ID   P2RY2_HUMAN             Reviewed;         377 AA.
AC   P41231; B2R9W3; Q96EM8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 4.
DT   27-MAR-2024, entry version 205.
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=P2U receptor 1;
DE   AltName: Full=Purinergic receptor;
GN   Name=P2RY2; Synonyms=P2RU1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-46.
RC   TISSUE=Airway epithelium;
RX   PubMed=8159738; DOI=10.1073/pnas.91.8.3275;
RA   Parr C.E., Sullivan D.M., Paradiso A.M., Lazarowski E.R., Burch L.H.,
RA   Olsen J.C., Erb L., Weisman G.A., Boucher R.C., Turner J.T.;
RT   "Cloning and expression of a human P2U nucleotide receptor, a target for
RT   cystic fibrosis pharmacotherapy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3275-3279(1994).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=7809171; DOI=10.1073/pnas.91.26.13067;
RA   Parr C.E., Sullivan D.M., Paradiso A.M., Lazarowski E.R., Burch L.H.,
RA   Olsen J.C., Erb L., Weisman G.A., Boucher R.C., Turner J.T.;
RT   "Cloning and expression of a human P2U nucleotide receptor, a target for
RT   cystic fibrosis pharmacotherapy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:13067-13067(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-46.
RC   TISSUE=Placenta;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-46 AND CYS-334.
RC   TISSUE=Pericardium;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LEU-46 AND
RP   CYS-334.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-46 AND SER-312.
RC   TISSUE=Kidney, and Leukocyte;
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 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   -!- INTERACTION:
CC       P41231; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-8677294, EBI-2837444;
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; U07225; AAC04923.1; -; mRNA.
DR   EMBL; AY136753; AAN01279.1; -; mRNA.
DR   EMBL; AK313942; BAG36660.1; -; mRNA.
DR   EMBL; AP002761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74882.1; -; Genomic_DNA.
DR   EMBL; BC012104; AAH12104.1; -; mRNA.
DR   EMBL; BC028135; AAH28135.1; -; mRNA.
DR   CCDS; CCDS8219.1; -.
DR   PIR; A54946; A54946.
DR   RefSeq; NP_002555.3; NM_002564.3.
DR   RefSeq; NP_788085.2; NM_176071.2.
DR   RefSeq; NP_788086.2; NM_176072.2.
DR   RefSeq; XP_005274076.1; XM_005274019.4.
DR   RefSeq; XP_005274077.1; XM_005274020.4.
DR   RefSeq; XP_005274078.1; XM_005274021.4.
DR   RefSeq; XP_011543376.1; XM_011545074.2.
DR   RefSeq; XP_016873328.1; XM_017017839.1.
DR   AlphaFoldDB; P41231; -.
DR   SMR; P41231; -.
DR   BioGRID; 111068; 117.
DR   CORUM; P41231; -.
DR   IntAct; P41231; 2.
DR   MINT; P41231; -.
DR   STRING; 9606.ENSP00000310305; -.
DR   BindingDB; P41231; -.
DR   ChEMBL; CHEMBL4398; -.
DR   DrugBank; DB04983; Denufosol.
DR   DrugBank; DB05390; INS 316.
DR   DrugBank; DB01069; Promethazine.
DR   DrugBank; DB04786; Suramin.
DR   DrugCentral; P41231; -.
DR   GuidetoPHARMACOLOGY; 324; -.
DR   TCDB; 9.A.14.13.16; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; P41231; 2 sites, No reported glycans.
DR   GlyGen; P41231; 2 sites.
DR   iPTMnet; P41231; -.
DR   PhosphoSitePlus; P41231; -.
DR   SwissPalm; P41231; -.
DR   BioMuta; P2RY2; -.
DR   DMDM; 311033490; -.
DR   EPD; P41231; -.
DR   jPOST; P41231; -.
DR   MassIVE; P41231; -.
DR   MaxQB; P41231; -.
DR   PaxDb; 9606-ENSP00000310305; -.
DR   PeptideAtlas; P41231; -.
DR   ProteomicsDB; 55440; -.
DR   Antibodypedia; 17116; 326 antibodies from 30 providers.
DR   DNASU; 5029; -.
DR   Ensembl; ENST00000311131.6; ENSP00000310305.2; ENSG00000175591.12.
DR   Ensembl; ENST00000393596.2; ENSP00000377221.2; ENSG00000175591.12.
