CASP5

This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. Overexpression of the active form of this enzyme induces apoptosis in fibroblasts. Max, a central component of the Myc/Max/Mad transcription regulation network important for cell growth, differentiation, and apoptosis, is cleaved by this protein; this process requires Fas-mediated dephosphorylation of Max. The expression of this gene is regulated by interferon-gamma and lipopolysaccharide. Alternatively spliced transcript variants have been identified for this gene. [provided by RefSeq, Aug 2010]

Caspase 5

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).

Apoptotic process Source: ProtInc
Cellular response to mechanical stimulus Source: UniProtKB
Execution phase of apoptosis Source: GOC
Proteolysis Source: ProtInc
Regulation of apoptotic process Source: InterPro
Regulation of inflammatory response Source: GO_Central
Substantia nigra development Source: UniProtKB

NLRP1 inflammasome complex; Cytoplasm

The two subunits are derived from the precursor sequence by an autocatalytic mechanism.