Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (  , ). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins ( , ). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond ( , ). Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain (By similarity). Cleaves and activates caspase-6, -7 and -9 . Involved in the cleavage of huntingtin . Triggers cell adhesion in sympathetic neurons through RET cleavage . Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress . Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction . Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (, ). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (, ).
Subcellular locations: Cytoplasm
Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.