IED ID | IndEnz0002004744 |
Enzyme Type ID | protease004744 |
Protein Name |
Caspase a EC 3.4.22.36 Cleaved into: Caspase a subunit p20; Caspase a subunit p10 |
Gene Name | caspa casp1 caspy |
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 | MAKSIKDHLQDALSNIGADNLRRFQSRLGDRKQEPRVRKSTIEKLKDEIDLVDLLVNTFTSDAVSVTVDILRGIKCNAVAEELLENTGQGGVSQPEPPVPEPIPKDPAQLKELKVTPCSQQFKNKILREKGQETYEIKDKSVRKRLALLINNVDFDDKAMKRSGSEKDEENMEKLLKELDYQVVKRPNLSAKEMDEAIRDFAQREEHKYSDSAFVVIMSHGKRDAIMGVHYHRTNNPSDSFPVDNVYRRLNSENCPALRDKPKVILIQACRGGEHGRVWASDGEPDEPIEIEDDDFVHKEKDFISLMSCTPDTKSYRHVQNGTFYVQTLVDVFIKCAHEDHIEELFRKVLRRFEHPNMIGNFKQMACKDRATLPKLFYLFPGL |
Enzyme Length | 383 |
Uniprot Accession Number | Q9I9L7 |
Absorption | |
Active Site | ACT_SITE 220; /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:0000269|PubMed:12464617}; |
DNA Binding | |
EC Number | 3.4.22.36 |
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 (PubMed:30150286). Its subsequent activation causes the cleavage of pro-il1b into the midformed il1b, which then evetually leads to il1b maturation and secretion in the extracellular milieu (PubMed:30150286). Required for the development of the cartilaginous pharyngeal skeleton (PubMed:12464617). {ECO:0000269|PubMed:12464617, ECO:0000269|PubMed:30150286}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (2); Domain (1); Propeptide (2); Region (1); Sequence conflict (9) |
Keywords | Cytoplasm;Hydrolase;Inflammasome;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 infection with E.tarda (PubMed:30150286). {ECO:0000269|PubMed:28402832, ECO:0000269|PubMed:30150286}. |
Subcellular Location | SUBCELLULAR LOCATION: Inflammasome {ECO:0000269|PubMed:30150286}. Cytoplasm {ECO:0000269|PubMed:12464617, ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, nlrp1 and caspb in the cytoplasm (PubMed:30150286). Co-localizes with pycard at large cytoplasmic aggregates, known as specks (PubMed:12464617, PubMed:30150286). {ECO:0000269|PubMed:12464617, 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:30150286}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 31852739; 32332700; |
Motif | |
Gene Encoded By | |
Mass | 43,966 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |