PILR-alpha (PILRA)

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. PILR-alpha is receptor for PANP.

PILR-alpha (PILRA) Alternative Names

PILR-alpha, PILRA, FDF03 [Homo sapiens]

PILR-alpha, Pilra, FDF03, AV021745 [Mus musculus]

Summaries for PILR-alpha (PILRA)

Entrez Gene summary for PILR-alpha (PILRA):

Cell signaling pathways rely on a dynamic interaction between activating and inhibiting processes. SHP-1-mediated dephosphorylation of protein tyrosine residues is central to the regulation of several cell signaling pathways. Two types of inhibitory receptor superfamily members are immunoreceptor tyrosine-based inhibitory motif (ITIM)-bearing receptors and their non-ITIM-bearing, activating counterparts. Control of cell signaling via SHP-1 is thought to occur through a balance between PILRalpha-mediated inhibition and PILRbeta-mediated activation. These paired immunoglobulin-like receptor genes are located in a tandem head-to-tail orientation on chromosome 7. This particular gene encodes the ITIM-bearing member of the receptor pair, which functions in the inhibitory role. Alternative splicing has been observed at this locus and three variants, each encoding a distinct isoform, are described. [provided by RefSeq, Jul 2008]

Human PILR-alpha (PILRA) Protein General Information

 

• Protein names: Paired immunoglobulin-like type 2 receptor alpha
  Short name=PILR-alpha
• Sequence length: 303 AA.
• 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.
• Sequence similarities: Contains 1 Ig-like V-type (immunoglobulin-like) domain.
• Post-translational modification: N- and O-glycosylated. , only N-glycosylated.
  Phosphorylated on tyrosine residues.
• 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.
• Subcellular location: 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.
• 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.

General information above from UniProt

Function for PILR-alpha (PILRA) Protein

UniProtKB:

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. PILR-alpha is receptor for PANP.

Genatlas:

• PILR-alpha may act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6 and PTPN11 that block signal transduction through dephosphorylation of signaling molecules
• PILR-alpha is coreceptor for HSV-1 infection
• Importance of PILRA and PILRB in innate immunity and the control of inflammation
• PANP and PILRA interactions might be involved in neural immune disorders such as multiple sclerosis

Homology for human PILR-alpha (PILRA)

• homolog to PILR(BETA)