Inhibitory receptor postulated to negatively regulate immune and non-immune functions (PubMed:17562706, PubMed:34310951). Upon phosphorylation, recruits SH2 domain-containing PTPN6 and PTPN11 phosphatases to its ITIM motif and antagonizes activation signals (PubMed:17562706, PubMed:34310951). Although it inhibits KLRK1/NKG2D-mediated signaling, it does not bind known ligands of KLRK1/NKG2D and therefore is not its inhibitory counterpart (PubMed:17562706). May limit activation of myeloid cell subsets in response to infection or tissue inflammation (PubMed:17562706). May protect target cells against natural killer cell-mediated lysis (PubMed:17562706). May negatively regulate cell cycle and differentiation of melanocytes via inactivation of STAT3 (PubMed:34310951). Homodimer. Interacts (via ITIM motif) with PTPN6 (PubMed:17562706). Interacts (via ITIM motif) with PTPN11; this interaction triggers dephosphorylation and activation of PTPN11 (PubMed:17562706, PubMed:34310951). Detected in colon, heart, kidney, liver, lung, mammary gland, ovary, spleen and testis (PubMed:17562706). Expressed in melanocytes (at protein level) (PubMed:34310951). Up-regulated upon differentiation of monocytes to macrophages. Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. N-glycosylated.