Precursor of a pore-forming protein involved in the transition from catagen to telogen at the end of hair follicle morphogenesis. This form constitutes the precursor of the pore: upon cleavage, the released N-terminal moiety (Gasdermin-A3, N-terminal) binds to membranes and forms pores, triggering cell death.; Pore-forming protein that causes membrane permeabilization and pyroptosis. Released upon cleavage in vitro of genetically engineered Gsdma3, and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis. Binds to membrane inner leaflet lipids, including bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-bisphosphate, and more weakly to monophosphorylated phosphatidylinositols. Also binds to bacterial and mitochondrial lipids, including cardiolipin, and exhibits bactericidal activity. The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown (Probable). Plays a role in the transition from catagen to telogen at the end of hair follicle morphogenesis, possibly by regulating hair follicle stem cell niche maintenance. Also required for mammary gland development.