Detail Information for IndEnz0002002744
IED ID IndEnz0002002744
Enzyme Type ID protease002744
Protein Name Caspase-1
CASP-1
EC 3.4.22.36
Interleukin-1 beta convertase
IL-1BC
Interleukin-1 beta-converting enzyme
ICE
IL-1 beta-converting enzyme
p45

Cleaved into: Caspase-1 subunit p20; Caspase-1 subunit p10
Gene Name CASP1 IL1BC
Organism Equus caballus (Horse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse)
Enzyme Sequence MADKVLKEKRRLFIRSVGTGTVNSLLDELLEKRVLNQEEMEKVRDENATVMDKARALIDAVIRKGPQACQIFIGHICEDDPHLAETLRLSSGPQSGNFLKTQDSQAVVHSSPALQAMPDDLAKLALSGPKVSLKLCSPEVVERIWKEKSAEMYPIMGKSMTRTRLALIICNTEFDNLSRRAGAEVDIASMKVLLEGLGYSVEVKENLTALDMTTELKAFAARPEHRSSDSTFLVFMSHGIREGICGKKFSEKVPDVLEVNTIFQIFNTRNCPNLRDKPKVIIIQACRGENQGVVWLKDSTGTSGNSSSLAPDDFEDDAIKKAHVEKDFIAFCSSTPDTVSWRSPTTGSVFIEKLIENLQEYAWSCDLEEIFRKVRLSFELPDARAQMPTAERVTLTRRFYLFPGH
Enzyme Length 405
Uniprot Accession Number Q9TV13
Absorption
Active Site ACT_SITE 238; /evidence=ECO:0000250|UniProtKB:P29466; ACT_SITE 286; /evidence=ECO:0000250|UniProtKB:P29466
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.; EC=3.4.22.36; Evidence={ECO:0000250|UniProtKB:P29466};
DNA Binding
EC Number 3.4.22.36
Enzyme Function FUNCTION: Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides. Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a proinflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves a tetrapeptide after an Asp residue at position P1. Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD. In contrast to cleavage of interleukins IL1B and IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly. {ECO:0000250|UniProtKB:P29466}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (2); Domain (1); Modified residue (1); Natural variant (2); Propeptide (2)
Keywords Apoptosis;Cell membrane;Cytoplasm;Hydrolase;Membrane;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29466}. Cell membrane {ECO:0000250|UniProtKB:P29466}.
Modified Residue MOD_RES 303; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P29452
Post Translational Modification PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism. {ECO:0000250|UniProtKB:P29466}.; PTM: Ubiquitinated via 'Lys-11'-linked polyubiquitination. Deubiquitinated by USP8. {ECO:0000250|UniProtKB:P29466}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 45,331
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.36;