PILRA Antibody – Mouse Monoclonal

Function: 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. Ref.2 Ref.5 Ref.7

Subunit structure: Monomer. Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon tyrosine phosphorylation. Interacts with herpes simplex virus 1 glycoprotein B; functions as an entry coreceptor for this virus. Ref.1 Ref.2 Ref.5

Subcellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein

Potential. Isoform 2: Cell membrane; Single-pass type I membrane protein

Potential. Isoform 3: Secreted

Potential. Isoform 4: Secreted

Potential.

Tissue specificity: 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. Ref.2

Domain: 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.

Post-translational modification: According to Ref.1, N- and O-glycosylated. According to Ref.2, only N-glycosylated. Ref.1 Ref.2Phosphorylated on tyrosine residues. Ref.1 Ref.2

Sequence similarities: Contains 1 Ig-like V-type (immunoglobulin-like) domain.