P2RY2_PIG
ID P2RY2_PIG Reviewed; 373 AA.
AC Q5YA25;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=P2Y purinoceptor 2;
DE Short=P2Y2;
GN Name=P2RY2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Coronary artery;
RX PubMed=15280443; DOI=10.1124/mol.104.002642;
RA Shen J., Seye C.I., Wang M., Weisman G.A., Wilden P.A., Sturek M.;
RT "Cloning, up-regulation, and mitogenic role of porcine P2Y2 receptor in
RT coronary artery smooth muscle cells.";
RL Mol. Pharmacol. 66:1265-1274(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. {ECO:0000269|PubMed:15280443}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, kidney, intestine, skeletal
CC muscle and adrenal gland. {ECO:0000269|PubMed:15280443}.
CC -!- INDUCTION: Up-regulated in stented coronary arteries (at protein
CC level). {ECO:0000269|PubMed:15280443}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY620400; AAU89436.1; -; mRNA.
DR RefSeq; NP_001006591.1; NM_001006591.1.
DR AlphaFoldDB; Q5YA25; -.
DR SMR; Q5YA25; -.
DR PRIDE; Q5YA25; -.
DR Ensembl; ENSSSCT00000052508; ENSSSCP00000042423; ENSSSCG00000040207.
DR Ensembl; ENSSSCT00005005082; ENSSSCP00005002915; ENSSSCG00005003464.
DR Ensembl; ENSSSCT00015110254; ENSSSCP00015047067; ENSSSCG00015080925.
DR Ensembl; ENSSSCT00030032359; ENSSSCP00030014566; ENSSSCG00030023292.
DR Ensembl; ENSSSCT00040053045; ENSSSCP00040022064; ENSSSCG00040039637.
DR Ensembl; ENSSSCT00060108930; ENSSSCP00060048668; ENSSSCG00060078754.
DR Ensembl; ENSSSCT00070038605; ENSSSCP00070032314; ENSSSCG00070019519.
DR GeneID; 450248; -.
DR KEGG; ssc:450248; -.
DR CTD; 5029; -.
DR VGNC; VGNC:98173; P2RY2.
DR GeneTree; ENSGT01030000234621; -.
DR InParanoid; Q5YA25; -.
DR OMA; YSFRSWD; -.
DR OrthoDB; 1077455at2759; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Chromosome 9.
DR Bgee; ENSSSCG00000040207; Expressed in longissimus lumborum muscle and 33 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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; IEA:InterPro.
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; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..373
FT /note="P2Y purinoceptor 2"
FT /id="PRO_0000369548"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 320..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 106..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 373 AA; 41651 MW; C80ECEBFB37AB670 CRC64;
MATGPDLWNG TVNGTSDGDD WGYRCRFHED FKYVLLPLSY GVVCVLGLSL NAGALYIFLC
RLKTWNASTT YMFHLAVSDA LYAASLPLLV YYYARGDHWP FSTALCKLVR FLFYTNLYCS
ILFLTCISVH RCLGVLRPLR SLRWGHARYA RRVAAAVWGL VLACQAPALY FITTTAQGGR
ITCHDTSAPE LFSHFVAYSL VMLSVLFAAP FAVILVCYAL MARRLLRPAY GTAGGLPRAK
RKSVRTIAVV LAVFALCFLP FHVTRTLYYS FRTLDLSCHT LDAINMAYKI TRPLASANSC
LDPVLYFLAG QRLVRFARDA KPPTDATPTA QACRRLGLRR SHGTDTKRTE DSASSEDSRR
TEITPARGED IRL
