
GO  GO:1900118;
GO  GO:0043065;
GO  GO:1904747;
GO  GO:2001056;
GO  GO:0010954;
GO  GO:1905808;
GO  GO:0030155;
GO  GO:0008361;
GO  GO:0043281;
GO  GO:0040034;
GO  GO:0031647;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLCEIECRALSTAHTRLIHDFEPRDALTYLEGKNIFTEDHSELISKMSTRLERIANFLRIYRRQASELGPLIDFFNYNNQ
SQ  SHLADFLEDYIDFAINEPDLLRPVVIAPQFSRQMLDRKLLLGNVPKQMTCYIREYHVDRVIKKLDEMCDLDSFFLFLHGR
SQ  AGSGKSVIASQALSKSDQLIGINYDSIVWLKDSGTAPKSTFDLFTDILLMLARVVSDTDDSHSITDFINRVLSRSEDDLL
SQ  NFPSVEHVTSVVLKRMICNALIDRPNTLFVFDDVVQEETIRWAQELRLRCLVTTRDVEISNAASQTCEFIEVTSLEIDEC
SQ  YDFLEAYGMPMPVGEKEEDVLNKTIELSSGNPATLMMFFKSCEPKTFEKMAQLNNKLESRGLVGVECITPYSYKSLAMAL
SQ  QRCVEVLSDEDRSALAFAVVMPPGVDIPVKLWSCVIPVDICSNEEEQLDDEVADRLKRLSKRGALLSGKRMPVLTFKIDH
SQ  IIHMFLKHVVDAQTIANGISILEQRLLEIGNNNVSVPERHIPSHFQKFRRSSASEMYPKTTEETVIRPEDFPKFMQLHQK
SQ  FYDSLKNFACC
//