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Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14]

 CSP2_CAEEL              Reviewed;         263 AA.
Q9TZP5; G5ECY5;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
30-AUG-2017, entry version 83.
RecName: Full=Putative inactive caspase B {ECO:0000305};
Contains:
RecName: Full=Putative inactive caspase B subunit p31 {ECO:0000305|PubMed:9857046};
Contains:
RecName: Full=Putative inactive caspase B subunit p17 {ECO:0000305|PubMed:9857046};
Contains:
RecName: Full=Putative inactive caspase subunit p14 {ECO:0000305|PubMed:9857046};
Flags: Precursor;
Name=csp-2 {ECO:0000303|PubMed:9857046,
ECO:0000312|WormBase:Y73B6BL.7};
ORFNames=Y73B6BL.7 {ECO:0000312|WormBase:Y73B6BL.7};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|EMBL:AAC98296.1};
[1] {ECO:0000312|EMBL:AAC98296.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, LACK OF
CATALYTIC ACTIVITY, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-8.
STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC98296.1};
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).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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).
[3] {ECO:0000305}
FUNCTION (ISOFORMS A AND B), INTERACTION WITH CED-3, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 131-TRP--LEU-132;
CYS-134 AND PHE-186.
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).
[4] {ECO:0000305}
DISRUPTION PHENOTYPE.
PubMed=23505386; DOI=10.1371/journal.pgen.1003341;
Denning D.P., Hatch V., Horvitz H.R.;
"Both the caspase CSP-1 and a caspase-independent pathway promote
programmed cell death in parallel to the canonical pathway for
apoptosis in Caenorhabditis elegans.";
PLoS Genet. 9:E1003341-E1003341(2013).
-!- FUNCTION: Isoform b: Putative inactive caspase (PubMed:9857046).
In the germline, binds caspase ced-3 zymogen and prevents ced-3
autoactivation. Does not affect the caspase activity of mature
ced-3 and ced-4-mediated mature ced-3 activation
(PubMed:19575016). Negatively regulates germline apoptosis by
inhibiting autocleavage of caspase ced-3 (PubMed:19575016).
Involved in fertility (PubMed:19575016).
{ECO:0000269|PubMed:19575016, ECO:0000269|PubMed:9857046}.
-!- FUNCTION: Isoform a: Putative inactive caspase (PubMed:9857046).
Dispensable for the inhibition of germline apoptosis
(PubMed:19575016). {ECO:0000269|PubMed:19575016,
ECO:0000303|PubMed:9857046}.
-!- SUBUNIT: Interacts with ced-3 (via large subunit p17 or small
subunit p13); the interaction inhibits ced-3 autoactivation.
{ECO:0000269|PubMed:19575016}.
-!- SUBCELLULAR LOCATION: Isoform b: Cytoplasm
{ECO:0000269|PubMed:19575016}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=b {ECO:0000312|EMBL:AAC98296.1};
IsoId=Q9TZP5-1; Sequence=Displayed;
Name=a {ECO:0000312|WormBase:Y73B6BL.7};
IsoId=Q9TZP5-2; Sequence=VSP_058807;
-!- TISSUE SPECIFICITY: Specifically expressed in the hermaphrodite
germline. {ECO:0000269|PubMed:19575016}.
-!- PTM: Cleavage by csp-1 isoform b or ced-3 removes the propeptide
and generates subunit p31 in vitro. An additional cleavage at Asp-
149 generates the 2 subunits p17 and p14 but this cleavage appears
to be less efficient. {ECO:0000269|PubMed:9857046}.
-!- DISRUPTION PHENOTYPE: Survival of touch neurons and several
pharyngeal cells is not affected during development. In a ced-3
n2427 or ced-3 n2427 and cps-3 n4872 mutant background, no extra
pharyngeal cells caused by impaired apoptosis are produced. In a
csp-3 n4872, csp-1 n4967 and ced-3 n3692 mutant background,
pharyngeal cells, that are normally fated to die, survive and 16
percent of animals have still 1 or more cell corpses that are
morphologically apoptotic and are internalized by engulfing cells.
In addition, apoptosis of the male linker cell occurs normally.
{ECO:0000269|PubMed:23505386}.
-!- SIMILARITY: Belongs to the peptidase C14A family.
{ECO:0000255|RuleBase:RU003971, ECO:0000255|SAAS:SAAS00535228}.
-!- CAUTION: Although the active site residues Cys and His are
conserved, appears to lack catalytic activity in vitro. This is
probably due to the active site pentapeptide VCCRG being highly
divergent from the canonical active site pentapeptide QAC[RQG]G
present in catalytically active caspases.
{ECO:0000303|PubMed:9857046}.
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EMBL; AF088288; AAC98295.1; -; mRNA.
EMBL; AF088289; AAC98296.1; -; mRNA.
EMBL; BX284604; CCD74157.1; -; Genomic_DNA.
EMBL; BX284604; SIT60436.1; -; Genomic_DNA.
PIR; T43638; T43638.
RefSeq; NP_001023575.1; NM_001028404.2. [Q9TZP5-2]
RefSeq; NP_001335546.1; NM_001348645.1. [Q9TZP5-1]
UniGene; Cel.19615; -.
