PI2R_MOUSE
ID PI2R_MOUSE Reviewed; 415 AA.
AC P43252; Q52KE5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7511597; DOI=10.1016/s0021-9258(17)36979-x;
RA Namba T., Oida H., Sugimoto Y., Negishi M., Kakizuka A., Ichikawa A.,
RA Narumiya S.;
RT "cDNA cloning of a mouse prostacyclin receptor. Multiple signaling pathways
RT and expression in thymic medulla.";
RL J. Biol. Chem. 269:9986-9992(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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).
RN [3]
RP ISOPRENYLATION AT CYS-412, AND MUTAGENESIS OF CYS-412.
RX PubMed=10446129; DOI=10.1074/jbc.274.34.23707;
RA Hayes J.S., Lawler O.A., Walsh M.T., Kinsella B.T.;
RT "The prostacyclin receptor is isoprenylated. Isoprenylation is required for
RT efficient receptor-effector coupling.";
RL J. Biol. Chem. 274:23707-23718(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 409-415 IN COMPLEX WITH PDZK1, AND
RP INTERACTION WITH PDZK1.
RX PubMed=23457445; DOI=10.1371/journal.pone.0053819;
RA Birrane G., Mulvaney E.P., Pal R., Kinsella B.T., Kocher O.;
RT "Molecular analysis of the prostacyclin receptor's interaction with the
RT PDZ1 domain of its adaptor protein PDZK1.";
RL PLoS ONE 8:E53819-E53819(2013).
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:0000269|PubMed:23457445}.
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:0000269|PubMed:10446129}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05144.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; D26157; BAA05144.1; ALT_INIT; mRNA.
DR EMBL; BC094386; AAH94386.1; -; mRNA.
DR CCDS; CCDS20857.2; -.
DR PIR; A54416; A54416.
DR RefSeq; NP_032993.2; NM_008967.3.
DR PDB; 4F8K; X-ray; 1.70 A; A/B=409-415.
DR PDBsum; 4F8K; -.
DR AlphaFoldDB; P43252; -.
DR SMR; P43252; -.
DR BioGRID; 202460; 4.
DR STRING; 10090.ENSMUSP00000122080; -.
DR BindingDB; P43252; -.
DR DrugCentral; P43252; -.
DR GuidetoPHARMACOLOGY; 345; -.
DR GlyGen; P43252; 1 site.
DR iPTMnet; P43252; -.
DR PhosphoSitePlus; P43252; -.
DR MaxQB; P43252; -.
DR PaxDb; P43252; -.
DR PRIDE; P43252; -.
DR ProteomicsDB; 289559; -.
DR Antibodypedia; 18117; 256 antibodies from 29 providers.
DR DNASU; 19222; -.
DR Ensembl; ENSMUST00000144408; ENSMUSP00000122080; ENSMUSG00000043017.
DR GeneID; 19222; -.
DR KEGG; mmu:19222; -.
DR UCSC; uc009fim.2; mouse.
DR CTD; 5739; -.
DR MGI; MGI:99535; Ptgir.
DR VEuPathDB; HostDB:ENSMUSG00000043017; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244902; -.
DR HOGENOM; CLU_045991_0_1_1; -.
DR InParanoid; P43252; -.
DR OMA; IHPFCGD; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; P43252; -.
DR TreeFam; TF324982; -.
DR Reactome; R-MMU-391908; Prostanoid ligand receptors.
DR Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 19222; 4 hits in 75 CRISPR screens.
DR PRO; PR:P43252; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P43252; protein.
DR Bgee; ENSMUSG00000043017; Expressed in lumbar dorsal root ganglion and 101 other tissues.
DR ExpressionAtlas; P43252; baseline and differential.
DR Genevisible; P43252; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; IMP:BHF-UCL.
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; IMP:BHF-UCL.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
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; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Methylation; Phosphoprotein;
KW Prenylation; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..412
FT /note="Prostacyclin receptor"
FT /id="PRO_0000070076"
FT PROPEP 413..415
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000240005"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..288
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43253"
FT MOD_RES 412
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 412
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:10446129"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 120..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT MUTAGEN 412
FT /note="C->S: Abolishes isoprenylation."
FT /evidence="ECO:0000269|PubMed:10446129"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:4F8K"
SQ SEQUENCE 415 AA; 44463 MW; 306929582DDDD24C CRC64;
MMASDGHPGP PSVTPGSPLS AGGREWQGMA GSCWNITYVQ DSVGPATSTL MFVAGVVGNG
LALGILGARR RSHPSAFAVL VTGLAVTDLL GTCFLSPAVF VAYARNSSLL GLAHGGTMLC
DTFAFAMTFF GLASTLILFA MAVERCLALS HPYLYAQLDG PRCARFALPS IYAFCCLFCS
LPLLGLGEHQ QYCPGSWCFI RMRSAQPGGC AFSLAYASLM ALLVTSIFFC NGSVTLSLYH
MYRQQRRHHG SFVPTSRARE DEVYHLILLA LMTVIMAVCS LPLMIRGFTQ AIAPDSREMG
DLLAFRFNAF NPILDPWVFI LFRKAVFQRL KFWLCCLCAR SVHGDLQAPL SRPASGRRDP
PAPTSLQAKE GSWVPLSSWG TGQVAPLTAV PLTGGDGCSV GMPSKSEAIA ACSLC
