GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]

 CED3_CAEEL              Reviewed;         503 AA.
P42573; P45435; Q9GQQ4; Q9NAQ8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
14-AUG-2001, sequence version 2.
08-MAY-2019, entry version 160.
RecName: Full=Cell death protein 3;
EC=3.4.22.60 {ECO:0000269|PubMed:18776901, ECO:0000269|PubMed:19575016, ECO:0000269|PubMed:25383666, ECO:0000269|PubMed:25432023, ECO:0000269|PubMed:27723735, ECO:0000269|PubMed:8654923, ECO:0000269|PubMed:9857046};
AltName: Full=Caspase ced-3 {ECO:0000305};
Contains:
RecName: Full=Cell death protein 3 subunit p17 {ECO:0000305|PubMed:8654923};
Contains:
RecName: Full=Cell death protein 3 subunit p15 {ECO:0000305|PubMed:8654923};
Contains:
RecName: Full=Cell death protein 3 subunit p13 {ECO:0000305|PubMed:8654923};
Flags: Precursor;
Name=ced-3 {ECO:0000312|WormBase:C48D1.2a};
ORFNames=C48D1.2 {ECO:0000312|WormBase:C48D1.2a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DEVELOPMENTAL STAGE.
STRAIN=Bristol N2;
PubMed=8242740; DOI=10.1016/0092-8674(93)90485-9;
Yuan J., Shaham S., Ledoux S., Ellis H.M., Horvitz H.R.;
"The C. elegans cell death gene ced-3 encodes a protein similar to
mammalian interleukin-1 beta-converting enzyme.";
Cell 75:641-652(1993).
[2]
SEQUENCE REVISION TO 418.
Horvitz H.R.;
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
REGULATION, PROTEOLYTIC CLEAVAGE, ACTIVE SITE, AND MUTAGENESIS OF
CYS-358; GLY-360; ALA-449 AND GLY-474.
PubMed=8654923; DOI=10.1101/gad.10.9.1073;
Xue D., Shaham S., Horvitz H.R.;
"The Caenorhabditis elegans cell-death protein CED-3 is a cysteine
protease with substrate specificities similar to those of the human
CPP32 protease.";
Genes Dev. 10:1073-1083(1996).
[5]
FUNCTION, AND MUTAGENESIS OF LEU-27; GLY-65 AND ALA-449.
PubMed=3955651;
Ellis H.M., Horvitz H.R.;
"Genetic control of programmed cell death in the nematode C.
elegans.";
Cell 44:817-829(1986).
[6]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PROTEOLYTIC
CLEAVAGE, ACTIVE SITE, AND MUTAGENESIS OF CYS-358.
STRAIN=Bristol N2;
PubMed=9857046; DOI=10.1074/jbc.273.52.35109;
Shaham S.;
"Identification of multiple Caenorhabditis elegans caspases and their
potential roles in proteolytic cascades.";
J. Biol. Chem. 273:35109-35117(1998).
[7]
FUNCTION.
PubMed=9927601;
Gumienny T.L., Lambie E., Hartwieg E., Horvitz H.R., Hengartner M.O.;
"Genetic control of programmed cell death in the Caenorhabditis
elegans hermaphrodite germline.";
Development 126:1011-1022(1999).
[8]
IDENTIFICATION IN A CED-3; CED-4 AND MAC-1 COMPLEX.
PubMed=10101135;
Wu D., Chen P.J., Chen S., Hu Y., Nunez G., Ellis R.E.;
"C. elegans MAC-1, an essential member of the AAA family of ATPases,
can bind CED-4 and prevent cell death.";
Development 126:2021-2031(1999).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10764728; DOI=10.1074/jbc.C000146200;
Chan S.L., Yee K.S., Tan K.M., Yu V.C.;
"The Caenorhabditis elegans sex determination protein FEM-1 is a CED-3
substrate that associates with CED-4 and mediates apoptosis in
mammalian cells.";
J. Biol. Chem. 275:17925-17928(2000).
[10]
INTERACTION WITH DCT-1.
PubMed=11114722; DOI=10.1038/sj.onc.1203929;
Cizeau J., Ray R., Chen G., Gietz R.D., Greenberg A.H.;
"The C. elegans orthologue ceBNIP3 interacts with CED-9 and CED-3 but
kills through a BH3- and caspase-independent mechanism.";
Oncogene 19:5453-5463(2000).
[11]
FUNCTION, AND MUTAGENESIS OF GLY-360.
PubMed=11226309; DOI=10.1073/pnas.041613098;
Aballay A., Ausubel F.M.;
"Programmed cell death mediated by ced-3 and ced-4 protects
Caenorhabditis elegans from Salmonella typhimurium-mediated killing.";
Proc. Natl. Acad. Sci. U.S.A. 98:2735-2739(2001).
