IED ID | IndEnz0002005904 |
Enzyme Type ID | protease005904 |
Protein Name |
Caspase b EC 3.4.22.58 Caspase 19a Cleaved into: Caspase b subunit p20; Caspase b subunit p10 |
Gene Name | caspb casp19a caspy2 |
Organism | Danio rerio (Zebrafish) (Brachydanio rerio) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio) |
Enzyme Sequence | MEDITQLLSDVLEDLVESELKQFTRQLWIGVKPGVEPIPRGKLENKDRQDVVDSMVQQYSEDAGTITVQTLRKIKQNERAKRLESNLLKVQSQGQENKQNSEEPQPIPQIISQPIQQIISQPINNAGSEDLQPIQADWQRPRQIIPCSQETKNTLLKAHGDDIYTPRSGTQRKGLALLITNIQFANTQHNRNGADRDEENAEWLLRSLGFAVIKYRNLSGKDIRRAVENFSKRREHEDADSTFIVIMSHGTRIDNKDAIVGVSDDVYFIEETFSHLNSVNCPALIDKPKVILIQACRGGQSSGVLAQDSVFASDSWVHMEKDFVCFMSTMPNTFAYRNPIEGSFFISYIVDVFCSSAHRDDIMELFRKVTLRMEKDQRFQGQAKLLPCIERTSISKRFYLFPGL |
Enzyme Length | 404 |
Uniprot Accession Number | Q504J1 |
Absorption | |
Active Site | ACT_SITE 249; /evidence=ECO:0000250|UniProtKB:P29466; ACT_SITE 296; /evidence=ECO:0000269|PubMed:30076291 |
Activity Regulation | ACTIVITY REGULATION: Activated by homooligomerization induced by direct binding to cytosolic LPS. {ECO:0000269|PubMed:30076291}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-.; EC=3.4.22.58; Evidence={ECO:0000269|PubMed:12464617, ECO:0000269|PubMed:30076291}; |
DNA Binding | |
EC Number | 3.4.22.58 |
Enzyme Function | FUNCTION: Thiol protease which cleaves IL-1 beta (il1b), releasing the mature cytokine which is involved in a variety of inflammatory processes, and mediates apoptosis (PubMed:12464617, PubMed:30150286). Component of the NLRP1 inflammasome, which plays a crucial role in innate immunity and inflammation (PubMed:30150286). In response to pathogens and other damage-associated signals, recruited to the NLRP1 inflammasome in its precursor form following the recruitment of caspase caspa (PubMed:30150286). Its subsequent activation causes the cleavage of the midformed pro-il1b and results in il1b maturation and secretion in the extracellular milieu (PubMed:30150286). Activated by direct binding to bacterial lipopolysaccharides (LPS), which causes non-canonical inflammasome activation and results in the pyroptosis of infected cells and their extrusion into the gut lumen, as well as in cytokine secretion (PubMed:30076291). Plays a crucial role in the restriction of bacterial infection to intestinal sites (PubMed:30076291). Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (By similarity). Promotes pyroptosis by bacterial infection by E.piscicida (PubMed:30076291). {ECO:0000250|UniProtKB:P49662, ECO:0000269|PubMed:12464617, ECO:0000269|PubMed:30076291, ECO:0000269|PubMed:30150286}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (2); Domain (1); Mutagenesis (1); Propeptide (2); Sequence conflict (7) |
Keywords | Apoptosis;Cytoplasm;Hydrolase;Immunity;Inflammasome;Inflammatory response;Innate immunity;Necrosis;Protease;Reference proteome;Thiol protease;Zymogen |
Interact With | |
Induction | INDUCTION: Up-regulated in response to pentachlorophenol (PCP), a toxic pollutant (PubMed:28402832). Up-regulated in response to bacterial lipopolysaccharides (LPS) and bacterial infection with E.piscicida (PubMed:30076291). Up-regulated in response to bacterial infection with E.tarda (PubMed:30150286). {ECO:0000269|PubMed:28402832, ECO:0000269|PubMed:30076291, ECO:0000269|PubMed:30150286}. |
Subcellular Location | SUBCELLULAR LOCATION: Inflammasome {ECO:0000269|PubMed:30150286}. Cytoplasm {ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, caspa and nlrp1 in the cytoplasm (PubMed:30150286). Co-localizes with pycard at large cytoplasmic aggregates, known as specks (PubMed:30150286). {ECO:0000269|PubMed:30150286}. |
Modified Residue | |
Post Translational Modification | PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism. {ECO:0000305|PubMed:30076291, ECO:0000305|PubMed:30150286}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 19220579; 31852739; 32111733; |
Motif | |
Gene Encoded By | |
Mass | 46,090 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |