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Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]

 CSP1_CAEEL              Reviewed;         536 AA.
G5EBM1; G5EBN4; G5EG94;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
22-NOV-2017, entry version 61.
RecName: Full=Caspase A {ECO:0000305};
EC=3.4.22.36 {ECO:0000269|PubMed:9857046};
Contains:
RecName: Full=Caspase A subunit p16 {ECO:0000305|PubMed:9857046};
Contains:
RecName: Full=Caspase A subunit p14 {ECO:0000305|PubMed:9857046};
Flags: Precursor;
Name=csp-1 {ECO:0000303|PubMed:9857046,
ECO:0000312|WormBase:Y48E1B.13a};
ORFNames=Y48E1B.13 {ECO:0000312|WormBase:Y48E1B.13a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:AAC98292.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), PARTIAL PROTEIN
SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT,
PROTEOLYTIC CLEAVAGE, ACTIVE SITE, AND MUTAGENESIS OF CYS-406.
STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC98292.1};
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, AND DISRUPTION PHENOTYPE.
PubMed=23721876; DOI=10.1016/j.neuro.2013.05.014;
Settivari R., VanDuyn N., LeVora J., Nass R.;
"The Nrf2/SKN-1-dependent glutathione S-transferase pi homologue GST-1
inhibits dopamine neuron degeneration in a Caenorhabditis elegans
model of manganism.";
NeuroToxicology 38:51-60(2013).
[4] {ECO:0000305}
FUNCTION (ISOFORMS A; B AND C), AND 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: Cysteine protease which, in vitro, cleaves itself and
caspase ced-3 into their mature active forms (PubMed:9857046).
Also cleaves, in vitro, inactive caspase csp-2 isoform b
(PubMed:9857046). Required maternally to induce apoptosis in a
subset of cells fated to die during embryogenesis, mostly
independently of the ced-9, ced-4 and ced-3 canonical apoptosis
pathway (PubMed:23505386). Involved in the degeneration of
dopaminergic CEP neurons in response to high Mn(2+) levels
(PubMed:23721876). {ECO:0000269|PubMed:23505386,
ECO:0000269|PubMed:23721876, ECO:0000269|PubMed:9857046}.
-!- FUNCTION: Isoform a: Dispensable for regulating apoptosis during
embryogenesis. {ECO:0000269|PubMed:23505386}.
-!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-
Asp-|-. {ECO:0000269|PubMed:9857046}.
-!- ENZYME REGULATION: Inhibited by cysteine protease inhibitor
iodoacetic acid (CH3COOI) but not by N-[N-(L-3-transcarboxirane-2-
carbonyl)-leucyl]-agmatine (E-64) or benzyloxycarbonyl-DEVD-
fluoro-methyl ketone (Z-DEVD-FMK). {ECO:0000269|PubMed:9857046}.
-!- SUBUNIT: Heterodimer formed by the tight association of the large
subunit p16 and the small subunit p14.
{ECO:0000303|PubMed:9857046}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a {ECO:0000312|WormBase:Y48E1B.13a};
IsoId=G5EBM1-1; Sequence=Displayed;
Name=b {ECO:0000312|WormBase:Y48E1B.13b};
IsoId=G5EBM1-2; Sequence=VSP_058804;
Name=c {ECO:0000312|WormBase:Y48E1B.13c};
IsoId=G5EBM1-3; Sequence=VSP_058804, VSP_058805, VSP_058806;
-!- TISSUE SPECIFICITY: Isoform a: Expression is restricted to the
late germline pachytene stage of meiosis I in both L4 larvae and
adult hermaphrodite gonads. Isoform b: Expression is restricted to
the late germline pachytene stage of meiosis I in both L4 larvae
and adult hermaphrodite gonads. {ECO:0000269|PubMed:23505386}.
-!- PTM: Autocatalytic cleavage removes the propeptide and generates
the two active subunits p16 and p14 in vitro. Cannot be cleaved by
ced-3 in vitro. {ECO:0000269|PubMed:9857046}.
-!- DISRUPTION PHENOTYPE: Survival of touch neurons and several
pharyngeal cells is not affected during development and no extra
pharyngeal cells caused by impaired apoptosis are produced
(PubMed:23505386). Basal and ionizing radiation-induced germline
apoptosis are normal (PubMed:23505386). In a ced-3 n2427 mutant
background, more animals have the M4 sister cell that survives
(PubMed:23505386). In a csp-3 n4872, csp-2 n4871 and ced-3 n3692
mutant background where the canonical apoptotic pathway is
impaired, 16 percent of animals have still 1 or more cell corpses
that are morphologically apoptotic and are internalized by
engulfing cells (PubMed:23505386). In addition, apoptosis of the
male linker cell occurs normally (PubMed:23505386). RNAi-mediated
knockdown causes a 50 percent inhibition of Mn(2+)-induced
dopaminergic CEP neuron degeneration (PubMed:23721876).
{ECO:0000269|PubMed:23505386, ECO:0000269|PubMed:23721876}.
-!- SIMILARITY: Belongs to the peptidase C14A family.
