CAS1B_XENLA
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 03-AUG-2022, entry version 105.
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 CTD; 378669; -.
DR Xenbase; XB-GENE-6077552; casp1.S.
DR OrthoDB; 1327703at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 378669; Expressed in liver and 9 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
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:0070269; P:pyroptosis; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR CDD; cd00032; CASc; 1.
DR Gene3D; 1.10.533.10; -; 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; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR Pfam; PF00619; CARD; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52129; SSF52129; 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
