P2RY1

P2RY1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4XNV, 4XNW
Identifiers
Aliases	P2RY1, P2Y1, purinergic receptor P2Y1, SARCC
External IDs	OMIM: 601167; MGI: 105049; HomoloGene: 1926; GeneCards: P2RY1; OMA:P2RY1 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3q25.2 Start 152,835,131 bp End 152,841,439 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 E1 Start 60,910,216 bp End 60,916,403 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gingival epithelium endothelial cell oral cavity internal globus pallidus visceral pleura amniotic fluid placenta nucleus accumbens tibia lower lobe of lung Top expressed in lumbar spinal ganglion duodenum islet of Langerhans granulocyte jejunum esophagus lip muscle of thigh embryo right kidney More reference expression data BioGPS More reference expression data
Gene ontology Molecular function A1 adenosine receptor binding G protein-coupled receptor activity scaffold protein binding ADP binding G protein-coupled purinergic nucleotide receptor activity signal transducer activity protein binding protein heterodimerization activity G protein-coupled ATP receptor activity ATP binding nucleotide binding signaling receptor activity Cellular component cell body integral component of membrane postsynaptic membrane membrane plasma membrane integral component of plasma membrane cell surface dendrite basolateral plasma membrane apical plasma membrane mitochondrion postsynaptic density glutamatergic synapse integral component of presynaptic active zone membrane cilium Biological process hemostasis cellular response to organic cyclic compound G protein-coupled adenosine receptor signaling pathway positive regulation of protein phosphorylation adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway eating behavior positive regulation of cytosolic calcium ion concentration response to mechanical stimulus ageing regulation of signaling receptor activity negative regulation of norepinephrine secretion signal transduction involved in regulation of gene expression wound healing G protein-coupled purinergic nucleotide receptor signaling pathway phospholipase C-activating G protein-coupled receptor signaling pathway cell surface receptor signaling pathway positive regulation of inositol trisphosphate biosynthetic process negative regulation of binding positive regulation of ion transport positive regulation of ERK1 and ERK2 cascade sensory perception of pain response to growth factor positive regulation of penile erection protein localization to plasma membrane positive regulation of hormone secretion relaxation of muscle positive regulation of transcription by RNA polymerase II glial cell migration signal transduction blood coagulation platelet activation blood vessel diameter maintenance G protein-coupled receptor signaling pathway regulation of cell shape cellular response to ATP cellular response to purine-containing compound regulation of presynaptic cytosolic calcium ion concentration regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5028 18441 Ensembl ENSG00000169860 ENSMUSG00000027765 UniProt P47900 P49650 RefSeq (mRNA) NM_002563 NM_001282016 NM_008772 RefSeq (protein) NP_002554 NP_001268945 NP_032798 Location (UCSC) Chr 3: 152.84 – 152.84 Mb Chr 3: 60.91 – 60.92 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

P2Y purinoceptor 1 is a protein that in humans is encoded by the P2RY1 gene.

Function

The product of this gene, P2Y₁ belongs to the family of G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor functions as a receptor for extracellular ATP and ADP. In platelets binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and probably to platelet aggregation.

