P2RY2_HUMAN
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 03-AUG-2022, entry version 196.
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 GlyGen; P41231; 2 sites.
DR iPTMnet; P41231; -.
DR PhosphoSitePlus; P41231; -.
DR BioMuta; P2RY2; -.
DR DMDM; 311033490; -.
DR EPD; P41231; -.
DR jPOST; P41231; -.
DR MassIVE; P41231; -.
DR MaxQB; P41231; -.
DR PaxDb; P41231; -.
DR PeptideAtlas; P41231; -.
DR PRIDE; P41231; -.
DR ProteomicsDB; 55440; -.
DR Antibodypedia; 17116; 298 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 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; YSFRSWD; -.
DR OrthoDB; 1077455at2759; -.
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; 16 hits in 1074 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 tissues.
DR Genevisible; P41231; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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; IBA:GO_Central.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:InterPro.
DR GO; GO:0006873; P:cellular ion homeostasis; TAS:ProtInc.
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: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 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..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
