This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-A2, 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-A2, 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-A2, N-terminal). Homooligomer; homooligomeric ring-shaped pore complex containing 27-28 subunits when inserted in the membrane. Expressed in the gastrointestinal tract, specifically from the middle to the upper region of the gastric mucosa in the glandular stomach. Expression is first detected at 16.6-17.5 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-A2, N-terminal) that initiates pyroptosis. Belongs to the gasdermin family.