C-type lectin domain family 12 protein A, CLEC12A CLL7, DCAL2, MICL, of 265 aas and 1 TMS near its N-terminus. It is a cell surface receptor that modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases in granulocytes and monocytes (Marshall et al. 2004). It alters dendrieic cell maturation and cytokine production (Chen et al. 2006). It is also a myeloid inhibitory receptor that negatively regulates inflammation in autoimmune and autoinflammatory arthritis (Vitry et al. 2021). Similarly to other C-type lectin receptors, CLEC12A harbours a stalk domain between its ligand binding and transmembrane domains. The stalk cysteines in CLEC12A differentially modulate this inhibitory receptor's expression, oligomerisation and signaling, suggestive of the regulation of CLEC12A in a redox-dependent manner during inflammation (Vitry et al. 2021).  Clec12a inhibits MSU-induced immune activation through lipid raft expulsion (Xu et al. 2023). The transmembrane domain of Clec12a disrupts monosodium uric acid (MSU)-induced lipid raft recruitment and thus attenuates downstream signals. Single amino acid mutagenesis study showed the critical role of phenylalanine in the transmembrane region for the interactions between C-type lectin receptors and lipid rafts, which is critical for the regulation of MSU-mediated lipid sorting and phagocyte activation. This indicates the molecular mechanisms of solid particle-induced immune activation (Xu et al. 2023).