C-type lectin domain family 12 member B (CLEC12B)

C-type lectin domain family 12 member B (CLEC12B) is a membrane-bound inhibitory receptor primarily expressed on myeloid cells. It is characterized by an extracellular C-type lectin-like domain and a cytoplasmic immunoreceptor tyrosine-based inhibition motif (ITIM)[3][1]. Upon activation and phosphorylation, CLEC12B recruits SH2 domain-containing tyrosine phosphatases (SHP-1 and SHP-2), antagonizing activating signals within immune cells and contributing to immune homeostasis and protection of target tissues against natural killer cell-mediated lysis. CLEC12B is involved in processes such as regulation of melanocyte proliferation, inhibition of signal transduction, and modulation of immune cell activation during infection and inflammation. Genetic associations include cone-rod dystrophy 1[1][4][7]. No known direct drug interactions or biomarker uses have been identified for CLEC12B at this time.

Other names

Macrophage antigen HTestis secretory sperm-binding protein Li 205aUNQ5782/PRO16089CLEC12BC-type lectin domain family 12 member B, macrophage antigen hUNQ5782Macrophage antigen h

Recruitment of phosphatases SHP-1 (PTPN6) and SHP-2 (PTPN11) to its immunoreceptor tyrosine-based inhibition motif (ITIM), resulting in antagonism of activating immune cell signals and downregulation of specific cell activation pathways[1][3][7].