| IED ID | IndEnz0002004469 |
| Enzyme Type ID | protease004469 |
| Protein Name |
Caspase-5 CASP-5 EC 3.4.22.58 ICE rel -III Protease ICH-3 Protease TY Cleaved into: Caspase-5 subunit p20; Caspase-5 subunit p10 |
| Gene Name | CASP5 ICH3 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAEDSGKKKRRKNFEAMFKGILQSGLDNFVINHMLKNNVAGQTSIQTLVPNTDQKSTSVKKDNHKKKTVKMLEYLGKDVLHGVFNYLAKHDVLTLKEEEKKKYYDTKIEDKALILVDSLRKNRVAHQMFTQTLLNMDQKITSVKPLLQIEAGPPESAESTNILKLCPREEFLRLCKKNHDEIYPIKKREDRRRLALIICNTKFDHLPARNGAHYDIVGMKRLLQGLGYTVVDEKNLTARDMESVLRAFAARPEHKSSDSTFLVLMSHGILEGICGTAHKKKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGEKHGELWVRDSPASLALISSQSSENLEADSVCKIHEEKDFIAFCSSTPHNVSWRDRTRGSIFITELITCFQKYSCCCHLMEIFRKVQKSFEVPQAKAQMPTIERATLTRDFYLFPGN |
| Enzyme Length | 434 |
| Uniprot Accession Number | P51878 |
| Absorption | |
| Active Site | ACT_SITE 267; /evidence=ECO:0000250|UniProtKB:P29466; ACT_SITE 315; /evidence=ECO:0000269|PubMed:28314590 |
| Activity Regulation | |
| 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:28314590}; |
| DNA Binding | |
| EC Number | 3.4.22.58 |
| Enzyme Function | FUNCTION: Thiol protease that acts as a mediator of programmed cell death (PubMed:29898893, PubMed:28314590). Initiates pyroptosis, a programmed lytic cell death pathway through cleavage of Gasdermin-D (GSDMD): cleavage releases the N-terminal gasdermin moiety (Gasdermin-D, N-terminal) that binds to membranes and forms pores, triggering pyroptosis (PubMed:29898893). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (PubMed:28314590). {ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:29898893}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (6); Chain (2); Domain (1); Erroneous initiation (5); Frameshift (1); Mutagenesis (1); Natural variant (11); Propeptide (2) |
| Keywords | Alternative initiation;Alternative splicing;Apoptosis;Hydrolase;Protease;Reference proteome;Thiol protease;Zymogen |
| Interact With | |
| Induction | INDUCTION: Up-regulated by bacterial lipopolysaccharides (LPS). {ECO:0000269|PubMed:16893518}. |
| Subcellular Location | |
| 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 | 12191486; 12479849; 12964016; 15886296; 16886895; 17418785; 17676485; 18430458; 19074885; 19203830; 19269008; 19270026; 19414860; 19573080; 19604093; 19773279; 20237496; 20379614; 20402676; 20434535; 20635389; 20855536; 21051981; 21191419; 21454616; 21668377; 21700414; 21969293; 25753570; 25943872; 26173988; 26375003; 26508369; 26884849; 28422993; 29158166; 29177860; 29715460; 29891674; 30250284; 30604868; 32109412; 34747049; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,736 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.58; |