P2RY4_MOUSE
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 03-AUG-2022, entry version 150.
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}.
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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 GlyGen; Q9JJS7; 1 site.
DR PhosphoSitePlus; Q9JJS7; -.
DR PaxDb; Q9JJS7; -.
DR PRIDE; Q9JJS7; -.
DR ProteomicsDB; 294418; -.
DR Antibodypedia; 13260; 281 antibodies from 28 providers.
DR DNASU; 57385; -.
DR Ensembl; ENSMUST00000053373; ENSMUSP00000055869; ENSMUSG00000044359.
DR GeneID; 57385; -.
DR KEGG; mmu:57385; -.
DR UCSC; uc009twc.1; mouse.
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; HWPFGTG; -.
DR OrthoDB; 1077455at2759; -.
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 72 CRISPR screens.
DR PRO; PR:Q9JJS7; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JJS7; protein.
DR Bgee; ENSMUSG00000044359; Expressed in esophagus and 22 other tissues.
DR ExpressionAtlas; Q9JJS7; baseline and differential.
DR Genevisible; Q9JJS7; MM.
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:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0038023; F:signaling receptor activity; IBA:GO_Central.
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 InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000018; P2Y4.
DR PANTHER; PTHR24231:SF21; PTHR24231:SF21; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01066; P2Y4PRNOCPTR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 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; 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