DR   Ensembl; ENST00000393597.7; ENSP00000377222.2; ENSG00000175591.12.
DR   GeneID; 5029; -.
DR   KEGG; hsa:5029; -.
DR   MANE-Select; ENST00000393597.7; ENSP00000377222.2; NM_002564.4; NP_002555.4.
DR   UCSC; uc001otj.5; human.
DR   AGR; HGNC:8541; -.
DR   CTD; 5029; -.
DR   DisGeNET; 5029; -.
DR   GeneCards; P2RY2; -.
DR   HGNC; HGNC:8541; P2RY2.
DR   HPA; ENSG00000175591; Tissue enhanced (esophagus, skeletal muscle, tongue).
DR   MIM; 600041; gene.
DR   neXtProt; NX_P41231; -.
DR   OpenTargets; ENSG00000175591; -.
DR   PharmGKB; PA32870; -.
DR   VEuPathDB; HostDB:ENSG00000175591; -.
DR   eggNOG; ENOG502QSTF; Eukaryota.
DR   GeneTree; ENSGT01030000234621; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; P41231; -.
DR   OMA; RFLGICF; -.
DR   OrthoDB; 4017151at2759; -.
DR   PhylomeDB; P41231; -.
DR   TreeFam; TF350009; -.
DR   PathwayCommons; P41231; -.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-417957; P2Y receptors.
DR   Reactome; R-HSA-5683826; Surfactant metabolism.
DR   SignaLink; P41231; -.
DR   SIGNOR; P41231; -.
DR   BioGRID-ORCS; 5029; 17 hits in 1156 CRISPR screens.
DR   ChiTaRS; P2RY2; human.
DR   GeneWiki; P2RY2; -.
DR   GenomeRNAi; 5029; -.
DR   Pharos; P41231; Tclin.
DR   PRO; PR:P41231; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P41231; Protein.
DR   Bgee; ENSG00000175591; Expressed in hindlimb stylopod muscle and 121 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031686; F:A1 adenosine receptor binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; IEA:InterPro.
DR   GO; GO:0071318; P:cellular response to ATP; TAS:ARUK-UCL.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006873; P:intracellular monoatomic ion homeostasis; TAS:ProtInc.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0070257; P:positive regulation of mucus secretion; IEA:InterPro.
DR   CDD; cd15373; 7tmA_P2Y2; 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; IPR000356; P2Y2_rcpt.
DR   PANTHER; PTHR24231:SF17; P2Y PURINOCEPTOR 2; 1.
DR   PANTHER; PTHR24231; PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00594; P2Y2PRNOCPTR.
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; P41231; HS.
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..377
FT                   /note="P2Y purinoceptor 2"
FT                   /id="PRO_0000070013"
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..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          318..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..358
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   VARIANT         46
FT                   /note="P -> L (in dbSNP:rs2511241)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8159738,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.6"
FT                   /id="VAR_054870"
FT   VARIANT         312
FT                   /note="R -> S (in dbSNP:rs3741156)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_054871"
FT   VARIANT         334
FT                   /note="R -> C (in dbSNP:rs1626154)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.6"
FT                   /id="VAR_054872"
FT   CONFLICT        350
FT                   /note="E -> G (in Ref. 1; AAC04923)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="S -> F (in Ref. 1; AAC04923)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   377 AA;  42273 MW;  F71DAF4A8DCB4062 CRC64;
     MAADLGPWND TINGTWDGDE LGYRCRFNED FKYVLLPVSY GVVCVPGLCL NAVALYIFLC
     RLKTWNASTT YMFHLAVSDA LYAASLPLLV YYYARGDHWP FSTVLCKLVR FLFYTNLYCS
     ILFLTCISVH RCLGVLRPLR SLRWGRARYA RRVAGAVWVL VLACQAPVLY FVTTSARGGR
     VTCHDTSAPE LFSRFVAYSS VMLGLLFAVP FAVILVCYVL MARRLLKPAY GTSGGLPRAK
     RKSVRTIAVV LAVFALCFLP FHVTRTLYYS FRSLDLSCHT LNAINMAYKV TRPLASANSC
     LDPVLYFLAG QRLVRFARDA KPPTGPSPAT PARRRLGLRR SDRTDMQRIE DVLGSSEDSR
     RTESTPAGSE NTKDIRL
//