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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.
27-SEP-2017, entry version 147.
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;
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, ENZYME
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, ENZYME 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, ENZYME 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, ENZYME 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, ENZYME 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, ENZYME 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 ENZYME 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, ENZYME 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, ENZYME 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]
X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 198-503 IN COMPLEX WITH
CED-4, CATALYTIC ACTIVITY, ENZYME 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). Acts in
cell fate patterning by cleaving heterochronic protein lin-28,
likely promoting its degradation (PubMed:25432023). 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:3955651, ECO:0000269|PubMed:8654923,
ECO:0000269|PubMed:9857046, ECO:0000269|PubMed:9927601}.
-!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
position P1 and has a preferred cleavage sequence of Asp-Glu-Val-
Asp-|-. {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}.
-!- ENZYME REGULATION: Octameric 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
octameric ced-4 (two ced-3 zymogens per one ced-4 octamer); the
interaction causes the autoproteolytic cleavage and activation of
ced-3 (PubMed:24065769, PubMed:20434985). 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).
{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}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-494247, EBI-494247;
P30429:ced-4; NbExp=8; IntAct=EBI-494247, EBI-494118;
P30429-2:ced-4; NbExp=10; IntAct=EBI-494247, EBI-536271;
P41958:ced-9; NbExp=2; IntAct=EBI-494247, EBI-494110;
-!- 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}.
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EMBL; L29052; AAA27982.2; -; Genomic_DNA.
EMBL; AF210702; AAG42045.1; -; mRNA.
EMBL; Z81049; CAB61001.2; -; Genomic_DNA.
PIR; A49429; A49429.
RefSeq; NP_001255708.1; NM_001268779.1.
UniGene; Cel.19438; -.
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; -.
ProteinModelPortal; P42573; -.
SMR; P42573; -.
BioGrid; 43363; 5.
DIP; DIP-244N; -.
IntAct; P42573; 3.
MINT; MINT-128934; -.
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; ENSGT00760000118912; -.
HOGENOM; HOG000016385; -.
InParanoid; P42573; -.
KO; K20106; -.
OMA; GYTVICK; -.
OrthoDB; EOG091G05YD; -.
PhylomeDB; P42573; -.
Reactome; R-CEL-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-CEL-448706; Interleukin-1 processing.
PRO; PR:P42573; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00000417; -.
ExpressionAtlas; P42573; baseline.
GO; GO:0008303; C:caspase complex; IMP:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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: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:WormBase.
GO; GO:1902742; P:apoptotic process involved in development; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
GO; GO:0097194; P:execution phase of apoptosis; IDA:WormBase.
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 disassembly; 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:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
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. Loss of
processing. No effect on the interaction
with ced-4. Loss of interaction with
octameric ced-4; when associated with
391-D--D-393.
{ECO:0000269|PubMed:24065769,
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
octameric 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


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