P2RY2_MOUSE
ID P2RY2_MOUSE Reviewed; 373 AA.
AC P35383; O09031; Q9CPZ4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=P2Y purinoceptor 2;
DE Short=P2Y2;
DE AltName: Full=ATP receptor;
DE AltName: Full=P2U purinoceptor 1;
DE Short=P2U1;
DE AltName: Full=Purinergic receptor;
GN Name=P2ry2; Synonyms=P2ru1;
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 [MRNA].
RX PubMed=7685114; DOI=10.1073/pnas.90.11.5113;
RA Lustig K.D., Shiau A.K., Brake A.J., Julius D.;
RT "Expression cloning of an ATP receptor from mouse neuroblastoma cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5113-5117(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8739319; DOI=10.1159/000109169;
RA Enomoto K., Furuya K., Moore R.C., Yamagishi S., Oka T., Maeno T.;
RT "Expression cloning and signal transduction pathway of P2U receptor in
RT mammary tumor cells.";
RL Biol. Signals 5:9-21(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Liver;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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).
RN [5]
RP MUTAGENESIS OF LYS-107; ARG-110; HIS-262; ARG-265; LYS-289 AND ARG-292.
RX PubMed=7876172; DOI=10.1074/jbc.270.9.4185;
RA Erb L., Garrad R.C., Wang Y., Quinn T., Turner J.T., Weisman G.A.;
RT "Site-directed mutagenesis of P2U purinoceptors. Positively charged amino
RT acids in transmembrane helices 6 and 7 affect agonist potency and
RT specificity.";
RL J. Biol. Chem. 270:4185-4188(1995).
CC -!- FUNCTION: Receptor for ATP and UTP coupled to G-proteins that activate
CC a phosphatidylinositol-calcium second messenger system. The affinity
CC range is UTP = ATP > ATP-gamma-S >> 2-methylthio-ATP = ADP.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Spleen, testis, kidney, liver, lung, heart and
CC brain.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L14751; AAA39871.1; -; mRNA.
DR EMBL; S83099; AAB50735.1; -; mRNA.
DR EMBL; AK005013; BAB23746.1; -; mRNA.
DR EMBL; AK017378; BAB30719.1; -; mRNA.
DR EMBL; BC006613; AAH06613.1; -; mRNA.
DR CCDS; CCDS21508.1; -.
DR PIR; A47556; A47556.
DR RefSeq; NP_001289275.1; NM_001302346.1.
DR RefSeq; NP_001289276.1; NM_001302347.1.
DR RefSeq; NP_032799.2; NM_008773.4.
DR AlphaFoldDB; P35383; -.
DR SMR; P35383; -.
DR STRING; 10090.ENSMUSP00000036765; -.
DR BindingDB; P35383; -.
DR ChEMBL; CHEMBL1075298; -.
DR GlyGen; P35383; 2 sites.
DR iPTMnet; P35383; -.
DR PhosphoSitePlus; P35383; -.
DR MaxQB; P35383; -.
DR PaxDb; P35383; -.
DR PRIDE; P35383; -.
DR ProteomicsDB; 294417; -.
DR DNASU; 18442; -.
DR GeneID; 18442; -.
DR KEGG; mmu:18442; -.
DR UCSC; uc009iny.2; mouse.
DR CTD; 5029; -.
DR MGI; MGI:105107; P2ry2.
DR eggNOG; ENOG502QSTF; Eukaryota.
DR InParanoid; P35383; -.
DR OrthoDB; 1077455at2759; -.
DR PhylomeDB; P35383; -.
DR TreeFam; TF350009; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-417957; P2Y receptors.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR BioGRID-ORCS; 18442; 1 hit in 73 CRISPR screens.
DR ChiTaRS; P2ry2; mouse.
DR PRO; PR:P35383; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35383; protein.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005769; C:early endosome; 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:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031686; F:A1 adenosine receptor binding; 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; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0070254; P:mucus secretion; IMP:MGI.
DR GO; GO:0030279; P:negative regulation of ossification; ISO:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0060406; P:positive regulation of penile erection; ISO:MGI.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
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:0019233; P:sensory perception of pain; ISO:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000356; P2Y2_rcpt.
DR PANTHER; PTHR24231:SF17; PTHR24231:SF17; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00594; P2Y2PRNOCPTR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..373
FT /note="P2Y purinoceptor 2"
FT /id="PRO_0000070015"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 318..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT MUTAGEN 107
FT /note="K->I: No effect on receptor activation."
FT /evidence="ECO:0000269|PubMed:7876172"
FT MUTAGEN 110
FT /note="R->L: No effect on receptor activation."
FT /evidence="ECO:0000269|PubMed:7876172"
FT MUTAGEN 262
FT /note="H->L: Decrease in receptor activation."
FT /evidence="ECO:0000269|PubMed:7876172"
FT MUTAGEN 265
FT /note="R->L: Decrease in receptor activation."
FT /evidence="ECO:0000269|PubMed:7876172"
FT MUTAGEN 289
FT /note="K->I: No effect on receptor activation."
FT /evidence="ECO:0000269|PubMed:7876172"
FT MUTAGEN 292
FT /note="R->L: Decrease in receptor activation."
FT /evidence="ECO:0000269|PubMed:7876172"
FT CONFLICT 17
FT /note="E -> D (in Ref. 2; AAB50735)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> R (in Ref. 2; AAB50735)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="T -> N (in Ref. 2; AAB50735)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="V -> M (in Ref. 2; AAB50735)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="V -> L (in Ref. 3; BAB23746/BAB30719)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="D -> N (in Ref. 2; AAB50735)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..371
FT /note="KDI -> PYV (in Ref. 2; AAB50735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42175 MW; 590BBE502E41B3AE CRC64;
MAADLEPWNS TINGTWEGDE LGYKCRFNED FKYVLLPVSY GVVCVLGLCL NVVALYIFLC
RLKTWNASTT YMFHLAVSDS LYAASLPLLV YYYARGDHWP FSTVLCKLVR FLFYTNLYCS
ILFLTCISVH RCLGVLRPLH SLRWGRARYA RRVAAVVWVL VLACQAPVLY FVTTSVRGTR
ITCHDTSARE LFSHFVAYSS VMLGLLFAVP FSVILVCYVL MARRLLKPAY GTTGGLPRAK
RKSVRTIALV LAVFALCFLP FHVTRTLYYS FRSLDLSCHT LNAINMAYKI TRPLASANSC
LDPVLYFLAG QRLVRFARDA KPPTEPTPSP QARRKLGLHR PNRTVRKDLS VSSDDSRRTE
STPAGSETKD IRL
