This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-C, N-terminal) binds to membranes and forms pores, triggering cell death. Pore-forming protein that causes membrane permeabilization and pyroptosis (By similarity). Released upon cleavage and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis (By similarity). The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown (By similarity). 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-C, N-terminal). Homooligomer; homooligomeric ring-shaped pore complex containing 27-28 subunits when inserted in the membrane. 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-C, N-terminal) that initiates pyroptosis. Belongs to the gasdermin family. Despite its name, does not contains a functional leucine zipper.