[12]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=17329362; DOI=10.1242/dev.02818;
Maurer C.W., Chiorazzi M., Shaham S.;
"Timing of the onset of a developmental cell death is controlled by
transcriptional induction of the C. elegans ced-3 caspase-encoding
gene.";
Development 134:1357-1368(2007).
[13]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PROTEOLYTIC
CLEAVAGE.
PubMed=17371877; DOI=10.1074/jbc.M611051200;
Taylor R.C., Brumatti G., Ito S., Hengartner M.O., Derry W.B.,
Martin S.J.;
"Establishing a blueprint for CED-3-dependent killing through
identification of multiple substrates for this protease.";
J. Biol. Chem. 282:15011-15021(2007).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-474.
PubMed=18722182; DOI=10.1016/j.molcel.2008.07.015;
Breckenridge D.G., Kang B.H., Kokel D., Mitani S., Staehelin L.A.,
Xue D.;
"Caenorhabditis elegans drp-1 and fis-2 regulate distinct cell-death
execution pathways downstream of ced-3 and independent of ced-9.";
Mol. Cell 31:586-597(2008).
[15]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH
CSP-3, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF GLY-474.
PubMed=18776901; DOI=10.1038/nsmb.1488;
Geng X., Shi Y., Nakagawa A., Yoshina S., Mitani S., Shi Y., Xue D.;
"Inhibition of CED-3 zymogen activation and apoptosis in
Caenorhabditis elegans by caspase homolog CSP-3.";
Nat. Struct. Mol. Biol. 15:1094-1101(2008).
[16]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH
CSP-2, AND PROTEOLYTIC CLEAVAGE.
PubMed=19575016; DOI=10.1038/cdd.2009.88;
Geng X., Zhou Q.H., Kage-Nakadai E., Shi Y., Yan N., Mitani S.,
Xue D.;
"Caenorhabditis elegans caspase homolog CSP-2 inhibits CED-3
autoactivation and apoptosis in germ cells.";
Cell Death Differ. 16:1385-1394(2009).
[17]
CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH CED-4, AND
PROTEOLYTIC CLEAVAGE.
PubMed=20434985; DOI=10.1016/j.cell.2010.03.017;
Qi S., Pang Y., Hu Q., Liu Q., Li H., Zhou Y., He T., Liang Q.,
Liu Y., Yuan X., Luo G., Li H., Wang J., Yan N., Shi Y.;
"Crystal structure of the Caenorhabditis elegans apoptosome reveals an
octameric assembly of CED-4.";
Cell 141:446-457(2010).
[18]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20223951; DOI=10.1126/science.1182374;
Nakagawa A., Shi Y., Kage-Nakadai E., Mitani S., Xue D.;
"Caspase-dependent conversion of Dicer ribonuclease into a death-
promoting deoxyribonuclease.";
Science 328:327-334(2010).
[19]
FUNCTION.
PubMed=21901106; DOI=10.1371/journal.pgen.1002238;
Rutkowski R., Dickinson R., Stewart G., Craig A., Schimpl M.,
Keyse S.M., Gartner A.;
"Regulation of Caenorhabditis elegans p53/CEP-1-dependent germ cell
apoptosis by Ras/MAPK signaling.";
PLoS Genet. 7:E1002238-E1002238(2011).
[20]
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=21909434; DOI=10.1371/journal.pone.0024444;
Contreras V., Friday A.J., Morrison J.K., Hao E., Keiper B.D.;
"Cap-independent translation promotes C. elegans germ cell apoptosis
through Apaf-1/CED-4 in a caspase-dependent mechanism.";
PLoS ONE 6:E24444-E24444(2011).
[21]
FUNCTION, AND MUTAGENESIS OF GLY-360.
PubMed=22629231; DOI=10.1371/journal.pbio.1001331;
Pinan-Lucarre B., Gabel C.V., Reina C.P., Hulme S.E.,
Shevkoplyas S.S., Slone R.D., Xue J., Qiao Y., Weisberg S.,
Roodhouse K., Sun L., Whitesides G.M., Samuel A., Driscoll M.;
"The core apoptotic executioner proteins CED-3 and CED-4 promote
initiation of neuronal regeneration in Caenorhabditis elegans.";
PLoS Biol. 10:E1001331-E1001331(2012).
[22]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24225442; DOI=10.1038/ncomms3726;
Chen Y.Z., Mapes J., Lee E.S., Skeen-Gaar R.R., Xue D.;
"Caspase-mediated activation of Caenorhabditis elegans CED-8 promotes
apoptosis and phosphatidylserine externalization.";
Nat. Commun. 4:2726-2726(2013).
[23]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND DISRUPTION
PHENOTYPE.
PubMed=25432023; DOI=10.7554/eLife.04265;
Weaver B.P., Zabinsky R., Weaver Y.M., Lee E.S., Xue D., Han M.;
"CED-3 caspase acts with miRNAs to regulate non-apoptotic gene
expression dynamics for robust development in C. elegans.";
Elife 3:E04265-E04265(2014).
