PILRA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPILRA, FDF03, paired immunoglobin like type 2 receptor alpha
External IDsOMIM: 605341 MGI: 2450529 HomoloGene: 8387 GeneCards: PILRA
Orthologs
SpeciesHumanMouse
Entrez

29992

231805

Ensembl

ENSG00000085514

ENSMUSG00000046245

UniProt

Q9UKJ1

Q2YFS3

RefSeq (mRNA)

NM_178273
NM_013439
NM_178272

NM_153510

RefSeq (protein)

NP_038467
NP_840056
NP_840057

NP_705730

Location (UCSC)Chr 7: 100.37 – 100.4 MbChr 5: 137.82 – 137.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Paired immunoglobin like type 2 receptor alpha is a protein that in humans is encoded by the PILRA gene. [5]

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.

In contrast to PILRbeta, which has only one known natural ligand, PILRalpha has many known protein-protein interactions.[6] PILRalpha recruits PTPN6 and PTPN1 via interactions of its ITIM motifs.[7] PILRalpha is also used by some viruses, notably HSV-1, for cell entry.[6][8]

Structure

As with other paired receptors, PILRalpha has a longer cytoplasmic tail compared to PILRbeta and features two intracellular ITIM motifs.[7][9] PILRalpha has an extracellular domain with a siglec-like immunoglobulin fold that substitutes hydrophobic interactions for the siglec fold's characteristic disulfide bond. The structure of this domain is very similar to that of PILRbeta, but the two proteins nevertheless have different binding affinities for sialic acid.[6]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000085514 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000046245 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ "Entrez Gene: Paired immunoglobin like type 2 receptor alpha". Retrieved 2017-01-10.
  6. 1 2 3 Lu Q, Lu G, Qi J, Wang H, Xuan Y, Wang Q, et al. (June 2014). "PILRα and PILRβ have a siglec fold and provide the basis of binding to sialic acid". Proceedings of the National Academy of Sciences of the United States of America. 111 (22): 8221–6. Bibcode:2014PNAS..111.8221L. doi:10.1073/pnas.1320716111. PMC 4050567. PMID 24843130.
  7. 1 2 Mousseau DD, Banville D, L'Abbé D, Bouchard P, Shen SH (February 2000). "PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta". The Journal of Biological Chemistry. 275 (6): 4467–74. doi:10.1074/jbc.275.6.4467. PMID 10660620.
  8. ↑ Furukawa A, Kakita K, Yamada T, Ishizuka M, Sakamoto J, Hatori N, et al. (December 2017). "Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILRα immune cell receptor". The Journal of Biological Chemistry. 292 (51): 21128–21136. doi:10.1074/jbc.M117.799239. PMC 5743085. PMID 29046357.
  9. ↑ Wilson MD, Cheung J, Martindale DW, Scherer SW, Koop BF (November 2006). "Comparative analysis of the paired immunoglobulin-like receptor (PILR) locus in six mammalian genomes: duplication, conversion, and the birth of new genes". Physiological Genomics. 27 (3): 201–18. doi:10.1152/physiolgenomics.00284.2005. PMID 16926269.

Further reading

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

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