Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP. (Microbial infection) Acts as an entry co-receptor for herpes simplex virus 1. Monomer. Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon tyrosine phosphorylation. (Microbial infection) Interacts with herpes simplex virus 1 glycoprotein B. Predominantly detected in hemopoietic tissues and is expressed by monocytes, macrophages, and granulocytes, but not by lymphocytes. Also strongly expressed by dendritic cells (DC); preferentially by CD14+/CD1a- DC derived from CD34+ progenitors. Also expressed by CD11c+ blood and tonsil DC, but not by CD11c- DC precursors. Contains 2 copies 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. PTPN6 seems to bind predominantly to the first ITIM motif. According to PubMed:10660620, N- and O-glycosylated. According to PubMed:10903717, only N-glycosylated. Phosphorylated on tyrosine residues.