ProteinModelPortal; Q9TZP5; -.
STRING; 6239.Y73B6BL.7; -.
MEROPS; C14.014; -.
PaxDb; Q9TZP5; -.
EnsemblMetazoa; Y73B6BL.7; Y73B6BL.7; WBGene00000820. [Q9TZP5-2]
GeneID; 177391; -.
KEGG; cel:CELE_Y73B6BL.7; -.
UCSC; Y73B6BL.7; c. elegans. [Q9TZP5-1]
CTD; 177391; -.
WormBase; Y73B6BL.7; CE28270; WBGene00000820; csp-2.
eggNOG; KOG0516; Eukaryota.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000119163; -.
OrthoDB; EOG091G0E4Y; -.
Reactome; R-CEL-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-CEL-448706; Interleukin-1 processing.
PRO; PR:Q9TZP5; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00000820; -.
ExpressionAtlas; Q9TZP5; baseline.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0097179; C:protease inhibitor complex; IMP:UniProtKB.
GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0035375; F:zymogen binding; IDA:UniProtKB.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:UniProtKB.
GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IGI:UniProtKB.
GO; GO:0090727; P:positive regulation of brood size; IMP:UniProtKB.
GO; GO:1905516; P:positive regulation of fertilization; IGI:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Reference proteome.
PROPEP 1 8 Removed in mature form by cps-1 or ced-3.
{ECO:0000269|PubMed:9857046}.
/FTId=PRO_0000439221.
CHAIN 9 263 Putative inactive caspase B subunit p31.
{ECO:0000303|PubMed:9857046}.
/FTId=PRO_0000439222.
CHAIN 9 149 Putative inactive caspase B subunit p17.
{ECO:0000303|PubMed:9857046}.
/FTId=PRO_0000439223.
CHAIN 150 263 Putative inactive caspase subunit p14.
{ECO:0000303|PubMed:9857046}.
/FTId=PRO_0000439224.
VAR_SEQ 1 1 M -> MKIGWLLITICSGIITKCINAHSSPYQNANESAIDD
AYFLVLIIPAVSVAIVLVVVIFLCCPRQQIRSDNVIKLEEG
VNDVIEENVTHVVSLREAKVSGMMTDLTRFRQEIFTKHLTF
NSNPESIDAATKNVQNVKQSLDTWRDRIKERLDEIDRLCTE
EGDSLTPEQYSALREMRRQLADEYDTVLRTVEGIHTRLNIL
SALLIEFSSVTSSMQSWMTDRARLAGDIRHKSGDPMRVDEA
RFEAKSLMDEVVREESRLKTIGASVLKIEQEISAMRDDVRA
SRSTDDVGISMDEVYEKRRRVEVDYMQLLRQCQDLISLQIR
LHAMNDEHAEQARRAEGWLQMLKNDVAGVAKDPRFKKDEDL
IERDEELNRMAAGGSGGPTSRQLAMREKIEQREREEEEWRR
KAKEKFEEEAAKNRARERKWAEEHGFNRPIRTRSQKYAEQD
RIRYARKKAALEQSNEQSNESTDDAVESDSDDVPAPQSPPT
PSPADPGPTTSSSSLTQDPASNATGFSDVPAPQAPPTPSPA
DPGPTTSSSSLTQDPASNATGFSGSSPPNSFEETRM (in
isoform a). {ECO:0000305}.
/FTId=VSP_058807.
MUTAGEN 8 8 D->A: Loss of propeptide cleavage.
{ECO:0000269|PubMed:9857046}.
MUTAGEN 131 132 WL->ER: Loss of interaction with ced-3
small subunit p13. Increased germline
apoptosis in a ced-6 n2095 mutant
background, loss of interaction with ced-
3 and loss of ced-3 autoactivation; when
associated with D-186.
{ECO:0000269|PubMed:19575016}.
MUTAGEN 134 134 C->E: Reduction in the interaction with
ced-3 small subunit p13.
{ECO:0000269|PubMed:19575016}.
MUTAGEN 186 186 F->D: Severe reduction in the interaction
with ced-3 large subunit p17. Increased
germline apoptosis in a ced-6 n2095
mutant background, loss of interaction
with ced-3 and loss of ced-3
autoactivation; when associated with E-
131 and R-132.
{ECO:0000269|PubMed:19575016}.
SEQUENCE 263 AA; 30401 MW; FE94EC95B8B59FEE CRC64;
MMCEDASDGK KIDETRKYRN NRSSKCRAII INNVVFCGME KRIGSDKDKK KLSKLFERLG
YQSTSYDNLK SSEILETVRQ FTQSNHGDSL IITIMSHGDQ GLLYGVDGVP VQMLDIIDLM
CTASLAKKPK WLMCVCCRGD RIDRAVRCDG FIDNFFDRFP KFFQFMKSKF PSHQTSSSQA
DLLVSFSTSP GFLSFRDETK GTWYIQELYR VIIENAKDTH LADLLMETNR RVVEKYEADK
VVIVCKQAPE FWSRFTKQLF FDV


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