ID  P45436;
PN  Cell death protein 3 subunit p13;
GN  ced;
OS  31234;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P42573}. Perikaryon {ECO:0000250|UniProtKB:P42573}. Synapse {ECO:0000250|UniProtKB:P42573}. Mitochondrion {ECO:0000250|UniProtKB:P42573}. Cytoplasm {ECO:0000250|UniProtKB:P42573}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P42573}. Note=Colocalizes with nucleoporin npp- 14 to the perinuclear region in germ cells. Becomes diffused in the cytoplasm in apoptotic germ cells. Localizes to axonal mitochondria and synapses of DD motor neurons. Synaptic localization is dependent on axonal mitochondria. {ECO:0000250|UniProtKB:P42573}.
DR  UNIPROT: P45436;
DR  UNIPROT: E3M6B9;
DR  Pfam: PF00619;
DR  PROSITE: PS50209;
DR  PROSITE: PS01122;
DR  PROSITE: PS01121;
DR  PROSITE: PS50207;
DR  PROSITE: PS50208;
DE  Function: Acts as a cysteine protease in controlling programmed cell death (apoptosis) by proteolytically activating or inactivating a wide range of substrates. 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 ced-4 but independently of egl-1. By cleaving and activating ced-8, promotes phosphatidylserine exposure on the surface of apoptotic cells; phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. By cleaving and converting dcr-1 into a deoxyribonuclease (DNase), promotes apoptotic chromosomal DNA fragmentation. By cleaving mitochondrial fission protein drp-1, may regulate the removal of mitochondria during apoptosis. During germline apoptosis, cleaves translation initiation factor ifg-1 (isoform p170) promoting cap-independent translation. During male tail morphogenesis, promotes apoptosis of the tail-spike cell downstream of ced-4 but independently of egl-1 and ced-9. By cleaving cnt-1, prevents the activation of the prosurvival akt-1/2 signaling pathway and thus promotes apoptosis. Downstream of ced-4, may play a role in sex- specific cell apoptosis by cleaving sex-determining protein fem-1. May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway. Cleaves ced-9 in vitro. Cleaves csp-2 isoform b resulting in the removal of the propeptide and the generation of csp-2 subunit p31 in vitro. Independently of its apoptotic role has additional functions. Probably by cleaving and thereby activating actin-severing protein gsnl-1, required for the elimination of transient presynaptic components during larval development downstream of egl-1, ced-9 and ced-4 pathway. Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), regulates temporal cell fate patterning during larval development. Acts in cell fate patterning by cleaving heterochronic protein lin-28, likely promoting its degradation. Also cleaves heterochronic protein lin-14 and exonuclease disl-2 in vitro. Downstream of calreticulin crt- 1 and ced-4 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy. Cleaves 14-3-3-like protein ftt-2, tubulin tbb-2 and calreticulin crt-1 in vitro. Plays also a role in resistance to S.typhimurium-mediated infection. {ECO:0000250|UniProtKB:P42573}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0008303;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0008656;
GO  GO:0097200;
GO  GO:0042802;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0046716;
GO  GO:1905803;
GO  GO:1900118;
GO  GO:1904747;
GO  GO:1905845;
GO  GO:0043525;
GO  GO:1901046;
GO  GO:0010954;
GO  GO:1905808;
GO  GO:0016540;
GO  GO:0030163;
GO  GO:0030155;
GO  GO:0042659;
GO  GO:0040034;
GO  GO:0040012;
GO  GO:0031647;
GO  GO:0040028;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMRQDRRNLLERNILVFSNKLQSEQILEVLIAKQILNADNGDVINSCRTERDKRKEIVKAVQRRGDVAFDAFYDALRDTG
SQ  HHELAAVLEPLARTIDFITPRDLECPMSPASHRRSRALSPSTFSSPTRVHRDSVSSVSSFTSTYQDVYTRARSTSRSSRP
SQ  LHASDRHNYVSPSNSFQSQPSSANSSFTGCSSLGYSSSRTRSYSKASAHSQYIFHEEDMNYVDAPTIHRVFDEKTMYRNF
SQ  STPRGLCLIINNEHFEQMPTRNGTKADKDNISNLFRCMGYIVHCKDNLTGRAMMLTIRDFAKNETHGDSAILVILSHGEE
SQ  NVIIGVDDVSVNVHEIYDLLNAANAPRLANKPKLVFVQACRGERRDNGFPVLDSVDGVPALIRPRGWDKGDGPLFNFLGC
SQ  VRPQAQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSLHAKDMDVVELLTEVNKKVACGFQTSQGANI
SQ  LKQMPELTSRLLKKFYFWPEDRNRSSAV
//