| IED ID | IndEnz0002005144 |
| Enzyme Type ID | protease005144 |
| Protein Name |
Caspase-1-B CASP-1-B EC 3.4.22.36 Interleukin-1 beta convertase homolog B xICE-B Cleaved into: Caspase-1 subunit p20; Caspase-1 subunit p10 |
| Gene Name | casp1-b casp1b |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MTAQLNKVRKAIINGCNPAMISDLLDDLQDKHVLKDYEVEHINKKNNTSRDRCRDMIDSVKKKGEYSSNILLESLVKNHKTLAESLGLHEHAPSPIQEHNEDTIKDKEINSVIPCSAEEFKNIYDSHGDKIYEVREREGRKRLALIICNETFQSMSERRGAKLDLEGMNKLLNELGYQVQQHTNLTKAEMVKAMKEFAAREEHADSDSTFIVLMSHGDKPGVCGTDSKKTENGQYGVTNLLQVDEIFSTFNNVNCSRLWDKPKVIIIQACRGENQGGELVRDDVAPAPLEDDAVHHVQTETDSICFYSSTPDTASWRNPTKGSVFIIRLIEKMNELAHCQPLGDIFLEVQSSFKDKSPNQYSQMPTQERSTMTKKFYLFPGY |
| Enzyme Length | 382 |
| Uniprot Accession Number | P55867 |
| Absorption | |
| Active Site | ACT_SITE 216; /evidence=ECO:0000250|UniProtKB:P29466; ACT_SITE 270; /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. {ECO:0000250|UniProtKB:P29466}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (2); Propeptide (2) |
| Keywords | Cell membrane;Cytoplasm;Hydrolase;Membrane;Protease;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29466}. Cell membrane {ECO:0000250|UniProtKB:P29466}. |
| Modified Residue | |
| Post Translational Modification | PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism. {ECO:0000250|UniProtKB:P29466}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,389 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |