Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis (PubMed:15107016). The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria (By similarity). Homooligomer; homooligomerizes to induce formation of the NLRC4 inflammasome (PubMed:25385754, PubMed:33420028). Homooligomerizes following activation by pathogenic proteins (By similarity). Component of the NLRC4 inflammasome, at least composed of NLRC4 and caspase-1 (CASP1) (By similarity). Some NLRC4 inflammasomes contain PYCARD/ASC, while some others directly contact and activate CASP1 (PubMed:25217959). Interacts (via CARD domain) with PYCARD/ASC, pro-caspase-1 (CASP1), NOD2, BCL10 and NALP1 (NAC) by CARD-CARD interaction (PubMed:15107016). Interacts with EIF2AK2/PKR (PubMed:22801494). Isoform 2 is expressed ubiquitously, although highly expressed in lung and spleen. Isoform 1 is highly expressed in lung, followed by leukocytes especially monocytes, lymph node, colon, brain, prostate, placenta, spleen, bone marrow and fetal liver. Isoform 4 is only detected in brain. In an autoinhibited form the C-terminal leucine-rich repeat (LRR) domain is positioned to sterically occlude one side of the NBD domain and consequently sequester NLRC4 in a monomeric state. An ADP-mediated interaction between the NBD and the WHD also contributes to the autoinhibition. Phosphorylated at Ser-533 following infection of macrophages with S.typhimurium (Salmonella). Phosphorylation is essential for NLRC4 inflammasome function to promote caspase-1 activation and pyroptosis. PRKCD phosphorylates Ser-533 in vitro. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.