ID   CAS1B_XENLA             Reviewed;         382 AA.
AC   P55867;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=Caspase-1-B;
DE            Short=CASP-1-B;
DE            EC=3.4.22.36 {ECO:0000250|UniProtKB:P29466};
DE   AltName: Full=Interleukin-1 beta convertase homolog B;
DE            Short=xICE-B;
DE   Contains:
DE     RecName: Full=Caspase-1 subunit p20 {ECO:0000250|UniProtKB:P29466};
DE   Contains:
DE     RecName: Full=Caspase-1 subunit p10 {ECO:0000250|UniProtKB:P29466};
DE   Flags: Precursor;
GN   Name=casp1-b; Synonyms=casp1b;
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].
RA   Nakajima K.;
RT   "Cloning of the Xenopus homologue of ICE.";
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thiol protease involved in a variety of inflammatory
CC       processes by proteolytically cleaving other proteins, such as the
CC       precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and
CC       interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D
CC       (GSDMD), into active mature peptides. Plays a key role in cell immunity
CC       as an inflammatory response initiator: once activated through formation
CC       of an inflammasome complex, it initiates a pro-inflammatory response
CC       through the cleavage of the two inflammatory cytokines IL1B and IL18,
CC       releasing the mature cytokines which are involved in a variety of
CC       inflammatory processes. Cleaves a tetrapeptide after an Asp residue at
CC       position P1. Also initiates pyroptosis, a programmed lytic cell death
CC       pathway, through cleavage of GSDMD. {ECO:0000250|UniProtKB:P29466}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Strict requirement for an Asp residue at position P1 and has a
CC         preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.; EC=3.4.22.36;
CC         Evidence={ECO:0000250|UniProtKB:P29466};
CC   -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC       heterodimers, each one formed by a 20 kDa (Caspase-1 subunit p20) and a
CC       10 kDa (Caspase-1 subunit p10) subunit. {ECO:0000250|UniProtKB:P29466}.
CC   -!- SUBUNIT: [Caspase-1 subunit p20]: Heterotetramer that consists of two
CC       anti-parallel arranged heterodimers, each one formed by a 20 kDa
CC       (Caspase-1 subunit p20) and a 10 kDa (Caspase-1 subunit p10) subunit.
CC       Can form a heterodimer with isoform epsilon which then has an
CC       inhibitory effect. {ECO:0000250|UniProtKB:P29466}.
CC   -!- SUBUNIT: [Caspase-1 subunit p10]: Heterotetramer that consists of two
CC       anti-parallel arranged heterodimers, each one formed by a 20 kDa
CC       (Caspase-1 subunit p20) and a 10 kDa (Caspase-1 subunit p10) subunit.
CC       {ECO:0000250|UniProtKB:P29466}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29466}. Cell
CC       membrane {ECO:0000250|UniProtKB:P29466}.
CC   -!- PTM: The two subunits are derived from the precursor sequence by an
CC       autocatalytic mechanism. {ECO:0000250|UniProtKB:P29466}.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR   EMBL; D89785; BAA14019.1; -; mRNA.
DR   RefSeq; NP_001079341.1; NM_001085872.1.
DR   AlphaFoldDB; P55867; -.
DR   SMR; P55867; -.
DR   GeneID; 378669; -.
DR   KEGG; xla:378669; -.
DR   AGR; Xenbase:XB-GENE-6077552; -.
DR   CTD; 378669; -.
DR   Xenbase; XB-GENE-6077552; casp1.S.
DR   OrthoDB; 6097640at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 378669; Expressed in liver and 9 other cell types or tissues.
DR   GO; GO:0097169; C:AIM2 inflammasome complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0072557; C:IPAF inflammasome complex; IBA:GO_Central.
DR   GO; GO:0072559; C:NLRP3 inflammasome complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR   GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   GO; GO:0070269; P:pyroptotic inflammatory response; ISS:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   CDD; cd00032; CASc; 1.
DR   FunFam; 3.40.50.1460:FF:000007; Caspase-1; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   InterPro; IPR001315; CARD.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR033139; Caspase_cys_AS.
DR   InterPro; IPR016129; Caspase_his_AS.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
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; PTHR47901; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 18; 1.
DR   PANTHER; PTHR47901:SF3; CASPASE-1; 1.
DR   Pfam; PF00619; CARD; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PIRSF; PIRSF038001; Caspase_ICE; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00114; CARD; 1.
DR   SMART; SM00115; CASc; 1.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   PROSITE; PS50209; CARD; 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   Cell membrane; Cytoplasm; Hydrolase; Membrane; Protease;
KW   Reference proteome; Thiol protease; Zymogen.
FT   PROPEP          1..98
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004539"
FT   CHAIN           99..282
FT                   /note="Caspase-1 subunit p20"
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
FT                   /id="PRO_0000451689"
FT   PROPEP          283..292
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
FT                   /id="PRO_0000451690"
FT   CHAIN           293..382
FT                   /note="Caspase-1 subunit p10"
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
FT                   /id="PRO_0000451691"
FT   ACT_SITE        216
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250|UniProtKB:P29466"
SQ   SEQUENCE   382 AA;  43389 MW;  81D2FB7BF3C2230F CRC64;
     MTAQLNKVRK AIINGCNPAM ISDLLDDLQD KHVLKDYEVE HINKKNNTSR DRCRDMIDSV
     KKKGEYSSNI LLESLVKNHK TLAESLGLHE HAPSPIQEHN EDTIKDKEIN SVIPCSAEEF
     KNIYDSHGDK IYEVREREGR KRLALIICNE TFQSMSERRG AKLDLEGMNK LLNELGYQVQ
     QHTNLTKAEM VKAMKEFAAR EEHADSDSTF IVLMSHGDKP GVCGTDSKKT ENGQYGVTNL
     LQVDEIFSTF NNVNCSRLWD KPKVIIIQAC RGENQGGELV RDDVAPAPLE DDAVHHVQTE
     TDSICFYSST PDTASWRNPT KGSVFIIRLI EKMNELAHCQ PLGDIFLEVQ SSFKDKSPNQ
     YSQMPTQERS TMTKKFYLFP GY
//