[24]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=25383666; DOI=10.1038/nsmb.2915;
Nakagawa A., Sullivan K.D., Xue D.;
"Caspase-activated phosphoinositide binding by CNT-1 promotes
apoptosis by inhibiting the AKT pathway.";
Nat. Struct. Mol. Biol. 21:1082-1090(2014).
[25]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
GLY-366.
PubMed=26074078; DOI=10.1016/j.celrep.2015.05.031;
Meng L., Mulcahy B., Cook S.J., Neubauer M., Wan A., Jin Y., Yan D.;
"The cell death pathway regulates synapse elimination through cleavage
of gelsolin in Caenorhabditis elegans neurons.";
Cell Rep. 11:1737-1748(2015).
[26]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH
NPP-14, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
LEU-27; LEU-30; ARG-51; GLY-65 AND GLY-360.
PubMed=27723735; DOI=10.1038/nsmb.3308;
Chen X., Wang Y., Chen Y.Z., Harry B.L., Nakagawa A., Lee E.S.,
Guo H., Xue D.;
"Regulation of CED-3 caspase localization and activation by C. elegans
nuclear-membrane protein NPP-14.";
Nat. Struct. Mol. Biol. 23:958-964(2016).
[27]
FUNCTION, IDENTIFICATION IN COMPLEX WITH ATE-1 AND UBR-1, AND
MUTAGENESIS OF CYS-358.
PubMed=28602583; DOI=10.1016/j.devcel.2017.05.013;
Weaver B.P., Weaver Y.M., Mitani S., Han M.;
"Coupled Caspase and N-End Rule Ligase Activities Allow Recognition
and Degradation of Pluripotency Factor LIN-28 during Non-Apoptotic
Development.";
Dev. Cell 41:665-673(2017).
[28]
X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 198-503 IN COMPLEX WITH
CED-4, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, REGION, ACTIVE
SITE, AND MUTAGENESIS OF CYS-358 AND 391-LEU--ASN-393.
PubMed=24065769; DOI=10.1101/gad.224428.113;
Huang W., Jiang T., Choi W., Qi S., Pang Y., Hu Q., Xu Y., Gong X.,
Jeffrey P.D., Wang J., Shi Y.;
"Mechanistic insights into CED-4-mediated activation of CED-3.";
Genes Dev. 27:2039-2048(2013).
-!- 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 calrecticulin crt-1 in vitro (PubMed:17371877). Plays also 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}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for an Asp residue at position P1 and
has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.;
EC=3.4.22.60; Evidence={ECO:0000269|PubMed:10764728,
ECO:0000269|PubMed:17371877, ECO:0000269|PubMed:18722182,
ECO:0000269|PubMed:18776901, ECO:0000269|PubMed:19575016,
ECO:0000269|PubMed:20223951, ECO:0000269|PubMed:21909434,
ECO:0000269|PubMed:24065769, ECO:0000269|PubMed:24225442,
ECO:0000269|PubMed:25383666, ECO:0000269|PubMed:25432023,
ECO:0000269|PubMed:27723735, ECO:0000269|PubMed:8654923,
ECO:0000269|PubMed:9857046, ECO:0000305|PubMed:26074078};
-!- ACTIVITY REGULATION: Octomeric ced-4 activates zymogen
autoprocessing and enhances activity of processed ced-3
(PubMed:18776901, PubMed:19575016, PubMed:27723735,
PubMed:24065769, PubMed:20434985). Zymogen autoactivation is
inhibited by csp-3 (PubMed:18776901). csp-3 has no effect on
active ced-3 (PubMed:18776901). Zymogen autoactivation is
inhibited by csp-2 (PubMed:19575016). Inhibited by cysteine
protease inhibitor iodoacetic acid (CH3COOI) (PubMed:8654923,
PubMed:9857046, PubMed:18776901, PubMed:19575016,
PubMed:27723735). Inhibited by benzyloxycarbonyl-DEVD-fluoro-
methyl ketone (zDEVD-fmk) (PubMed:8654923, PubMed:9857046,
PubMed:25432023). Inhibited by benzyloxycarbonyl-VAD-fluoro-methyl
ketone (zVAD-fmk) (PubMed:17371877, PubMed:21909434). Not
inhibited by N-[N-(L-3-transcarboxirane-2-carbonyl)-leucyl]-
agmatine (E-64) or by the serine and cysteine protease inhibitor
L-1-chloro-3-[4-to-osylamido]-7-amino-2-heptanone (TLCK)
(PubMed:8654923, PubMed:9857046). {ECO:0000269|PubMed:17371877,
ECO:0000269|PubMed:18776901, ECO:0000269|PubMed:19575016,
ECO:0000269|PubMed:20434985, ECO:0000269|PubMed:21909434,
ECO:0000269|PubMed:24065769, ECO:0000269|PubMed:25432023,
ECO:0000269|PubMed:27723735, ECO:0000269|PubMed:8654923,
ECO:0000269|PubMed:9857046}.
