P2RX3

P2RX3
Identifiers
Aliases	P2RX3, P2X3, purinergic receptor P2X 3
External IDs	OMIM: 600843; MGI: 1097160; HomoloGene: 1922; GeneCards: P2RX3; OMA:P2RX3 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q12.1 Start 57,338,352 bp End 57,372,396 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 D Start 84,998,583 bp End 85,037,462 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gonad testicle apex of heart left testis right testis left ventricle right lobe of liver left adrenal cortex right adrenal gland striated muscle tissue Top expressed in lumbar spinal ganglion spermatid ganglion of vagus nerve trigeminal ganglion blastocyst seminiferous tubule greater petrosal nerve spermatocyte neural tube tail of embryo More reference expression data BioGPS n/a
Gene ontology Molecular function purinergic nucleotide receptor activity ion channel activity ATP binding extracellularly ATP-gated cation channel activity nucleotide binding ATP-gated ion channel activity Cellular component integral component of membrane rough endoplasmic reticulum Golgi apparatus membrane receptor complex dendritic spine integral component of nuclear inner membrane integral component of plasma membrane soma terminal bouton axon membrane raft neuron projection plasma membrane Schaffer collateral - CA1 synapse hippocampal mossy fiber to CA3 synapse integral component of presynaptic membrane Biological process peristalsis response to ATP response to hypoxia positive regulation of calcium-mediated signaling positive regulation of calcium ion transport into cytosol urinary bladder smooth muscle contraction response to mechanical stimulus cation transport response to heat ion transport behavioral response to formalin induced pain response to organic substance cation transmembrane transport regulation of synaptic plasticity neuromuscular synaptic transmission positive regulation of sensory perception of pain behavioral response to pain response to cold protein homooligomerization response to carbohydrate sensory perception of taste signal transduction neuronal action potential response to temperature stimulus chemical synaptic transmission purinergic nucleotide receptor signaling pathway blood coagulation excitatory postsynaptic potential protein homotrimerization cellular response to ATP modulation of chemical synaptic transmission ion transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5024 228139 Ensembl ENSG00000109991 ENSMUSG00000027071 UniProt P56373 Q3UR32 RefSeq (mRNA) NM_002559 NM_145526 RefSeq (protein) NP_002550 NP_663501 Location (UCSC) Chr 11: 57.34 – 57.37 Mb Chr 2: 85 – 85.04 Mb PubMed search
Wikidata
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P2X purinoceptor 3 is a protein that in humans is encoded by the P2RX3 gene.

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel and may transduce ATP-evoked nociceptor activation. Mouse studies suggest that this receptor is important for peripheral pain responses, and also participates in pathways controlling urinary bladder volume reflexes, platelet aggregation, macrophage activation, apoptosis and neuronal–glial interactions. It is possible that the development of selective antagonists for this receptor may have a therapeutic potential in pain relief and in the treatment of disorders of urine storage.

Ligands

Antagonists

Not true antagonists, but negative allosteric modulators:

• Camlipixant (BLU-5937)
• Gefapixant
• Opiranserin
• Quercetin
• PSFL2915

See also

• P2X purinoreceptor
• Purinergic receptor
• Ligand-gated ion channel
• Nociceptor

Further reading

• North RA (October 2002). "Molecular physiology of P2X receptors". Physiological Reviews. 82 (4): 1013–1067. doi:10.1152/physrev.00015.2002. PMID 12270951.
• Jarvis MF (August 2003). "Contributions of P2X3 homomeric and heteromeric channels to acute and chronic pain". Expert Opinion on Therapeutic Targets. 7 (4): 513–522. doi:10.1517/14728222.7.4.513. PMID 12885270. S2CID 25459817.
• Kennedy C, Leff P (October 1995). "Painful connection for ATP". Nature. 377 (6548): 385–386. Bibcode:1995Natur.377..385K. doi:10.1038/377385a0. PMID 7566110. S2CID 4315283.
• Lewis C, Neidhart S, Holy C, North RA, Buell G, Surprenant A (October 1995). "Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons". Nature. 377 (6548): 432–435. Bibcode:1995Natur.377..432L. doi:10.1038/377432a0. PMID 7566120. S2CID 4361850.
• Garcia-Guzman M, Soto F, Gomez-Hernandez JM, Lund PE, Stühmer W (January 1997). "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue". Molecular Pharmacology. 51 (1): 109–118. doi:10.1124/mol.51.1.109. PMID 9016352.
• Cook SP, McCleskey EW (October 2000). "ATP, pain and a full bladder". Nature. 407 (6807): 951–952. Bibcode:2000Natur.407..951C. doi:10.1038/35039648. PMID 11069162. S2CID 4367628.
• Renton T, Yiangou Y, Baecker PA, Ford AP, Anand P (2003). "Capsaicin receptor VR1 and ATP purinoceptor P2X3 in painful and nonpainful human tooth pulp". Journal of Orofacial Pain. 17 (3): 245–250. PMID 14520770.
• Mason HS, Bourke S, Kemp PJ (December 2004). "Selective modulation of ligand-gated P2X purinoceptor channels by acute hypoxia is mediated by reactive oxygen species". Molecular Pharmacology. 66 (6): 1525–1535. doi:10.1124/mol.104.000851. PMID 15331767. S2CID 24536809.
• Fabbretti E, Sokolova E, Masten L, D'Arco M, Fabbro A, Nistri A, et al. (December 2004). "Identification of negative residues in the P2X3 ATP receptor ectodomain as structural determinants for desensitization and the Ca2+-sensing modulatory sites". The Journal of Biological Chemistry. 279 (51): 53109–53115. doi:10.1074/jbc.M409772200. PMID 15475563.
• Brown DA, Yule DI (February 2007). "Protein kinase C regulation of P2X3 receptors is unlikely to involve direct receptor phosphorylation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1773 (2): 166–175. doi:10.1016/j.bbamcr.2006.09.020. PMC 1861828. PMID 17052768.

External links

• P2RX3+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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