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   24-JAN-2024, entry version 172.
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};
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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   GlyCosmos; P43252; 1 site, No reported glycans.
DR   GlyGen; P43252; 1 site.
DR   iPTMnet; P43252; -.
DR   PhosphoSitePlus; P43252; -.
DR   MaxQB; P43252; -.
DR   PaxDb; 10090-ENSMUSP00000122080; -.
DR   ProteomicsDB; 289559; -.
DR   Antibodypedia; 18117; 285 antibodies from 29 providers.
DR   DNASU; 19222; -.
DR   Ensembl; ENSMUST00000144408.2; ENSMUSP00000122080.2; ENSMUSG00000043017.10.
DR   GeneID; 19222; -.
DR   KEGG; mmu:19222; -.
DR   UCSC; uc009fim.2; mouse.
DR   AGR; MGI:99535; -.
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; FAVFVCN; -.
DR   OrthoDB; 5355693at2759; -.
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; 5 hits in 80 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 102 other cell types or tissues.
DR   ExpressionAtlas; P43252; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
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   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.
DR   Genevisible; P43252; MM.
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
//