-!- SUBUNIT: The active form is probably a heterodimer of the p17
subunit with either the p15 or p13 subunit which are all derived
from the precursor by autocatalysis (Probable). Interacts with
octomeric ced-4 (two ced-3 zymogens per one ced-4 octamer); the
interaction causes the autoproteolytic cleavage and activation of
ced-3 (PubMed:20434985, PubMed:24065769). Processed ced-3 also
interacts with ced-4 octamer to form a stable holoenzyme
(PubMed:20434985). Interacts (via large subunit p17) with csp-3;
the interaction prevents ced-3 autoactivation and delays ced-4-
induced ced-3 processing (PubMed:18776901). Interacts (via large
subunit p17 or small subunit p13 or p15) with csp-2; the
interaction inhibits ced-3 autoactivation (PubMed:19575016).
Interacts (via propeptide) with nucleoporin npp-14; the
interaction tethers ced-3 to the nuclear membrane and prevents its
autoprocessing in absence of ced-4 (PubMed:27723735). Interacts
with dct-1 (PubMed:11114722). May form a complex composed of ced-
3, ced-4 and mac-1 (PubMed:10101135). Component of a complex
containing at least ced-3, ubr-1 and possibly ate-1
(PubMed:28602583). Within complex interacts (via the p17 subunit)
with ubr-1; this interaction is required for the ced-3-mediated
cleavage and subsequent degradation of the heterochronic protein
lin-28 (PubMed:28602583). Interacts with ate-1 (isoform a and
isoform d); interaction with ate-1 (isoform a) is in the presence
or absent of ubr-1 (PubMed:28602583).
{ECO:0000269|PubMed:10101135, ECO:0000269|PubMed:11114722,
ECO:0000269|PubMed:18776901, ECO:0000269|PubMed:19575016,
ECO:0000269|PubMed:20434985, ECO:0000269|PubMed:24065769,
ECO:0000269|PubMed:27723735, ECO:0000269|PubMed:28602583,
ECO:0000305}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-494247, EBI-494247;
P30429:ced-4; NbExp=10; IntAct=EBI-494247, EBI-494118;
P30429-2:ced-4; NbExp=13; IntAct=EBI-494247, EBI-536271;
P41958:ced-9; NbExp=4; IntAct=EBI-494247, EBI-494110;
G5ECW5:csp-3; NbExp=3; IntAct=EBI-494247, EBI-15727537;
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000269|PubMed:27723735}. Perikaryon
{ECO:0000269|PubMed:26074078}. Cell junction, 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}.
-!- DEVELOPMENTAL STAGE: Highly expressed in embryos and to a lesser
extent in adults (PubMed:8242740). Expression is low throughout
the larval stage (PubMed:8242740). Expressed in all cells, except
intestinal cells and their precursors, starting at around 100-150
minutes post-fertilization and continuing throughout the comma
stage of embryogenesis (PubMed:17329362). Not expressed after the
3-fold embryonic stage, and only expressed in 2-3 cells in larvae
and adults (PubMed:17329362). In males, expressed in the tail at
the L4 larval stage (PubMed:17329362). Expression in the tail-
spike cell is restricted to the 3-fold embryonic stage prior to
the tail-spike cell death (PubMed:17329362).
{ECO:0000269|PubMed:17329362, ECO:0000269|PubMed:8242740}.
-!- DOMAIN: The CARD domain is involved in ced-4 binding.
{ECO:0000269|PubMed:24065769}.
-!- PTM: Autocatalytic cleavage removes the propeptide and generates
the catalytic subunit p17 and two non-catalytic subunits p15 and
p13; autoproteolysis is induced by ced-4 oligomer (PubMed:8654923,
PubMed:9857046, PubMed:17371877, PubMed:18776901, PubMed:19575016,
PubMed:27723735, PubMed:20434985). Cleaved by caspase csp-1
probably at Asp-144 and Asp-374 (PubMed:9857046).
{ECO:0000269|PubMed:18776901, ECO:0000269|PubMed:19575016,
ECO:0000269|PubMed:20434985, ECO:0000269|PubMed:27723735,
ECO:0000269|PubMed:8654923, ECO:0000269|PubMed:9857046}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a rupture of
the vulva and an increase in laid oocytes in a small proportion of
animals. In an ain-1 mutant background, enhances the proportion of
animals arrested at the larval stage, with egg-laying defects and
with a ruptured vulva. {ECO:0000269|PubMed:25432023}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L29052; AAA27982.2; -; Genomic_DNA.
EMBL; AF210702; AAG42045.1; -; mRNA.
EMBL; BX284604; CAB61001.2; -; Genomic_DNA.
PIR; A49429; A49429.
RefSeq; NP_001255708.1; NM_001268779.1.
PDB; 4M9R; X-ray; 2.66 A; A/B=198-503.