See also

• P2Y receptor

Further reading

• Janssens R, Communi D, Pirotton S, Samson M, Parmentier M, Boeynaems JM (April 1996). "Cloning and tissue distribution of the human P2Y1 receptor". Biochemical and Biophysical Research Communications. 221 (3): 588–93. doi:10.1006/bbrc.1996.0640. PMID 8630005.
• Léon C, Vial C, Cazenave JP, Gachet C (June 1996). "Cloning and sequencing of a human cDNA encoding endothelial P2Y1 purinoceptor". Gene. 171 (2): 295–7. doi:10.1016/0378-1119(96)00027-3. PMID 8666290.
• Léon C, Hechler B, Vial C, Leray C, Cazenave JP, Gachet C (February 1997). "The P2Y1 receptor is an ADP receptor antagonized by ATP and expressed in platelets and megakaryoblastic cells". FEBS Letters. 403 (1): 26–30. doi:10.1016/S0014-5793(97)00022-7. PMID 9038354.
• Ayyanathan K, Naylor SL, Kunapuli SP (September 1996). "Structural characterization and fine chromosomal mapping of the human P2Y1 purinergic receptor gene (P2RY1)". Somatic Cell and Molecular Genetics. 22 (5): 419–24. doi:10.1007/BF02369897. PMID 9039850.
• Maier R, Glatz A, Mosbacher J, Bilbe G (August 1997). "Cloning of P2Y6 cDNAs and identification of a pseudogene: comparison of P2Y receptor subtype expression in bone and brain tissues". Biochemical and Biophysical Research Communications. 237 (2): 297–302. doi:10.1006/bbrc.1997.7135. PMID 9268704.
• Jin J, Daniel JL, Kunapuli SP (January 1998). "Molecular basis for ADP-induced platelet activation. II. The P2Y1 receptor mediates ADP-induced intracellular calcium mobilization and shape change in platelets". The Journal of Biological Chemistry. 273 (4): 2030–4. doi:10.1074/jbc.273.4.2030. PMID 9442040.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Hall RA, Ostedgaard LS, Premont RT, Blitzer JT, Rahman N, Welsh MJ, Lefkowitz RJ (July 1998). "A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins". Proceedings of the National Academy of Sciences of the United States of America. 95 (15): 8496–501. doi:10.1073/pnas.95.15.8496. PMC 21104. PMID 9671706.
• Sabala P, Czajkowski R, Przybyłek K, Kalita K, Kaczmarek L, Barańska J (January 2001). "Two subtypes of G protein-coupled nucleotide receptors, P2Y(1) and P2Y(2) are involved in calcium signalling in glioma C6 cells". British Journal of Pharmacology. 132 (2): 393–402. doi:10.1038/sj.bjp.0703843. PMC 1572584. PMID 11159687.
• Yoshioka K, Saitoh O, Nakata H (June 2001). "Heteromeric association creates a P2Y-like adenosine receptor". Proceedings of the National Academy of Sciences of the United States of America. 98 (13): 7617–22. doi:10.1073/pnas.121587098. PMC 34717. PMID 11390975.
• James G, Butt AM (October 2001). "Changes in P2Y and P2X purinoceptors in reactive glia following axonal degeneration in the rat optic nerve". Neuroscience Letters. 312 (1): 33–6. doi:10.1016/S0304-3940(01)02189-9. PMID 11578839.
• Moore DJ, Chambers JK, Wahlin JP, Tan KB, Moore GB, Jenkins O, Emson PC, Murdock PR (October 2001). "Expression pattern of human P2Y receptor subtypes: a quantitative reverse transcription-polymerase chain reaction study". Biochimica et Biophysica Acta. 1521 (1–3): 107–19. doi:10.1016/S0167-4781(01)00291-3. PMID 11690642.
• Czajkowski R, Lei L, Sabała P, Barańska J (February 2002). "ADP-evoked phospholipase C stimulation and adenylyl cyclase inhibition in glioma C6 cells occur through two distinct nucleotide receptors, P2Y(1) and P2Y(12)". FEBS Letters. 513 (2–3): 179–83. doi:10.1016/S0014-5793(02)02255-X. PMID 11904146.
• Aktas B, Hönig-Liedl P, Walter U, Geiger J (August 2002). "Inhibition of platelet P2Y12 and alpha2A receptor signaling by cGMP-dependent protein kinase". Biochemical Pharmacology. 64 (3): 433–9. doi:10.1016/S0006-2952(02)01113-9. PMID 12147294.
• Nurden P, Poujol C, Winckler J, Combrié R, Pousseau N, Conley PB, Levy-Toledano S, Habib A, Nurden AT (February 2003). "Immunolocalization of P2Y1 and TPalpha receptors in platelets showed a major pool associated with the membranes of alpha -granules and the open canalicular system". Blood. 101 (4): 1400–8. doi:10.1182/blood-2002-02-0642. PMID 12393588.
• Burrell HE, Bowler WB, Gallagher JA, Sharpe GR (March 2003). "Human keratinocytes express multiple P2Y-receptors: evidence for functional P2Y1, P2Y2, and P2Y4 receptors". The Journal of Investigative Dermatology. 120 (3): 440–7. doi:10.1046/j.1523-1747.2003.12050.x. PMID 12603858.
• Jagroop IA, Burnstock G, Mikhailidis DP (February 2003). "Both the ADP receptors P2Y1 and P2Y12, play a role in controlling shape change in human platelets". Platelets. 14 (1): 15–20. doi:10.1080/0953710021000062914. PMID 12623443.
• Greig AV, Linge C, Terenghi G, McGrouther DA, Burnstock G (June 2003). "Purinergic receptors are part of a functional signaling system for proliferation and differentiation of human epidermal keratinocytes". The Journal of Investigative Dermatology. 120 (6): 1007–15. doi:10.1046/j.1523-1747.2003.12261.x. PMID 12787128.
• Wang L, Ostberg O, Wihlborg AK, Brogren H, Jern S, Erlinge D (February 2003). "Quantification of ADP and ATP receptor expression in human platelets". Journal of Thrombosis and Haemostasis. 1 (2): 330–6. doi:10.1046/j.1538-7836.2003.00070.x. PMID 12871508.

External links

• "P2Y Receptors: P2Y₁". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.

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