CSP3_CAEEL
ID CSP3_CAEEL Reviewed; 139 AA.
AC G5ECW5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Non-catalytic caspase homolog csp-3 {ECO:0000305};
GN Name=csp-3 {ECO:0000303|PubMed:9857046, ECO:0000312|WormBase:Y47H9C.6a};
GN ORFNames=Y47H9C.6 {ECO:0000312|WormBase:Y47H9C.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAC98297.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC98297.1};
RX PubMed=9857046; DOI=10.1074/jbc.273.52.35109;
RA Shaham S.;
RT "Identification of multiple Caenorhabditis elegans caspases and their
RT potential roles in proteolytic cascades.";
RL J. Biol. Chem. 273:35109-35117(1998).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CED-3, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PHE-57.
RX PubMed=18776901; DOI=10.1038/nsmb.1488;
RA Geng X., Shi Y., Nakagawa A., Yoshina S., Mitani S., Shi Y., Xue D.;
RT "Inhibition of CED-3 zymogen activation and apoptosis in Caenorhabditis
RT elegans by caspase homolog CSP-3.";
RL Nat. Struct. Mol. Biol. 15:1094-1101(2008).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=23505386; DOI=10.1371/journal.pgen.1003341;
RA Denning D.P., Hatch V., Horvitz H.R.;
RT "Both the caspase CSP-1 and a caspase-independent pathway promote
RT programmed cell death in parallel to the canonical pathway for apoptosis in
RT Caenorhabditis elegans.";
RL PLoS Genet. 9:E1003341-E1003341(2013).
CC -!- FUNCTION: Non-catalytic caspase homolog which does not contain the
CC region necessary for caspase activity (PubMed:9857046). Acts as an
CC inhibitor of caspase ced-3 zymogen autoactivation and delays ced-4-
CC induced ced-3 processing (PubMed:18776901). Has no effect on active
CC ced-3 (PubMed:18776901). Probably by preventing ced-3 activation,
CC protects cells, whose fate is to live, from apoptosis during embryonic
CC and larval development (PubMed:18776901). {ECO:0000269|PubMed:18776901,
CC ECO:0000303|PubMed:9857046}.
CC -!- SUBUNIT: Interacts with ced-3 (via large subunit p17); the interaction
CC prevents ced-3 autoactivation. {ECO:0000269|PubMed:18776901}.
CC -!- INTERACTION:
CC G5ECW5; P42573: ced-3; NbExp=3; IntAct=EBI-15727537, EBI-494247;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18776901}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo and in larvae.
CC {ECO:0000269|PubMed:18776901}.
CC -!- DISRUPTION PHENOTYPE: Hatching is impaired in 5-6 percent of mutant
CC embryos and about 2 percent of adults have uncoordinated movement
CC (PubMed:18776901). In the anterior pharynx of L4 larvae, several cells
CC including muscle and neuronal cells that normally survive during
CC development are missing (PubMed:18776901). Slight increase in the
CC number of cell corpses during embryonic development (PubMed:18776901).
CC In a ced-5 n1812 or ced-6 n2095 mutant background, where cell corpse
CC engulfment is defective, the number of cell corpses during embryonic
CC development and in L1 larvae is further increased (PubMed:18776901). In
CC a ced-3 n2427 or ced-3 n2427 and cps-3 n4872 mutant background, no
CC extra pharyngeal cells caused by impaired apoptosis are produced
CC (PubMed:23505386). In a csp-3 n4872, csp-1 n4967 and ced-3 n3692 mutant
CC background, pharyngeal cells, that are normally fated to die, survive
CC and 16 percent of animals have still 1 or more cell corpses that are
CC morphologically apoptotic and are internalized by engulfing cells
CC (PubMed:23505386). In addition, apoptosis of the male linker cell
CC occurs normally (PubMed:23505386). {ECO:0000269|PubMed:18776901,
CC ECO:0000269|PubMed:23505386}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000255}.
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DR EMBL; AF088290; AAC98297.1; -; mRNA.
DR EMBL; BX284601; CAA21735.3; -; Genomic_DNA.
DR PIR; T26968; T26968.
DR PIR; T43642; T43642.
DR RefSeq; NP_493011.2; NM_060610.3.
DR AlphaFoldDB; G5ECW5; -.
DR SMR; G5ECW5; -.
DR IntAct; G5ECW5; 1.
DR STRING; 6239.Y47H9C.6; -.
DR MEROPS; C14.014; -.
DR PaxDb; G5ECW5; -.
DR EnsemblMetazoa; Y47H9C.6a.1; Y47H9C.6a.1; WBGene00000821.
DR GeneID; 190006; -.
DR KEGG; cel:CELE_Y47H9C.6; -.
DR CTD; 190006; -.
DR WormBase; Y47H9C.6a; CE27635; WBGene00000821; csp-3.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00970000196149; -.
DR HOGENOM; CLU_1846942_0_0_1; -.
DR InParanoid; G5ECW5; -.
DR OrthoDB; 1921969at2759; -.
DR PhylomeDB; G5ECW5; -.
DR PRO; PR:G5ECW5; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000821; Expressed in material anatomical entity and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0035375; F:zymogen binding; IMP:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
DR GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1904746; P:negative regulation of apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IGI:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..139
FT /note="Non-catalytic caspase homolog csp-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439225"
FT MUTAGEN 57
FT /note="F->D: Reduced binding to ced-3. No effect on ced-3
FT autoactivation. Delays the ced-3 activation by ced-4.
FT Causes ectopic cell death during development."
FT /evidence="ECO:0000269|PubMed:18776901"
SQ SEQUENCE 139 AA; 16440 MW; 42C9E79856177520 CRC64;
MFFGKLGGFA FFLQRAVRCD GFIDNFFDRI PKFFQFMKSK FPSHQTSSSQ ADLLVSFSTS
PGFLSFKDET KDTWYIQELY RVIIENAKDT HLADLLTETN RRVVEKYEAD KVVFVCKQAP
EFWSRFTKQL FFMSRNDVF