PDB; 4M9S; X-ray; 3.21 A; E/F/G/H=390-397.
PDB; 4M9X; X-ray; 3.34 A; C/D=390-395.
PDB; 4M9Y; X-ray; 4.20 A; C/D=390-397.
PDB; 4M9Z; X-ray; 3.40 A; E/F/G/H=390-397.
PDBsum; 4M9R; -.
PDBsum; 4M9S; -.
PDBsum; 4M9X; -.
PDBsum; 4M9Y; -.
PDBsum; 4M9Z; -.
SMR; P42573; -.
BioGrid; 43363; 6.
ComplexPortal; CPX-1358; ced-3-ced-4-mac-1 complex.
ComplexPortal; CPX-1360; ced-3-ced-4 caspase complex.
DIP; DIP-244N; -.
IntAct; P42573; 6.
MINT; P42573; -.
STRING; 6239.C48D1.2a; -.
ChEMBL; CHEMBL1250361; -.
MEROPS; C14.002; -.
EPD; P42573; -.
PaxDb; P42573; -.
PeptideAtlas; P42573; -.
EnsemblMetazoa; C48D1.2a; C48D1.2a; WBGene00000417.
GeneID; 178272; -.
KEGG; cel:CELE_C48D1.2; -.
UCSC; C48D1.2; c. elegans.
CTD; 178272; -.
WormBase; C48D1.2a; CE29088; WBGene00000417; ced-3.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000171812; -.
HOGENOM; HOG000016385; -.
InParanoid; P42573; -.
KO; K20106; -.
OMA; GYTVICK; -.
OrthoDB; 1092723at2759; -.
PhylomeDB; P42573; -.
Reactome; R-CEL-5660668; CLEC7A/inflammasome pathway.
Reactome; R-CEL-6798695; Neutrophil degranulation.
PRO; PR:P42573; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00000417; Expressed in 5 organ(s), highest expression level in adult organism.
ExpressionAtlas; P42573; baseline and differential.
GO; GO:0008303; C:caspase complex; IMP:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:WormBase.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
GO; GO:0098793; C:presynapse; IDA:UniProtKB.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:WormBase.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:WormBase.
GO; GO:0004175; F:endopeptidase activity; IDA:WormBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030042; P:actin filament depolymerization; IMP:UniProtKB.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:1902742; P:apoptotic process involved in development; IMP:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; IDA:WormBase.
GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:UniProtKB.
GO; GO:1905803; P:negative regulation of cellular response to manganese ion; IMP:UniProtKB.
GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IMP:UniProtKB.
GO; GO:1905845; P:positive regulation of cellular response to gamma radiation; IMP:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
GO; GO:0010954; P:positive regulation of protein processing; IMP:UniProtKB.
GO; GO:1905808; P:positive regulation of synapse pruning; IMP:UniProtKB.
GO; GO:0012501; P:programmed cell death; IMP:WormBase.
GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
GO; GO:0030163; P:protein catabolic process; IDA:WormBase.
GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0042659; P:regulation of cell fate specification; IGI:UniProtKB.
GO; GO:0040034; P:regulation of development, heterochronic; IGI:UniProtKB.
GO; GO:0040012; P:regulation of locomotion; IGI:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IGI:UniProtKB.
GO; GO:0050807; P:regulation of synapse organization; IGI:UniProtKB.
GO; GO:0040028; P:regulation of vulval development; IGI:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Autocatalytic cleavage; Cell junction;
Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
Membrane; Mitochondrion; Nucleus; Protease; Reference proteome;
Synapse; Thiol protease; Zymogen.
PROPEP 1 221 {ECO:0000269|PubMed:8654923}.
/FTId=PRO_0000441117.
CHAIN 222 374 Cell death protein 3 subunit p17.
{ECO:0000305}.
/FTId=PRO_0000004674.
CHAIN 375 503 Cell death protein 3 subunit p15.
{ECO:0000305}.
/FTId=PRO_0000004675.
CHAIN 389 503 Cell death protein 3 subunit p13.
{ECO:0000305}.
/FTId=PRO_0000441118.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
REGION 389 404 Required for interaction with ced-4.
{ECO:0000269|PubMed:24065769}.
ACT_SITE 315 315 {ECO:0000250|UniProtKB:P29466}.
ACT_SITE 358 358 {ECO:0000269|PubMed:24065769,
ECO:0000269|PubMed:8654923,
ECO:0000269|PubMed:9857046}.
SITE 221 222 Cleavage; by autolysis.
{ECO:0000269|PubMed:8654923}.
SITE 374 375 Cleavage; by autolysis.
{ECO:0000269|PubMed:8654923}.
SITE 388 389 Cleavage; by autolysis.
{ECO:0000269|PubMed:8654923}.
MUTAGEN 27 27 L->F: In n1040; increased autoprocessing
in absence of ced-4. Autoprocessing is
blocked in presence of npp-14 and reduced
in presence of both ced-4 and npp-14.
