ID  Q60Z52;
PN  Cell death protein 4;
GN  ced;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion {ECO:0000250|UniProtKB:P30429}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P30429}. Note=In non cell death induced cells, ced-9 is required for mitochondrial localization. Perinuclear in cell death induced cells. {ECO:0000250|UniProtKB:P30429}.
DR  UNIPROT: Q60Z52;
DR  UNIPROT: A8XSP2;
DR  Pfam: PF00619;
DR  Pfam: PF00931;
DE  Function: Plays a major role in programmed cell death (PCD, apoptosis). 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. Also forms an holoenzyme with processed ced-3 enhancing ced-3 activity. 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. During oogenesis, required for germline apoptosis downstream of ced-9 and upstream of ced-3 but independently of egl-1. May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway. Regulates CEP neuron apoptosis in response to high Al(3+) levels. During male tail morphogenesis, promotes apoptosis of the tail-spike cell. 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. 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. May play a role in resistance to S.typhimurium-mediated infection. {ECO:0000250|UniProtKB:P30429}.
DE  Reference Proteome: Yes;
GO  GO:0008303;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
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:0030042;
GO  GO:0097202;
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:0010954;
GO  GO:1905808;
GO  GO:0030155;
GO  GO:0008361;
GO  GO:0040034;
GO  GO:0031647;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLCEIECRALNAAHTMLIQDFEPRDALTYLEGEKIFTEDHSDLISNMPTRLERIANFLRAYRRQASELAPLIDFFEYNNQ
SQ  NHLKDFLDEYLWFATHQPDKLRPVVLVPKFSRQMLDRKLLLGNVPKQMNCFSREFHVDRVIEKLDEMCDLESFFLFLHGR
SQ  SGSGKSVIASQALSKSDQLIGINYDSVVWLKDSGTTPKATFDLFTDLLLMLKRARVVSDTDDSHNMPDFINRVLSRSEDD
SQ  LLNFPSVEHVTSVVLKRMIANALIDRPNTLFVLDDVVQEDTIRWAQELRLRCLITTRDVEISNAASPECEFIEVTPLESY
SQ  ECFELLESYGMPVPAIERDEDILHKTIDLTSGNPAALMMIFKSCEPKTFEKMAQLNSKLETRGLSAIECITPYCYKSLSS
SQ  SLQRCVEVLSDEDRSALAFAVIMPPGIDIPVKIWSCVIPVDICSNEEDQLDDEVADRLKRLSKRGALLSGKRSPVLTYKI
SQ  DHVIHLFLKHVVDVQTIANGISILEQRLHELGNNNTPTPERHMPSKFRRTSAGDMFPKVEDSVIRPEDYSKFMQIHRTFY
SQ  DSLKKFTSQ
//