ID P2RY4_MOUSE Reviewed; 361 AA. AC Q9JJS7; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=P2Y purinoceptor 4; DE Short=P2Y4; GN Name=P2ry4; Synonyms=P2y4r; 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/SvJ; RX PubMed=11290369; DOI=10.1016/s0014-2999(01)00875-5; RA Suarez-Huerta N., Pouillon V., Boeynaems J.-M., Robaye B.; RT "Molecular cloning and characterization of the mouse P2Y4 nucleotide RT receptor."; RL Eur. J. Pharmacol. 416:197-202(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Receptor for ATP and UTP coupled to G-proteins that activate CC a phosphatidylinositol-calcium second messenger system. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in the liver, intestine, stomach, bladder CC and lung. CC -!- PTM: Phosphorylation of Ser-329 and Ser-330 is a key step in agonist- CC dependent desensitization and loss of surface P2RY4. This CC phosphorylation does not involve PKC, nor other calcium-activated CC kinases (By similarity). {ECO:0000250}. 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; AJ277752; CAB91043.1; -; Genomic_DNA. DR EMBL; AK076364; BAC36314.1; -; mRNA. DR CCDS; CCDS30303.1; -. DR RefSeq; NP_065646.1; NM_020621.4. DR RefSeq; XP_006528238.1; XM_006528175.2. DR RefSeq; XP_006528239.1; XM_006528176.3. DR RefSeq; XP_006528240.1; XM_006528177.2. DR RefSeq; XP_006528241.1; XM_006528178.2. DR AlphaFoldDB; Q9JJS7; -. DR SMR; Q9JJS7; -. DR STRING; 10090.ENSMUSP00000055869; -. DR GlyCosmos; Q9JJS7; 1 site, No reported glycans. DR GlyGen; Q9JJS7; 1 site. DR PhosphoSitePlus; Q9JJS7; -. DR PaxDb; 10090-ENSMUSP00000055869; -. DR ProteomicsDB; 294418; -. DR Antibodypedia; 13260; 312 antibodies from 28 providers. DR DNASU; 57385; -. DR Ensembl; ENSMUST00000053373.2; ENSMUSP00000055869.2; ENSMUSG00000044359.2. DR GeneID; 57385; -. DR KEGG; mmu:57385; -. DR UCSC; uc009twc.1; mouse. DR AGR; MGI:1926594; -. DR CTD; 5030; -. DR MGI; MGI:1926594; P2ry4. DR VEuPathDB; HostDB:ENSMUSG00000044359; -. DR eggNOG; ENOG502QSTF; Eukaryota. DR GeneTree; ENSGT01030000234621; -. DR HOGENOM; CLU_009579_8_2_1; -. DR InParanoid; Q9JJS7; -. DR OMA; TRTIYYM; -. DR OrthoDB; 4017151at2759; -. DR PhylomeDB; Q9JJS7; -. DR TreeFam; TF350009; -. DR Reactome; R-MMU-417957; P2Y receptors. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR BioGRID-ORCS; 57385; 2 hits in 77 CRISPR screens. DR PRO; PR:Q9JJS7; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; Q9JJS7; Protein. DR Bgee; ENSMUSG00000044359; Expressed in esophagus and 22 other cell types or tissues. DR ExpressionAtlas; Q9JJS7; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IEA:InterPro. DR GO; GO:0045030; F:G protein-coupled UTP receptor activity; IDA:MGI. DR GO; GO:0019103; F:pyrimidine nucleotide binding; IC:MGI. DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI. DR GO; GO:0030321; P:transepithelial chloride transport; IDA:MGI. DR CDD; cd15374; 7tmA_P2Y4; 1. 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; IPR000018; P2Y4. DR PANTHER; PTHR24231:SF21; P2Y PURINOCEPTOR 4; 1. DR PANTHER; PTHR24231; PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01066; P2Y4PRNOCPTR. DR PRINTS; PR01157; P2YPURNOCPTR. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; Q9JJS7; MM. PE 2: Evidence at transcript level; KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..361 FT /note="P2Y purinoceptor 4" FT /id="PRO_0000070022" FT TOPO_DOM 1..30 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 31..58 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 59..68 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 69..91 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 92..108 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 109..127 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 128..149 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 150..170 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 171..192 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 193..218 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 219..242 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 243..265 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 266..283 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 284..305 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 306..361 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 175 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 104..181 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 361 AA; 41034 MW; 3E8EA84B65BC0A20 CRC64; MTSADSLLFT SLGPSPSSGD GDCKFNEEFK FILLPLSYAV VFVLGLALNA PTLWLFLFRL RPWDATATYM FHLALSDTLY VLSLPTLVYY YAARNHWPFG TGFCKFVRFL FYWNLYCSVL FLTCISVHRY MGICHPLRAI RWGRPRFAGL LCLGVWLVVA GCLVPNLFFV TTNANGTTIL CHDTTLPEEF DHYVYFSSTI MVLLFGFPFL ITLVCYGLMA RRLYRPLPGA GQSSSRLRSL RTIAVVLTVF AVCFVPFHIT RTIYYLARLL NAECRVLNIV NVVYKVTRPL ASANSCLDPV LYLFTGDKYR NQLQQLCRGS TPKRRTTASS LALVTLHEES ISRWADIHQD SIFPAYEGDR L //