Abundant protease in the cytosolic granules of cytotoxic T- cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:1985927, PubMed:3262682, PubMed:3263427). It cleaves after Asp (PubMed:1985927, PubMed:8258716). Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore- forming moiety of GSDME, thereby triggering pyroptosis and target cell death (PubMed:31953257, PubMed:32188940). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -9 and -10 (CASP3, CASP9 and CASP10, respectively) to give rise to active enzymes mediating apoptosis (PubMed:9852092). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity). {ECO:0000250|UniProtKB:P04187, ECO:0000269|PubMed:1985927, ECO:0000269|PubMed:31953257, ECO:0000269|PubMed:32188940, ECO:0000269|PubMed:3262682, ECO:0000269|PubMed:3263427, ECO:0000269|PubMed:8258716, ECO:0000269|PubMed:9852092}. This is the function of ENSG00000100453 (GZMB, granzyme B).