ID P2RY6_MOUSE Reviewed; 328 AA. AC Q9ERK9; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 161. DE RecName: Full=P2Y purinoceptor 6; DE Short=P2Y6; GN Name=P2ry6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=129/SvEv; RX PubMed=11259526; RA Lazarowski E.R., Rochelle L.G., O'Neal W.K., Ribeiro C.M.P., Grubb B.R., RA Zhang V., Harden T.K., Boucher R.C.; RT "Cloning and functional characterization of two murine uridine nucleotide RT receptors reveal a potential target for correcting ion transport deficiency RT in cystic fibrosis gallbladder."; RL J. Pharmacol. Exp. Ther. 297:43-49(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Receptor for extracellular UTP > ADP = 2-methylthio-ATP > CC ADP-beta-S > ATP = ATP-gamma-S. The activity of this receptor is CC mediated by G proteins which activate a phosphatidylinositol-calcium CC second messenger system. Functionally coupled to phospholipase C (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF298899; AAG24619.1; -; Genomic_DNA. DR EMBL; BC027331; AAH27331.1; -; mRNA. DR EMBL; BC064095; AAH64095.1; -; mRNA. DR CCDS; CCDS21507.1; -. DR RefSeq; NP_898991.1; NM_183168.2. DR RefSeq; XP_006507703.1; XM_006507640.3. DR RefSeq; XP_011240041.1; XM_011241739.2. DR AlphaFoldDB; Q9ERK9; -. DR SMR; Q9ERK9; -. DR BioGRID; 231427; 1. DR STRING; 10090.ENSMUSP00000055697; -. DR GlyCosmos; Q9ERK9; 2 sites, No reported glycans. DR GlyGen; Q9ERK9; 2 sites. DR PhosphoSitePlus; Q9ERK9; -. DR MaxQB; Q9ERK9; -. DR PaxDb; 10090-ENSMUSP00000055697; -. DR ProteomicsDB; 294357; -. DR Antibodypedia; 17126; 310 antibodies from 35 providers. DR DNASU; 233571; -. DR Ensembl; ENSMUST00000060174.6; ENSMUSP00000055697.5; ENSMUSG00000048779.6. DR GeneID; 233571; -. DR KEGG; mmu:233571; -. DR UCSC; uc009inw.2; mouse. DR AGR; MGI:2673874; -. DR CTD; 5031; -. DR MGI; MGI:2673874; P2ry6. DR VEuPathDB; HostDB:ENSMUSG00000048779; -. DR eggNOG; ENOG502QRYJ; Eukaryota. DR GeneTree; ENSGT01030000234621; -. DR HOGENOM; CLU_009579_8_2_1; -. DR InParanoid; Q9ERK9; -. DR OMA; CYCRMAQ; -. DR OrthoDB; 4628437at2759; -. DR PhylomeDB; Q9ERK9; -. DR TreeFam; TF330775; -. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR Reactome; R-MMU-417957; P2Y receptors. DR BioGRID-ORCS; 233571; 2 hits in 79 CRISPR screens. DR PRO; PR:Q9ERK9; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q9ERK9; Protein. DR Bgee; ENSMUSG00000048779; Expressed in stroma of bone marrow and 128 other cell types or tissues. DR ExpressionAtlas; Q9ERK9; baseline and differential. DR Genevisible; Q9ERK9; MM. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; ISO:MGI. DR GO; GO:0045029; F:G protein-coupled UDP receptor activity; IDA:MGI. DR GO; GO:0045030; F:G protein-coupled UTP receptor activity; ISO:MGI. DR GO; GO:0019103; F:pyrimidine nucleotide binding; IC:MGI. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI. DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI. DR GO; GO:0071415; P:cellular response to purine-containing compound; ISO:MGI. DR GO; GO:1905835; P:cellular response to pyrimidine ribonucleotide; ISO:MGI. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006909; P:phagocytosis; ISO:MGI. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI. DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISO:MGI. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0030321; P:transepithelial chloride transport; IDA:MGI. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR001973; P2Y6_rcpt. DR PANTHER; PTHR24231:SF16; P2Y PURINOCEPTOR 6; 1. DR PANTHER; PTHR24231; PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01068; P2Y6PRNOCPTR. DR PRINTS; PR01157; P2YPURNOCPTR. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 2: Evidence at transcript level; KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..328 FT /note="P2Y purinoceptor 6" FT /id="PRO_0000070029" FT TOPO_DOM 1..27 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 28..48 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 49..62 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 63..83 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 84..101 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 102..122 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 123..144 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 145..165 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 166..194 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 195..215 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 216..236 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 237..257 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 258..280 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 281..303 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 304..328 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 5 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 173 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 99..177 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 328 AA; 36721 MW; 00F9DF5ADADF903E CRC64; MEQDNGTIQA PGLPPTTCVY REDFKRLLLT PVYSVVLVVG LPLNICVIAQ ICASRRTLTR SAVYTLNLAL ADLMYACSLP LLIYNYARGD HWPFGDLACR FVRFLFYANL HGSILFLTCI SFQRYLGICH PLASWHKRGG RRAAWVVCGV VWLAVTAQCL PTAVFAATGI QRNRTVCYDL SPPILSTRYL PYGMALTVIG FLLPFIALLA CYCRMARRLC RQDGPAGPVA QERRSKAARM AVVVAAVFAI SFLPFHITKT AYLAVRSTPG VSCPVLETFA AAYKGTRPFA SVNSVLDPIL FYFTQQKFRR QPHDLLQRLT AKWQRQRV //