P2RY2_RAT
ID P2RY2_RAT Reviewed; 374 AA.
AC P41232;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 142.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7811468; DOI=10.1165/ajrcmb.12.1.7811468;
RA Rice W.R., Burton F.M., Fiedeldey D.T.;
RT "Cloning and expression of the alveolar type II cell P2u-purinergic
RT receptor.";
RL Am. J. Respir. Cell Mol. Biol. 12:27-32(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pituitary;
RA Chen Z.P., Krull N., Xu S., Levy A., Lightman S.L.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=9437211; DOI=10.1161/01.atv.17.12.3602;
RA Seye C.I., Gadeau A.P., Daret D., Dupuch F., Alzieu P., Capron L.,
RA Desgranges C.;
RT "Overexpression of P2Y2 purinoceptor in intimal lesions of the rat aorta.";
RL Arterioscler. Thromb. Vasc. Biol. 17:3602-3610(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U09402; AAA61565.1; -; mRNA.
DR EMBL; L46865; AAB02099.1; -; mRNA.
DR EMBL; U56839; AAC00048.1; -; mRNA.
DR EMBL; BC061754; AAH61754.1; -; mRNA.
DR RefSeq; NP_058951.1; NM_017255.1.
DR AlphaFoldDB; P41232; -.
DR SMR; P41232; -.
DR STRING; 10116.ENSRNOP00000026115; -.
DR BindingDB; P41232; -.
DR ChEMBL; CHEMBL4419; -.
DR GlyGen; P41232; 2 sites.
DR iPTMnet; P41232; -.
DR PhosphoSitePlus; P41232; -.
DR PaxDb; P41232; -.
DR GeneID; 29597; -.
DR KEGG; rno:29597; -.
DR UCSC; RGD:62088; rat.
DR CTD; 5029; -.
DR RGD; 62088; P2ry2.
DR eggNOG; ENOG502QSTF; Eukaryota.
DR InParanoid; P41232; -.
DR PhylomeDB; P41232; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-417957; P2Y receptors.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR PRO; PR:P41232; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031686; F:A1 adenosine receptor binding; IPI:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; TAS:RGD.
DR GO; GO:0045030; F:G protein-coupled UTP receptor activity; IDA:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IDA:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071415; P:cellular response to purine-containing compound; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEP:RGD.
DR GO; GO:0030279; P:negative regulation of ossification; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0070257; P:positive regulation of mucus secretion; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:0060406; P:positive regulation of penile erection; IDA:RGD.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IDA:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0070848; P:response to growth factor; IEP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IDA:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..374
FT /note="P2Y purinoceptor 2"
FT /id="PRO_0000070016"
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..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 318..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..374
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 CONFLICT 132
FT /note="C -> S (in Ref. 1; AAA61565)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="S -> R (in Ref. 1; AAA61565)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> T (in Ref. 1; AAA61565)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> D (in Ref. 1; AAA61565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 42137 MW; 2DA6853AA20A1AF3 CRC64;
MAAGLDSWNS TINGTWEGDE LGYKCRFNED FKYVLLPVSY GVVCVLGLCL NVVALYIFLC
RLKTWNASTT YMFHLAVSDS LYAASLPLLV YYYAQGDHWP FSTVLCKLVR FLFYTNLYCS
ILFLTCISVH RCLGVLRPLH SLSWGHARYA RRVAAVVWVL VLACQAPVLY FVTTSVRGTR
ITCHDTSARE LFSHFVAYSS VMLGLLFAVP FSIILVCYVL MARRLLKPAY GTTGLPRAKR
KSVRTIALVL AVFALCFLPF HVTRTLYYSF RSLDLSCHTL NAINMAYKIT RPLASANSCL
DPVLYFLAGQ RLVRFARDAK PATEPTPSPQ ARRKLGLHRP NRTDTVRKDL SISSDDSRRT
ESTPAGSETK DIRL
