IED ID | IndEnz0002018943 |
Enzyme Type ID | protease018943 |
Protein Name |
Caspase-6 CASP-6 EC 3.4.22.59 Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11 |
Gene Name | CASP6 |
Organism | Gallus gallus (Chicken) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
Enzyme Sequence | MSGAERRPAAGRVQLDSKPTPTTTADGNQNITEVDAFDKRQTFDPAVQYKMNHQRRGVALIFNHEHFFWHLRLPDRRGTLADRNNLKRSLTDLGFEVRIFDDLKAEDVLKKVFEASRDDYSNADCFVCVFLSHGENDHVYAYDAQIKIETITNMFRGDKCQSLVGKPKIFIIQACRGDKHDDPVLVQDSVDSKDETTVNQTEVDAAGVYTLPAGADFIMCYSVAQGYFSHRETVNGSWYIQDLCEALGKHGSSLEFTELLTVVNRKVSHRKVDICRDINAIGKKQIPCFASMLTKKLYFHPKSK |
Enzyme Length | 304 |
Uniprot Accession Number | A0A1D5PPP7 |
Absorption | |
Active Site | ACT_SITE 133; /evidence=ECO:0000250|UniProtKB:P55212; ACT_SITE 175; /evidence=ECO:0000250|UniProtKB:P55212 |
Activity Regulation | ACTIVITY REGULATION: During activation, the N-terminal prodomain is removed by cleavage (By similarity). Concomitantly, double cleavage gives rise to a large 18-kDa and a small 11-kDa subunit (By similarity). The two large and two small subunits then assemble to form the active CASP6 complex (By similarity). Intramolecular cleavage at Asp-191 is a prerequisite for CASP6 self-activation (By similarity). {ECO:0000250|UniProtKB:P55212}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000250|UniProtKB:P55212}; |
DNA Binding | |
EC Number | 3.4.22.59 |
Enzyme Function | FUNCTION: Cysteine protease that plays essential roles in programmed cell death, development and innate immunity (PubMed:11953316). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein lamin-A/LMNA thereby inducing nuclear shrinkage and fragmentation (PubMed:11953316). Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution (PubMed:11953316). Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity. PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis (By similarity). {ECO:0000250|UniProtKB:P55212, ECO:0000269|PubMed:11953316}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (3); Propeptide (2); Region (2); Sequence conflict (4) |
Keywords | Apoptosis;Autocatalytic cleavage;Cytoplasm;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 34,476 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |