Aliases for P2RY1 Gene
External Ids for P2RY1 Gene
The product of this gene 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. [provided by RefSeq, Jul 2008]
GeneCards Summary for P2RY1 Gene
P2RY1 (Purinergic Receptor P2Y, G-Protein Coupled, 1) is a Protein Coding gene. Diseases associated with P2RY1 include extrapulmonary tuberculosis. Among its related pathways are GPCR Pathway and Ras signaling pathway. GO annotations related to this gene include protein heterodimerization activity and scaffold protein binding. An important paralog of this gene is PTAFR.
UniProtKB/Swiss-Prot for P2RY1 Gene
Receptor for extracellular adenine nucleotides such as 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.
P2Y receptors are G-protein-coupled receptors that respond to extracellular purine and pyrimidine nucleotides. To date eight mammalian P2Y receptors are known (P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, P2Y12, P2Y13 and P2Y14) as well as the non-mammalian chick p2y3, Xenopus p2y8 and turkey p2y receptors. p2y9 and p2y10 receptors are considered to be orphan receptors, and p2y5 is now known to actually be a leukotriene B4 receptor. P2Y receptor signaling is mediated through coupling to G proteins, mainly Gq/11, with P2Y12, P2Y13 and P2Y14 signaling through Gi/o. Activation of P2Y receptors initiates a wide range of signaling cascades including PLCbeta, PLD, PLA2, AC and MAPK/MEK kinase. P2Y receptors are found in most human tissues. They have diverse physiological roles including regulation of platelet aggregation, muscle contraction, neurotransmission, and epithelial cell communication and migration.