ID  P42573;
PN  Cell death protein 3 subunit p13;
GN  ced;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:27723735}. Perikaryon {ECO:0000269|PubMed:26074078}. Synapse {ECO:0000269|PubMed:26074078}. Mitochondrion {ECO:0000269|PubMed:26074078}. Cytoplasm {ECO:0000269|PubMed:27723735}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27723735}. Note=Colocalizes with nucleoporin npp-14 to the perinuclear region in germ cells (PubMed:27723735). Becomes diffused in the cytoplasm in apoptotic germ cells (PubMed:27723735). Localizes to axonal mitochondria and synapses of DD motor neurons (PubMed:26074078). Synaptic localization is dependent on axonal mitochondria (PubMed:26074078). {ECO:0000269|PubMed:26074078, ECO:0000269|PubMed:27723735}.
DR  UNIPROT: P42573;
DR  UNIPROT: P45435;
DR  UNIPROT: Q9GQQ4;
DR  UNIPROT: Q9NAQ8;
DR  PDB: 4M9R;
DR  PDB: 4M9S;
DR  PDB: 4M9X;
DR  PDB: 4M9Y;
DR  PDB: 4M9Z;
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 (PubMed:8654923, PubMed:3955651, PubMed:18722182, PubMed:26074078, PubMed:27723735). 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, PubMed:17329362, PubMed:25432023, PubMed:27723735). During oogenesis, required for germline apoptosis downstream of ced-9 and ced-4 but independently of egl-1 (PubMed:9927601). 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 (PubMed:24225442). By cleaving and converting dcr-1 into a deoxyribonuclease (DNase), promotes apoptotic chromosomal DNA fragmentation (PubMed:20223951). By cleaving mitochondrial fission protein drp-1, may regulate the removal of mitochondria during apoptosis (PubMed:18722182). During germline apoptosis, cleaves translation initiation factor ifg-1 (isoform p170) promoting cap- independent translation (PubMed:21909434). During male tail morphogenesis, promotes apoptosis of the tail-spike cell downstream of ced-4 but independently of egl-1 and ced-9 (PubMed:17329362). By cleaving cnt-1, prevents the activation of the prosurvival akt-1/2 signaling pathway and thus promotes apoptosis (PubMed:25383666). Downstream of ced-4, may play a role in sex-specific cell apoptosis by cleaving sex-determining protein fem-1 (PubMed:10764728). May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway (PubMed:21901106). Cleaves ced-9 in vitro (PubMed:17371877, PubMed:18776901, PubMed:19575016, PubMed:25432023, PubMed:27723735). Cleaves csp-2 isoform b resulting in the removal of the propeptide and the generation of csp-2 subunit p31 in vitro (PubMed:9857046). 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 (PubMed:26074078). Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), regulates temporal cell fate patterning during larval development (PubMed:25432023). In complex with ubr-1, which is E3 ubiquitin-protein ligase and component of the N-end rule pathway, acts in seam cell fate patterning during larval development by cleaving the heterochronic protein lin-28, and promoting its degradation (PubMed:25432023, PubMed:28602583). Also cleaves heterochronic protein lin-14 and exonuclease disl-2 in vitro (PubMed:25432023). 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 (PubMed:22629231). Cleaves 14-3-3- like protein ftt-2, tubulin tbb-2 and calreticulin crt-1 in vitro (PubMed:17371877). Also plays 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:17371877, ECO:0000269|PubMed:18722182, ECO:0000269|PubMed:18776901, ECO:0000269|PubMed:19575016, ECO:0000269|PubMed:20223951, ECO:0000269|PubMed:21901106, ECO:0000269|PubMed:21909434, ECO:0000269|PubMed:22629231, ECO:0000269|PubMed:24225442, ECO:0000269|PubMed:25383666, ECO:0000269|PubMed:25432023, ECO:0000269|PubMed:26074078, ECO:0000269|PubMed:27723735, ECO:0000269|PubMed:28602583, ECO:0000269|PubMed:3955651, ECO:0000269|PubMed:8654923, ECO:0000269|PubMed:9857046, ECO:0000269|PubMed:9927601}.
DE  Reference Proteome: Yes;
DE  Interaction: P30429; IntAct: EBI-494268; Score: 0.86
DE  Interaction: Q8STE5; IntAct: EBI-8001700; Score: 0.37
DE  Interaction: P41958; IntAct: EBI-494631; Score: 0.70
DE  Interaction: P42573; IntAct: EBI-2655158; Score: 0.75
DE  Interaction: G5ECW5; IntAct: EBI-15727540; Score: 0.60
DE  Interaction: Q9XXH8; IntAct: EBI-16127213; Score: 0.44
DE  Interaction: Q9NAG4; IntAct: EBI-16587378; Score: 0.35
GO  GO:0070161;
GO  GO:0008303;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0031965;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0008656;
GO  GO:0004197;
GO  GO:0097153;
GO  GO:0097199;
GO  GO:0097200;
GO  GO:0004175;
GO  GO:0042802;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0097194;
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:0012501;
GO  GO:0016540;
GO  GO:0030163;
GO  GO:0006508;
GO  GO:0030155;
GO  GO:0042659;
GO  GO:0040034;
GO  GO:0040012;
GO  GO:0031647;
GO  GO:0050807;
GO  GO:0040028;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMRQDRRSLLERNIMMFSSHLKVDEILEVLIAKQVLNSDNGDMINSCGTVREKRREIVKAVQRRGDVAFDAFYDALRSTG
SQ  HEGLAEVLEPLARSVDSNAVEFECPMSPASHRRSRALSPAGYTSPTRVHRDSVSSVSSFTSYQDIYSRARSRSRSRALHS
SQ  SDRHNYSSPPVNAFPSQPSSANSSFTGCSSLGYSSSRNRSFSKASGPTQYIFHEEDMNFVDAPTISRVFDEKTMYRNFSS
SQ  PRGMCLIINNEHFEQMPTRNGTKADKDNLTNLFRCMGYTVICKDNLTGRGMLLTIRDFAKHESHGDSAILVILSHGEENV
SQ  IIGVDDIPISTHEIYDLLNAANAPRLANKPKIVFVQACRGERRDNGFPVLDSVDGVPAFLRRGWDNRDGPLFNFLGCVRP
SQ  QVQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSTHAKDMDVVELLTEVNKKVACGFQTSQGSNILKQ
SQ  MPEMTSRLLKKFYFWPEARNSAV
//