Loss of embryonic and postembryonic
apoptosis resulting in survival of cells
in the head, ventral cord, postdeirid
sensilla and Q descendants in a ced-1
mutant background defective in cell-
corpse clearance. Apoptosis is partially
restored in a ced-1 (e1735) and npp-14
(sm160) double mutant background.
{ECO:0000269|PubMed:27723735,
ECO:0000269|PubMed:3955651}.
MUTAGEN 30 30 L->F: In n2439; increased autoprocessing
in absence of ced-4. Autoprocessing is
blocked in presence of npp-14 and reduced
in presence of both ced-4 and npp-14.
Loss of embryonic and postembryonic
apoptosis resulting in survival of cells
in the anterior pharynx in a ced-1 mutant
background defective in cell-corpse
clearance. Apoptosis is partially
restored in a ced-1 (e1735) and npp-14
(sm160) double mutant background.
{ECO:0000269|PubMed:27723735}.
MUTAGEN 51 51 R->H: In n2449; normal autoprocessing. No
effect on embryonic and postembryonic
apoptosis in a ced-1 mutant background
defective in cell-corpse clearance.
{ECO:0000269|PubMed:27723735}.
MUTAGEN 65 65 G->R: In n718; increased autoprocessing
in absence of ced-4. Autoprocessing is
blocked in presence of npp-14 and reduced
in presence of both ced-4 and npp-14.
Loss of embryonic and postembryonic
apoptosis resulting in survival of cells
in the head, ventral cord, postdeirid
sensilla and Q descendants in a ced-1
mutant background defective in cell-
corpse clearance. Apoptosis is partially
restored in a ced-1 (e1735) and npp-14
(sm160) double mutant background.
{ECO:0000269|PubMed:27723735,
ECO:0000269|PubMed:3955651}.
MUTAGEN 358 358 C->S: Loss of catalytic activity.
Prevents cell death. Loss of processing.
No effect on the interaction with ced-4.
Loss of interaction with octomeric ced-4;
when associated with 391-D--D-393.
{ECO:0000269|PubMed:24065769,
ECO:0000269|PubMed:28602583,
ECO:0000269|PubMed:8654923,
ECO:0000269|PubMed:9857046}.
MUTAGEN 360 360 G->S: In n2433; loss of catalytic
activity. Loss of processing. Severe
reduction in the number of apoptotic
cells in the anterior pharynx. Loss of
embryonic apoptosis in a ced-1 mutant
background defective in cell-corpse
clearance. Impaired axonal regeneration
following injury. Resistance to
S.typhimurium-mediated killing.
{ECO:0000269|PubMed:11226309,
ECO:0000269|PubMed:22629231,
ECO:0000269|PubMed:27723735,
ECO:0000269|PubMed:8654923}.
MUTAGEN 366 366 G->R: In ju1056; Loss of gsnl-1 cleavage.
Impaired elimination of presynaptic
components in RME neurons in adults.
Abnormal accumulation of F-actin at the
non-eliminated transient synapses in DD
neuron dorsal cord in L4 larvae.
{ECO:0000269|PubMed:26074078}.
MUTAGEN 391 393 LFN->DDD: Loss of interaction with
octomeric ced-4; when associated with S-
358. {ECO:0000269|PubMed:24065769}.
MUTAGEN 449 449 A->V: In n1229/n1164; severe reduction in
catalytic activity. Partially processed.
Reduction in the number of apoptotic
cells in the anterior pharynx. In a ced-1
mutant background, loss of embryonic and
postembryonic apoptosis resulting in
survival of cells in the head, ventral
cord, postdeirid sensilla, Q descendants
and cells of the anterior pharynx.
{ECO:0000269|PubMed:3955651,
ECO:0000269|PubMed:8654923}.
MUTAGEN 474 474 G->R: In n2427/n2438; slight reduction in
catalytic activity. Almost complete
processing. Slight reduction in the
number of apoptotic cells in the anterior
pharynx. Reduction is higher in a drp-1
or fis-2 mutant background. Reduction in
number of eggs laid. In a ced-9 (n1653)
mutant background, causes 60 percent
embryonic lethality.
{ECO:0000269|PubMed:18722182,
ECO:0000269|PubMed:18776901,
ECO:0000269|PubMed:8654923}.
HELIX 214 216 {ECO:0000244|PDB:4M9R}.
HELIX 222 228 {ECO:0000244|PDB:4M9R}.
TURN 231 233 {ECO:0000244|PDB:4M9R}.
STRAND 243 249 {ECO:0000244|PDB:4M9R}.
STRAND 254 256 {ECO:0000244|PDB:4M9R}.
HELIX 262 275 {ECO:0000244|PDB:4M9R}.
STRAND 278 285 {ECO:0000244|PDB:4M9R}.
HELIX 288 298 {ECO:0000244|PDB:4M9R}.
