Detail Information for IndEnz0002005904
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