{ECO:0000255|RuleBase:RU003971, ECO:0000255|SAAS:SAAS00535228}.
-----------------------------------------------------------------------
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EMBL; AF088285; AAC98292.1; -; mRNA.
EMBL; AF088286; AAC98293.1; -; mRNA.
EMBL; AF088287; AAC98294.1; -; mRNA.
EMBL; BX284602; CAB07698.2; -; Genomic_DNA.
EMBL; BX284602; CAD18879.1; -; Genomic_DNA.
EMBL; BX284602; CAD18880.1; -; Genomic_DNA.
PIR; T27021; T27021.
PIR; T43633; T43633.
PIR; T43637; T43637.
RefSeq; NP_001022452.1; NM_001027281.1. [G5EBM1-1]
RefSeq; NP_001022453.1; NM_001027282.1. [G5EBM1-2]
RefSeq; NP_001022454.1; NM_001027283.1. [G5EBM1-3]
UniGene; Cel.18227; -.
ProteinModelPortal; G5EBM1; -.
STRING; 6239.Y48E1B.13a; -.
MEROPS; C14.A06; -.
EPD; G5EBM1; -.
PaxDb; G5EBM1; -.
EnsemblMetazoa; Y48E1B.13a; Y48E1B.13a; WBGene00000819. [G5EBM1-1]
EnsemblMetazoa; Y48E1B.13b; Y48E1B.13b; WBGene00000819. [G5EBM1-2]
EnsemblMetazoa; Y48E1B.13c; Y48E1B.13c; WBGene00000819. [G5EBM1-3]
GeneID; 175007; -.
KEGG; cel:CELE_Y48E1B.13; -.
CTD; 175007; -.
WormBase; Y48E1B.13a; CE29378; WBGene00000819; csp-1.
WormBase; Y48E1B.13b; CE30016; WBGene00000819; csp-1.
WormBase; Y48E1B.13c; CE30017; WBGene00000819; csp-1.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
OrthoDB; EOG091G05YD; -.
Reactome; R-CEL-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-CEL-448706; Interleukin-1 processing.
PRO; PR:G5EBM1; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00000819; -.
ExpressionAtlas; G5EBM1; baseline.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0043073; C:germ cell nucleus; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
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; IGI:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; IMP:UniProtKB.
GO; GO:0016485; P:protein processing; IMP:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
InterPro; IPR006570; SPK_dom.
Pfam; PF04435; SPK; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SMART; SM00583; SPK; 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; Apoptosis; Complete proteome;
Direct protein sequencing; Hydrolase; Protease; Reference proteome;
Thiol protease; Zymogen.
PROPEP 1 273 Removed in mature form by autoprocessing.
{ECO:0000269|PubMed:9857046}.
/FTId=PRO_0000439218.
CHAIN 274 418 Caspase A subunit p16.
{ECO:0000303|PubMed:9857046}.
/FTId=PRO_0000439219.
CHAIN 419 536 Caspase A subunit p14.
{ECO:0000303|PubMed:9857046}.
/FTId=PRO_0000439220.
ACT_SITE 364 364 {ECO:0000250|UniProtKB:P29466}.
ACT_SITE 406 406 {ECO:0000269|PubMed:9857046}.
VAR_SEQ 1 268 Missing (in isoform b and isoform c).
{ECO:0000305}.
/FTId=VSP_058804.
VAR_SEQ 411 417 LNMGVPV -> IEHGCSR (in isoform c).
{ECO:0000305}.
/FTId=VSP_058805.
VAR_SEQ 418 536 Missing (in isoform c). {ECO:0000305}.
/FTId=VSP_058806.
MUTAGEN 406 406 C->S: Loss of catalytic activity. Loss of
autoprocessing.
{ECO:0000269|PubMed:9857046}.
SEQUENCE 536 AA; 61467 MW; 089F72490C6AA69E CRC64;
MVLKTIEDNC KSQFDDDLVE DFNNFQTTSS MSSSTTISTE DFNTIEIEST FEICRSGSYT
EEPILGENDE FLIDFEMERF LKFLKDKTKQ VEKRKEPFSQ KEIYAVFQRR IKSELCIETV
KKKFQPLLPN AIQTCEFDEE TMIRMIYGAG IRIDSVDFWN RFTSKATISL DCYSRLISYS
SDSLTLSGTH RSGFTYHWIS TPPVTYHRTE NKDPNIQEPS PVEFLDVQSS LGSSMKPPIL
DKPTKLDDPA ETRHDCSYSL EEYDSQSRMP RTDAKKSNHK HKYCYEMNSN PRGTVLILSN
ENFKNMERRV GTKQDEVNLT KLFQKLQYTV ICKRNLEAES MLEAIKEFAE MAHTDSIILF
LLSHGDGAGS VFGIDDMPVN VMEVSTYLAY HQNLLLKPKW VAVSACRGGK LNMGVPVDGL
PALEDKCAPI SKFWNLMMSR IMPGTFTSLN ADVIISFSTT DGFTSYRDEE AGTWYIKSMC
KVFNKHSKTM HLLDILTETG RNVVTKYENV QGNVVLKQAP EILSRLTKQW HFSRSM


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