STRAND 306 317 {ECO:0000244|PDB:4M9R}.
STRAND 320 322 {ECO:0000244|PDB:4M9R}.
HELIX 331 336 {ECO:0000244|PDB:4M9R}.
TURN 340 342 {ECO:0000244|PDB:4M9R}.
STRAND 351 357 {ECO:0000244|PDB:4M9R}.
STRAND 360 362 {ECO:0000244|PDB:4M9R}.
TURN 411 414 {ECO:0000244|PDB:4M9R}.
STRAND 415 421 {ECO:0000244|PDB:4M9R}.
TURN 431 433 {ECO:0000244|PDB:4M9R}.
HELIX 436 448 {ECO:0000244|PDB:4M9R}.
TURN 449 451 {ECO:0000244|PDB:4M9R}.
HELIX 454 468 {ECO:0000244|PDB:4M9R}.
STRAND 471 473 {ECO:0000244|PDB:4M9R}.
STRAND 476 478 {ECO:0000244|PDB:4M9R}.
STRAND 483 486 {ECO:0000244|PDB:4M9R}.
STRAND 489 491 {ECO:0000244|PDB:4M9R}.
SEQUENCE 503 AA; 56617 MW; 722D5831F94DAA69 CRC64;
MMRQDRRSLL ERNIMMFSSH LKVDEILEVL IAKQVLNSDN GDMINSCGTV REKRREIVKA
VQRRGDVAFD AFYDALRSTG HEGLAEVLEP LARSVDSNAV EFECPMSPAS HRRSRALSPA
GYTSPTRVHR DSVSSVSSFT SYQDIYSRAR SRSRSRALHS SDRHNYSSPP VNAFPSQPSS
ANSSFTGCSS LGYSSSRNRS FSKASGPTQY IFHEEDMNFV DAPTISRVFD EKTMYRNFSS
PRGMCLIINN EHFEQMPTRN GTKADKDNLT NLFRCMGYTV ICKDNLTGRG MLLTIRDFAK
HESHGDSAIL VILSHGEENV IIGVDDIPIS THEIYDLLNA ANAPRLANKP KIVFVQACRG
ERRDNGFPVL DSVDGVPAFL RRGWDNRDGP LFNFLGCVRP QVQQVWRKKP SQADILIAYA
TTAQYVSWRN SARGSWFIQA VCEVFSTHAK DMDVVELLTE VNKKVACGFQ TSQGSNILKQ
MPEMTSRLLK KFYFWPEARN SAV


Related products :

Catalog number Product name Quantity
18-001-30077 Cell death activator CIDE-3 - Cell death-inducing DFFA-like effector protein C; Fat-specific protein FSP27 homolog Polyclonal 0.1 mg
EIAAB07403 Cell death activator CIDE-3,Cell death-inducing DFFA-like effector protein C,CIDEC,Fat-specific protein FSP27 homolog,FSP27,Homo sapiens,Human
EIAAB07404 Cell death activator CIDE-3,Cell death-inducing DFFA-like effector protein C,Cidec,Fat-specific protein FSP27,Fsp27,Mouse,Mus musculus
EIAAB30261 Death up-regulated gene protein,Dug,Pdcd4,Programmed cell death protein 4,Rat,Rattus norvegicus
25-256 BTBD10 appears to behave as a suppressor of cell death including neuronal cell death related to amyotrophic lateral sclerosis and an enhancer of cell growth via its positive regulation of Akt phosphor 0.05 mg
18-661-15195 Bcl2 antagonist of cell death - BAD; Bcl-2-binding component 6; Bcl-XL_Bcl-2-associated death promoter; Bcl-2-like 8 protein Polyclonal 0.1 mg
18-661-15186 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 - EC 2.4.1.119; Oligosaccharyl transferase subunit DAD1; Defender against cell death 1; DAD-1 Polyclonal 0.1 mg
EIAAB07402 Cell death activator CIDE-B,Cell death-inducing DFFA-like effector B,Cideb,Mouse,Mus musculus
EIAAB07399 Cell death activator CIDE-A,Cell death-inducing DFFA-like effector A,Cidea,Mouse,Mus musculus
EIAAB07400 Bos taurus,Bovine,Cell death activator CIDE-B,Cell death-inducing DFFA-like effector B,CIDEB
EIAAB07398 Cell death activator CIDE-A,Cell death-inducing DFFA-like effector A,CIDEA,Homo sapiens,Human
EIAAB07401 Cell death activator CIDE-B,Cell death-inducing DFFA-like effector B,CIDEB,Homo sapiens,Human
18-661-15048 Cell death activator CIDE-A - Cell death-inducing DFFA-like effector A Polyclonal 0.1 mg
18-661-15049 Cell death activator CIDE-A - Cell death-inducing DFFA-like effector A Polyclonal 0.1 mg
18-661-15050 Cell death activator CIDE-B - Cell death-inducing DFFA-like effector B Polyclonal 0.1 mg
EIAAB10386 DAD1,DAD-1,Defender against cell death 1,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1,Oligosaccharyl transferase subunit DAD1,Pig,Sus scrofa
EIAAB10385 Dad1,DAD-1,Defender against cell death 1,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1,Oligosaccharyl transferase subunit DAD1,Rat,Rattus norvegicus
EIAAB10388 Dad1,DAD-1,Defender against cell death 1,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1,Mouse,Mus musculus,Oligosaccharyl transferase subunit DAD1
EIAAB10384 Bos taurus,Bovine,DAD1,DAD-1,Defender against cell death 1,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1,Oligosaccharyl transferase subunit DAD1
EIAAB10387 DAD1,DAD-1,Defender against cell death 1,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1,Homo sapiens,Human,Oligosaccharyl transferase subunit DAD1
18-661-15200 Protein BEX3 - Brain-expressed X-linked protein 3; p75NTR-associated cell death executor; Nerve growth factor receptor-associated protein 1; Ovarian granulosa cell 13.0 kDa protein HGR74 Polyclonal 0.1 mg
