PILRA
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.
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.
(Microbial infection) Acts as an entry co-receptor for herpes simplex virus 1.
Post-translational modifications
According to PubMed:10660620, N- and O-glycosylated. According to PubMed:10903717, only N-glycosylated.
Phosphorylated on tyrosine residues.
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.
Cellular localization
- Isoform 1
- Cell membrane
- Single-pass type I membrane protein
- Isoform 2
- Cell membrane
- Single-pass type I membrane protein
- Isoform 3
- Secreted
- Isoform 4
- Secreted
Alternative names
Paired immunoglobulin-like type 2 receptor alpha, Cell surface receptor FDF03, Inhibitory receptor PILR-alpha, PILRA