ID PI2R_RAT Reviewed; 416 AA. AC P43253; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 171. DE RecName: Full=Prostacyclin receptor; DE AltName: Full=Prostaglandin I2 receptor; DE Short=PGI receptor; DE Short=PGI2 receptor; DE AltName: Full=Prostanoid IP receptor; DE Flags: Precursor; GN Name=Ptgir; 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]. RC TISSUE=Lung; RX PubMed=7803522; DOI=10.1016/0167-4889(94)90300-x; RA Sasaki Y., Usui T., Tanaka I., Nakagawa O., Sando T., Takahashi T., RA Namba T., Narumiya S., Nakao K.; RT "Cloning and expression of a cDNA for rat prostacyclin receptor."; RL Biochim. Biophys. Acta 1224:601-605(1994). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Receptor for prostacyclin (prostaglandin I2 or PGI2). The CC activity of this receptor is mediated by G(s) proteins which activate CC adenylate cyclase. CC -!- SUBUNIT: Interacts (non-isoprenylated C-terminus) with PDZK1. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- PTM: Isoprenylation does not influence ligand binding but is required CC for efficient coupling to the effectors adenylyl cyclase and CC phospholipase C. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D28966; BAA06091.1; -; mRNA. DR PIR; S52078; S52078. DR RefSeq; NP_001071112.1; NM_001077644.1. DR AlphaFoldDB; P43253; -. DR SMR; P43253; -. DR FunCoup; P43253; 76. DR STRING; 10116.ENSRNOP00000022461; -. DR BindingDB; P43253; -. DR ChEMBL; CHEMBL3322; -. DR DrugCentral; P43253; -. DR GuidetoPHARMACOLOGY; 345; -. DR GlyCosmos; P43253; 1 site, No reported glycans. DR GlyGen; P43253; 1 site. DR iPTMnet; P43253; -. DR PhosphoSitePlus; P43253; -. DR PaxDb; 10116-ENSRNOP00000022461; -. DR Ensembl; ENSRNOT00000022461.5; ENSRNOP00000022461.2; ENSRNOG00000016756.7. DR GeneID; 292661; -. DR KEGG; rno:292661; -. DR UCSC; RGD:1310890; rat. DR AGR; RGD:1310890; -. DR CTD; 5739; -. DR RGD; 1310890; Ptgir. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01050000244902; -. DR HOGENOM; CLU_045991_0_1_1; -. DR InParanoid; P43253; -. DR OMA; IHPFCGD; -. DR OrthoDB; 71863at9989; -. DR PhylomeDB; P43253; -. DR Reactome; R-RNO-391908; Prostanoid ligand receptors. DR Reactome; R-RNO-392851; Prostacyclin signalling through prostacyclin receptor. DR PRO; PR:P43253; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000016756; Expressed in lung and 16 other cell types or tissues. DR ExpressionAtlas; P43253; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0016501; F:prostacyclin receptor activity; IBA:GO_Central. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; ISO:RGD. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:RGD. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central. DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD. DR GO; GO:0042311; P:vasodilation; IDA:RGD. DR FunFam; 1.20.1070.10:FF:000198; Prostaglandin I2 receptor; 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; IPR008365; Prostanoid_rcpt. DR InterPro; IPR000370; Prostglndn_IP_rcpt. DR PANTHER; PTHR11866; G-PROTEIN COUPLED RECEPTOR FAMILY 1 MEMBER; 1. DR PANTHER; PTHR11866:SF7; PROSTACYCLIN RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01788; PROSTANOIDR. DR PRINTS; PR00856; PRSTNOIDIPR. 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. PE 1: Evidence at protein level; KW Cell membrane; Disulfide bond; G protein-coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Methylation; Phosphoprotein; Prenylation; Receptor; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..413 FT /note="Prostacyclin receptor" FT /id="PRO_0000070077" FT PROPEP 414..416 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000240006" FT TOPO_DOM 1..45 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 46..67 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 68..80 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 81..105 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 106..123 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 124..144 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 145..163 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 164..187 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 188..215 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 216..237 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 238..264 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 265..289 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 290..302 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 303..323 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 324..416 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOD_RES 366 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 413 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250" FT LIPID 413 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 36 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 34..194 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT DISULFID 121..199 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 416 AA; 44662 MW; 03171B5ED21C4171 CRC64; MVASGGRPDG PPSITPESPL IVGGREWQGM AGSCWNITYV QDSVGPATST LMFVAGVVGN GLALGILGAR RRSHPSAFAV LVTGLAVTDL LGTCFLSPAV FVAYARNSSL LGLAHGGTML CDTFAFAMTF FGLASTLILF AMAVERCLAL SHPYLYAQLD GPRCARLALP AIYAFCCLFC SLPLLGLGEH QQYCPGSWCF IRMRSPQPGG CAFSLAYASL MALLVTSIFF CNGSVTLSLC HMYRQQRRHH GSFVPTSRAR EDEVYHLILL ALMTGIMAVC SLPLTIRGFT QAIAPDSREM GDLHAFRFNA FNPILDPWVF ILFRKAVFQR LKFWLCCLCA RSVHGDLQTP LSRPVSGRRD TLAPDSLQAK EGNWVPLSTW GTGQVAPLTA VPLSGGDGCS VGMPSKTEAV VACSLC //