EIAAB30250 CCM3,Cerebral cavernous malformations 3 protein,Homo sapiens,Human,PDCD10,Programmed cell death protein 10,TF-1 cell apoptosis-related protein 15,TFAR15
EIAAB10383 Chicken,DAD1,DAD-1,Defender against cell death 1,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1,Gallus gallus,Oligosaccharyl transferase subunit DAD1
EIAAB30251 Mouse,Mus musculus,Pdcd10,Programmed cell death protein 10,TF-1 cell apoptosis-related protein 15,Tfar15
31-008 The protein encoded by FADD is an adaptor molecule that interacts with various cell surface receptors and mediates cell apoptotic signals. Through its C-terminal death domain, this protein can be recr 0.05 mg
Pathways :
WP367: Programmed Cell Death
WP2272: Pathogenic Escherichia coli infection
WP1694: Pyrimidine metabolism
WP1566: Citrate cycle (TCA cycle)
WP2292: Chemokine signaling pathway
WP1693: Purine metabolism
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1644: DNA replication
WP1165: G Protein Signaling Pathways
WP1900: Regulation of mitotic cell cycle
WP2414: Quercetin and Nf-kB/ AP-1 induced cell apoptosis
WP844: Cell cycle
WP1613: 1,4-Dichlorobenzene degradation
WP1714: Tyrosine metabolism
WP2152: BDNF
WP45: G1 to S cell cycle control
WP908: B Cell Receptor Signaling Pathway
WP1624: Bacterial secretion system
WP1782: APC/C-mediated degradation of cell cycle proteins
WP2218: sGC
WP536: Calcium Regulation in the Cardiac Cell
WP1200: Cell cycle
WP1675: Nitrogen metabolism
WP285: B Cell Receptor Signaling Pathway

Related Genes :
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[ced-3 CRE_10123] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[BID] BH3-interacting domain death agonist (p22 BID) (BID) [Cleaved into: BH3-interacting domain death agonist p15 (p15 BID); BH3-interacting domain death agonist p13 (p13 BID); BH3-interacting domain death agonist p11 (p11 BID)]
[Bid] BH3-interacting domain death agonist (p22 BID) (BID) [Cleaved into: BH3-interacting domain death agonist p15 (p15 BID); BH3-interacting domain death agonist p13 (p13 BID); BH3-interacting domain death agonist p11 (p11 BID)]
[Bid] BH3-interacting domain death agonist (p22 BID) (BID) [Cleaved into: BH3-interacting domain death agonist p15 (p15 BID); BH3-interacting domain death agonist p13 (p13 BID); BH3-interacting domain death agonist p11 (p11 BID)]
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[Casp2 Ich1 Nedd-2 Nedd2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CASP2 ICH1 NEDD2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[gag-pro-pol] Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[gag-pro-pol] Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[CASP3 CPP32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[C PreC preC PreC-C preC-C PreC/C precore precore+core] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Nucleocapsid protein p7 (NC); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Nucleocapsid protein p7 (NC); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pro-pol] Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; Reverse transcriptase/ribonuclease H, p49 subunit (p49 RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Reverse transcriptase/ribonuclease H, p62 subunit (p62 RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pro-pol] Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; Reverse transcriptase/ribonuclease H, p49 subunit (p49 RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Reverse transcriptase/ribonuclease H, p62 subunit (p62 RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pro-pol] Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; Reverse transcriptase/ribonuclease H, p49 subunit (p49 RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Reverse transcriptase/ribonuclease H, p62 subunit (p62 RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[Casp7 Lice2 Mch3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[ced-9 T07C4.8] Apoptosis regulator ced-9 (Cell death protein 9)

Bibliography :
[9620337] Fas-mediated apoptosis in mouse hepatocytes involves the processing and activation of caspases.