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)
End	152,841,439 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	60,916,403 bp
RNA expression pattern
	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
	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
	5028
	18441
	ENSG00000169860
	ENSMUSG00000027765
	P47900
	P49650
	NM_002563
	NM_001282016; NM_008772
	NP_002554
	NP_001268945; NP_032798
	Wikidata
View/Edit Human	View/Edit Mouse

P2Y purinoceptor 1 is a protein that in humans is encoded by the P2RY1 gene.^[5]

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.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000169860 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000027765 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ayyanathan K, Webbs TE, Sandhu AK, Athwal RS, Barnard EA, Kunapuli SP (January 1996). "Cloning and chromosomal localization of the human P2Y1 purinoceptor". Biochemical and Biophysical Research Communications. 218 (3): 783–8. doi:10.1006/bbrc.1996.0139. PMID 8579591.
^ "Entrez Gene: P2RY1 purinergic receptor P2Y, G-protein coupled, 1".

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. S2CID 10518131.
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. S2CID 28971344.
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.
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. Bibcode:1998PNAS...95.8496H. 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. Bibcode:2001PNAS...98.7617Y. 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. S2CID 30936205.
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 (BBA) - Gene Structure and Expression. 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. S2CID 43212335.
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. S2CID 30407515.
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. S2CID 13637415.
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. S2CID 19101147.

External links

"P2Y Receptors: P2Y₁". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Archived from the original on 2016-03-03. Retrieved 2008-12-09.

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

This transmembrane receptor-related article is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000169860 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000027765 – 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.

[pmid8579591-5] Ayyanathan K, Webbs TE, Sandhu AK, Athwal RS, Barnard EA, Kunapuli SP (January 1996). "Cloning and chromosomal localization of the human P2Y1 purinoceptor". Biochemical and Biophysical Research Communications. 218 (3): 783–8. doi:10.1006/bbrc.1996.0139. PMID 8579591.

[entrez-6] "Entrez Gene: P2RY1 purinergic receptor P2Y, G-protein coupled, 1".

[1]

[2]

[3]

[4]

[5]

[6]

P2RY1

P2RY1

P2RY1

Add your contribution

Hub overview

Root Wikipedia Article

P2RY1

Function

See also

References

Further reading

External links