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Full view of all proteins: here.
CED-1 The ced-1 gene encodes a transmembrane protein on phagocytic cells that is homologous to human CD91, a low density lipoprotein receptor paralog. the cytoplasmic tail of CED-1 contains two motifs important for engulfment. [Source: WormBase] manually curated
CED-3 The ced-3 gene encodes a protease required for apoptosis. [Source: WormBase] manually curated
CED-4 ced-4 encodes a novel protein. along with CED-3, CED-4 is required for the initiation of programmed cell death. accordingly, genetic analyses indicate that ced-3 and ced-4 function upstream of ced-1, ced-2, and nuc-1 in the programmed cell death pathway. in yeast two-hybrid experiments, and upon coexpression in mammalian cells, CED-4 interacts with CED-9, an anti-apoptotic BCL-2 homolog. coexpression of CED-4 and CED-9 results in redistribution of CED-4 from the cytosol to organellar membranes, suggesting that CED-9 may negatively regulate CED-4 activity by sequestering CED-4 to intracellular membranes. [Source: WormBase] manually curated
CED-8 The ced-8 gene encodes a homolog of the human putative membrane transporter XK. ced-8 is required for apoptosis to occur with normal speed during embryonic development. [Source: WormBase] manually curated
CED-9 ced-9 encodes the sole C. elegans homolog of the mammalian cell-death inhibitor Bcl-2. during development, CED-9 activity is essential for preventing cells from undergoing programmed cell death and CED-9 functions by binding and repressing the activity of CED-4, a protein similar to human APAF-1 that positively regulates CED-3 caspase activity. CED-9 localizes to mitochondria. [Source: WormBase] manually curated
CEP-1 TRANSCRIPTION FACTOR CEP-1, C.ELEGANS P53-LIKE PROTEIN 1 Ancestral member of the p53 family (p53, p63, p73) manually curated
CSP-3 csp-3 encodes a protein that is homologous to the C-terminal domain of caspase-like cysteine proteases. unlike other caspases, CSP-3 does not contain a middle or N-terminal domain, and thus may either function in concert with the middle domains of other caspases or may play a regulatory (dominant negative) role in caspase activation. [Source: WormBase] manually curated
DCT-1 dct-1 encodes a protein with similarity to the mammalian BNIP3 proteins that interact with Bcl-2 and the Adenovirus E1B 19kDa protein and that have been shown to have pro-apoptotic activity. loss of dct-1 activity via RNAi in daf-2 mutants and in gld-1. daf-2 doubly mutant animals indicates that dct-1 can function to regulate both lifespan and tumor cell proliferation. when expressed in mammalian cells, DCT-1 can: 1) induce delayed apoptosis and increase apoptosis when coexpressed with CED-3 (perhaps by increasing proteolyic processing of CED-3), 2) physically interact with CED-9 or the CED-3 prodomain when coexpressed, and 3) physically interact with both CED-9 and CED-3 when all three are coexpressed. chromatin immunoprecipitation experiments have demonstrated that the dct-1 promoter is bound in vivo by the forkhead transcription factor DAF-16. expression of DCT-1 in mammalian cells suggests that, like its mammalian orthologs, DCT-1 localizes to mitochondria via a predicted C-terminal transmembrane domain. [Source: WormBase] manually curated
EGL-1 egl-1 encodes a novel protein that contains a region similar to the BH3 (Bcl-2 homology region 3) domain of mammalian cell death activators. EGL-1 functions as an upstream activator in the general programmed cell death pathway and positively regulates programmed cell death by interacting directly with CED-9 to induce CED-4 release from CED-4/CED-9 complexes and ultimately activate the CED-3 caspase. EGL-1 also induces WAH-1/apoptosis-inducing factor release from the mitochondria. in hermaphrodites, egl-1 is transcriptionally repressed by TRA-1, permitting survival of the HSN neurons required for egg laying. egl-1 message is detected at low abundance in embryonic and L1 larval mRNA preparations, but not in mRNA preparations from later larval stages or young adults. [Source: WormBase] manually curated
NEX-1 nex-1 encodes an annexin, a member of a family of calcium-dependent phospholipid binding proteins. NEX-1 is required for efficient engulfment of apoptotic cell corpses in the pharynx, and may also function in other membrane fusion events, such as exocytosis. NEX-1 in vitro can bind phosphatidylserine, phosphatidylinositol, heparin, heparan sulfate, and chondroitin sulfate. NEX-1 is expressed in the pharynx, hypodermal cells, the vulva, the uterus, the spermathecal valve, and yolk granules of maturing oocytes. [Source: WormBase] manually curated
WAH-1 wah-1 encodes a putative flavin-adenine dinucleotide (FAD)-binding oxidoreductase orthologous to mammalian PDCD8 (AIF. OMIM:300169, mutated in Harlequin mice). WAH-1 is required for apoptotic DNA degratation, SCRM-1 phospholipid scramblase activity, phosphatidylserine exposure, rapid apoptosis during embryonic development, and rapid engulfment of apoptotic cells in the germline. WAH-1 is also required for normally rapid growth and large brood sizes, and has a subtle proapoptotic function revealed in ced-3 or ced-4 mutant backgrounds. WAH-1 is expressed in most, if not all, cells of embryos and larvae. WAH-1 is normally mitochondrial, but can be released into the cytosol and nucleus by EGL-1 and CED-3. residues 380-550 of WAH-1 specifically bind SCRM-1 in vitro, but not SCRM-2 through SCRM-4, and WAH-1 binding is required in liposomes for more than residual SCRM-1 activity. WAH-1 also binds and activates CPS-6, promoting apoptotic DNA degradation, and transgenic coexpression of WAH-1 with CPS-6 specifically induces ectopic CED-3-dependent apoptosis in touch receptor neurons. CPS-6 shares a genetic pathway with WAH-1, whereas CED-3, CED-4, CED-8, and NUC-1 act independently of it. WAH-1 is paralogous to C. elegans F20D6.11 and human AIFM3 (AIFL). [Source: WormBase] manually curated Uniprot