ID   CASP3_XENLA             Reviewed;         282 AA.
AC   P55866;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   02-SEP-2026, entry version 130.
DE   RecName: Full=Caspase-3;
DE            Short=CASP-3;
DE            EC=3.4.22.56;
DE   AltName: Full=Apopain;
DE   AltName: Full=Cysteine protease CPP32;
DE            Short=xCPP32;
DE   Contains:
DE     RecName: Full=Caspase-3 subunit p17;
DE   Contains:
DE     RecName: Full=Caspase-3 subunit p12;
DE   Flags: Precursor;
GN   Name=casp3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9030578; DOI=10.1074/jbc.272.8.5122;
RA   Yaoita Y., Nakajima K.;
RT   "Induction of apoptosis and CPP32 expression by thyroid hormone in a
RT   myoblastic cell line derived from tadpole tail.";
RL   J. Biol. Chem. 272:5122-5127(1997).
CC   -!- FUNCTION: Important mediator of apoptosis. At the onset of apoptosis,
CC       it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-
CC       Asp-|-Gly-217' bond (By similarity). {ECO:0000250|UniProtKB:P42574}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Strict requirement for an Asp residue at positions P1 and P4.
CC         It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a
CC         hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid
CC         residue at P3, although Val or Ala are also accepted at this
CC         position.; EC=3.4.22.56; Evidence={ECO:0000250|UniProtKB:P42574};
CC   -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC       heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12)
CC       subunit. {ECO:0000250|UniProtKB:P42574}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42574}.
CC   -!- MISCELLANEOUS: The subunits are derived from the precursor sequence by
CC       a probable autocatalytic mechanism and probably by other caspases.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR   EMBL; D89784; BAA14018.1; -; mRNA.
DR   RefSeq; NP_001081225.1; NM_001087756.1.
DR   AlphaFoldDB; P55866; -.
DR   SMR; P55866; -.
DR   MEROPS; C14.003; -.
DR   GeneID; 397720; -.
DR   KEGG; xla:397720; -.
DR   AGR; Xenbase:XB-GENE-865327; -.
DR   CTD; 397720; -.
DR   Xenbase; XB-GENE-865327; casp3.2.S.
DR   OrthoDB; 6116485at2759; -.
DR   BRENDA; 3.4.22.56; 6725.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 397720; Expressed in zone of skin and 16 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031264; C:death-inducing signaling complex; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0008047; F:enzyme activator activity; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR   GO; GO:0030218; P:erythrocyte differentiation; IBA:GO_Central.
DR   GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
DR   GO; GO:0030216; P:keratinocyte differentiation; IBA:GO_Central.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00032; CASc; 1.
DR   FunFam; 3.40.50.1460:FF:000001; Caspase-3 preproprotein; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR033139; Caspase_cys_AS.
DR   InterPro; IPR016129; Caspase_his_AS.
DR   InterPro; IPR002398; Pept_C14.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   InterPro; IPR015917; Pept_C14A.
DR   PANTHER; PTHR10454; CASPASE; 1.
DR   PANTHER; PTHR10454:SF198; CASPASE-3; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   PROSITE; PS01122; CASPASE_CYS; 1.
DR   PROSITE; PS01121; CASPASE_HIS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW   Thiol protease; Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000250|UniProtKB:P42574"
FT                   /id="PRO_0000004593"
FT   CHAIN           ?..186
FT                   /note="Caspase-3 subunit p17"
FT                   /evidence="ECO:0000250|UniProtKB:P42574"
FT                   /id="PRO_0000004594"
FT   CHAIN           187..282
FT                   /note="Caspase-3 subunit p12"
FT                   /evidence="ECO:0000250|UniProtKB:P42574"
FT                   /id="PRO_0000004595"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
SQ   SEQUENCE   282 AA;  32125 MW;  CB390E6980CAB77F CRC64;
     MEESQNGVKY GGDATDAKEY FTIQPRSLQN CDLKDIERKT KFAHLQNYRT NYPEMGMCLI
     INNKNFHSSN MAVRNGTDVD ALKLHETFTG LGYEVMVCND QKSSDIIGRL KKISEEDHSK
     RSSFVCAILS HGEEDGSICG VDVPIHIKNL TDLFRGDRCK TLVGKPKIFF IQACRGTELD
     SGIETDSCSE PREEIQRIPV EADFLYAYST VPGYCSWRDK MDGSWFIQSL CKMIKLYGSH
     LELIQILTCV NHMVALDFET FHAKKQIPCV VSMLTKSFYF FK
//