PI2R_BOVIN
ID PI2R_BOVIN Reviewed; 385 AA.
AC P79393;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 121.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hasse A., Schroer K.;
RT "Cloning and sequencing of the bovine prostacyclin receptor gene.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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; Z93039; CAB07510.1; -; Genomic_DNA.
DR EMBL; Z93040; CAB07510.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P79393; -.
DR SMR; P79393; -.
DR STRING; 9913.ENSBTAP00000019413; -.
DR PaxDb; P79393; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P79393; -.
DR Proteomes; UP000009136; Unplaced.
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:0016501; F:prostacyclin receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
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; PTHR11866; 1.
DR PANTHER; PTHR11866:SF7; PTHR11866:SF7; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01788; PROSTANOIDR.
DR PRINTS; PR00856; PRSTNOIDIPR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Methylation; Prenylation; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..382
FT /note="Prostacyclin receptor"
FT /id="PRO_0000070074"
FT PROPEP 383..385
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000240003"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..76
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..94
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..158
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 315..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 382
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 382
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 5..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 92..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 385 AA; 41247 MW; 0CDA5A4D18E035C7 CRC64;
MADSCRNLTY VRDSVGPATS TLMFVAGVVG NGLALGILGA RRHSRPSAFA VLVTGLGVTD
LLGTCFLSPA VFAAYARNSS LLGLARGRPA LCDAFAFAMT FFGLASTLIL FAMAVERCLA
LSHPYLYAQL DGPRRARLAL PAIYAFCTIF CSLPFLGLGQ HQQYCPGSWC FIRMRSAEPG
GCAFLLAYAS LVALLVAAIV LCNGSVTLSL CRMYRQQRRH QARCPRPRAG EDEVDHLILL
ALMTGIMAVC SLPLTPQIRG FTQAIAPDSS EMGDLLAFRF NAFNPILDPW VFILFRKSVF
QRLKLWFCCL YSRPAQGDSR TSLSQSASGR KDSSAPPALE GKKGNWVPLS AWGEGQGGPL
PAVQLPTSTV GTPSKAGSEA ACSLC
