CASP5
Function
Thiol protease that acts as a mediator of programmed cell death (PubMed:28314590, PubMed:29898893). 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). Also mediates cleavage and maturation of IL18 (PubMed:37993714). Cleavage of GSDMD and IL18 is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP4 (PubMed:37993714). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (PubMed:28314590).
Post-translational modifications
The two subunits are derived from the precursor sequence by an autocatalytic mechanism.
Sequence Similarities
Belongs to the peptidase C14A family.
Tissue Specificity
Expressed in barely detectable amounts in most tissues except brain, highest levels being found in lung, liver and skeletal muscle.
Alternative names
ICH3, CASP5, Caspase-5, CASP-5, ICE(rel)-III, Protease ICH-3, Protease TY