This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-A, N-terminal) binds to membranes and forms pores, triggering cell death. Pore-forming protein that causes membrane permeabilization and pyroptosis. Released upon cleavage of Gasdermin-A, 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, such as phosphatidylinositol (4,5)-bisphosphate. The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown. The full-length protein before cleavage is inactive: intramolecular interactions between N- and C-terminal domains mediate autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the released N-terminal moiety (Gasdermin-A, N-terminal). Homooligomer; homooligomeric ring-shaped pore complex containing 27-28 subunits when inserted in the membrane. Expressed predominantly in the gastrointestinal (GI) tract and in the skin at a lower level. In the GI tract, the expression is highly restricted to the esophagus and forestomach. Expression is first detected at 12.5 dpc. Intramolecular interactions between N- and C-terminal domains are important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain. Cleavage relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-A, N-terminal) that initiates pyroptosis. Belongs to the gasdermin family.