Alternative titles; symbols
HGNC Approved Gene Symbol: P2RY13
Cytogenetic location: 3q25.1 Genomic coordinates (GRCh38): 3:151,326,312-151,329,549 (from NCBI)
G protein-coupled receptors, such as GPR86, play a role in cell communication. They are characterized by an extracellular N terminus, 7 transmembrane regions, and an intracellular C terminus (summary by Wittenberger et al., 2001).
By batch EST database searching, Wittenberger et al. (2001) identified a cDNA encoding GPR86. The deduced 333-amino acid protein lacks a leader peptide but possesses a DRF motif. Northern blot analysis revealed wide expression of a 2.9-kb GPR86 transcript in spleen, with weaker expression in placenta, leukocytes, and brain. In brain, expression was strongest in substantia nigra, thalamus, and medulla.
Lee et al. (2001) identified GPR86, which they designated GPR94, in a genomic database using sequences of a related GPR as query. They designed PCR primers to amplify and clone GPR86 from a genomic library. Full-length GPR86 encodes a deduced 333-amino acid protein that shares 51 to 57% identity in the transmembrane regions with the platelet ADP receptor P2Y12 (600515), the UDP-glucose receptor, and GPR87 (606379). Northern blot analysis of human brain tissues detected a 3.2-kb transcript in frontal cortex, caudate putamen, and thalamus, but not in hippocampus, pons, or cerebellum.
Communi et al. (2001) cloned GPR86 from human spleen cDNA by PCR using primers based on the genomic sequence. The predicted GPR86 protein contains 3 N-glycosylation sites, 2 protein kinase C sites, and a protein kinase A site. By RT-PCR, Communi et al. (2001) found strong expression of GPR86 in spleen and adult brain, lower expression in placenta, lung, liver, spinal cord, thymus, small intestine, uterus, stomach, testis, fetal brain, and adrenal gland, and no expression in pancreas, heart, kidney, skeletal muscle, ovary, or fetal aorta. Expression was clearly detected in lymph node and bone marrow and weakly detected in peripheral blood mononuclear cells and leukocytes. Expression was also obtained by PCR of all brain regions examined.
Bruneau and Lombardo (1995) showed that a multiprotein complex, including Grp94, plays an essential role in the folding of BSDL (CEL; 114840) in rat pancreas. Bruneau et al. (1998) showed that BSDL and Grp94 antigenic sites in rat were associated all along the secretory pathway and, upon secretion, remained associated in the pancreatic juice when transported from the pancreas to the intestinal lumen. In pancreatic juice, the proteins appeared as a complex of 180 kD containing at least one each of p94 and BSDL molecules, interacting by hydrophobic forces. Grp94 and BSDL were detected on microvilli and in the endosomal compartment of enterocytes. Both proteins dissociated in the late endosomal compartment and BSDL, but not Grp94, was transferred to the basolateral membrane.
Communi et al. (2001) determined that GPR86 shows a high affinity for ADP through pharmacologic characterization of GPR86-transfected human astrocytoma cells and CHO cells. Stimulation of GPR86 by ADP in stably expressing CHO cells resulted in inhibition of adenylyl cyclase and the phosphorylation of the MAP kinases Erk1 (601795) and Erk2 (176948). Communi et al. (2001) noted that inhibition of adenylyl cyclase and phosphorylation of the MAP kinases are transduction mechanisms that involve Gi proteins (see 139310).
By genomic sequence analysis, Wittenberger et al. (2001) determined that the GPR86 gene contains no introns.
By electronic PCR, Wittenberger et al. (2001) mapped the GPR86 gene to 3q24. Lee et al. (2001) noted that GPR86 lies within the same contig of chromosome 3 (GenBank AC024886) containing P2Y12 and GPR87.
Bruneau, N., Lombardo, D., Bendayan, M. Participation of GRP94-related protein in secretion of pancreatic bile salt-dependent lipase and in its internalization by the intestinal epithelium. J. Cell Sci. 111: 2665-2679, 1998. [PubMed: 9701565] [Full Text: https://doi.org/10.1242/jcs.111.17.2665]
Bruneau, N., Lombardo, D. Chaperon function of a Grp94-related protein for folding and transport of the pancreatic bile salt-dependent lipase. J. Biol. Chem. 270: 13524-13533, 1995. [PubMed: 7768954] [Full Text: https://doi.org/10.1074/jbc.270.22.13524]
Communi, D., Gonzalez, N. S., Detheux, M., Brezillon, S., Lannoy, V., Parmentier, M., Boeynaems, J.-M. Identification of a novel human ADP receptor coupled to G(i). J. Biol. Chem. 276: 41479-41485, 2001. [PubMed: 11546776] [Full Text: https://doi.org/10.1074/jbc.M105912200]
Lee, D. K., Nguyen, T., Lynch, K. R., Cheng, R., Vanti, W. B., Arkhitko, O., Lewis, T., Evans, J. F., George, S. R., O'Dowd, B. F. Discovery and mapping of ten novel G protein-coupled receptor genes. Gene 275: 83-91, 2001. [PubMed: 11574155] [Full Text: https://doi.org/10.1016/s0378-1119(01)00651-5]
Wittenberger, T., Schaller, H. C., Hellebrand, S. An expressed sequence tag (EST) data mining strategy succeeding in the discovery of new G-protein coupled receptors. J. Molec. Biol. 307: 799-813, 2001. [PubMed: 11273702] [Full Text: https://doi.org/10.1006/jmbi.2001.4520]