PILRA

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Identifiers
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External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
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Wikidata
View/Edit Human

Paired immunoglobin like type 2 receptor alpha is a protein that in humans is encoded by the PILRA gene.

Function

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.

Further reading

• Tabata S, Kuroki K, Maita N, Wang J, Shiratori I, Arase H, Kohda D, Maenaka K (2008). "Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor alpha (PILRalpha)". Acta Crystallographica Section F. 64 (Pt 1): 44–6. doi:10.1107/S1744309107065384. PMC 2373998. PMID 18097101.
• Satoh T, Arii J, Suenaga T, Wang J, Kogure A, Uehori J, Arase N, Shiratori I, Tanaka S, Kawaguchi Y, Spear PG, Lanier LL, Arase H (2008). "PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B". Cell. 132 (6): 935–44. doi:10.1016/j.cell.2008.01.043. PMC 2394663. PMID 18358807.
• Arii J, Uema M, Morimoto T, Sagara H, Akashi H, Ono E, Arase H, Kawaguchi Y (2009). "Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor alpha". J. Virol. 83 (9): 4520–7. doi:10.1128/JVI.02601-08. PMC 2668467. PMID 19244335.
• Fan Q, Lin E, Satoh T, Arase H, Spear PG (2009). "Differential effects on cell fusion activity of mutations in herpes simplex virus 1 glycoprotein B (gB) dependent on whether a gD receptor or a gB receptor is overexpressed". J. Virol. 83 (15): 7384–90. doi:10.1128/JVI.00087-09. PMC 2708615. PMID 19457990.
• Kogure A, Shiratori I, Wang J, Lanier LL, Arase H (2011). "PANP is a novel O-glycosylated PILRα ligand expressed in neural tissues". Biochem. Biophys. Res. Commun. 405 (3): 428–33. doi:10.1016/j.bbrc.2011.01.047. PMC 4089865. PMID 21241660.
• Sun Y, Senger K, Baginski TK, Mazloom A, Chinn Y, Pantua H, Hamidzadeh K, Ramani SR, Luis E, Tom I, Sebrell A, Quinones G, Ma Y, Mukhyala K, Sai T, Ding J, Haley B, Shadnia H, Kapadia SB, Gonzalez LC, Hass PE, Zarrin AA (2012). "Evolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands". J. Biol. Chem. 287 (19): 15837–50. doi:10.1074/jbc.M111.286633. PMC 3346071. PMID 22396535.
• Chowdhury S, Naderi M, Chouljenko VN, Walker JD, Kousoulas KG (2012). "Amino acid differences in glycoproteins B (gB), C (gC), H (gH) and L (gL) are associated with enhanced herpes simplex virus type-1 (McKrae) entry via the paired immunoglobulin-like type-2 receptor α". Virol. J. 9: 112. doi:10.1186/1743-422X-9-112. PMC 3402990. PMID 22695228.
• Chowdhury S, Chouljenko VN, Naderi M, Kousoulas KG (2013). "The amino terminus of herpes simplex virus 1 glycoprotein K is required for virion entry via the paired immunoglobulin-like type-2 receptor alpha". J. Virol. 87 (6): 3305–13. doi:10.1128/JVI.02982-12. PMC 3592154. PMID 23302878.
• Lun YZ, Chi Q, Wang XL, Wang F, Sui W (2014). "Identification of paired immunoglobulin-like type 2 receptor α as hepatitis B virus DNA polymerase transactivated protein 1 interacting proteins". Mol Med Rep. 9 (2): 720–4. doi:10.3892/mmr.2013.1813. PMID 24253495.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.