PF2R_RAT
ID PF2R_RAT Reviewed; 366 AA.
AC P43118; Q62787;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Prostaglandin F2-alpha receptor;
DE Short=PGF receptor;
DE Short=PGF2-alpha receptor;
DE AltName: Full=Prostanoid FP receptor;
GN Name=Ptgfr;
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 STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RX PubMed=7972878; DOI=10.1016/0090-6980(94)90094-9;
RA Kitanaka J., Hashimoto H., Sugimoto Y., Negishi M., Aino H., Gotoh M.,
RA Ichikawa A., Baba A.;
RT "Cloning and expression of a cDNA for rat prostaglandin F2 alpha
RT receptor.";
RL Prostaglandins 48:31-41(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7988697; DOI=10.1016/0014-5793(94)01198-2;
RA Lake S., Gullberg H., Wahlqvist J., Sjoegren A.-M., Kinhult A., Lind P.,
RA Hellstroem-Lindahl E., Stjernschantz J.;
RT "Cloning of the rat and human prostaglandin F2 alpha receptors and the
RT expression of the rat prostaglandin F2 alpha receptor.";
RL FEBS Lett. 355:317-325(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RA de Vries C., Neuschaefer-Rube F., Haenecke K., Jungermann K.,
RA Pueschel G.P.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=8912810; DOI=10.1016/0303-7207(96)03894-4;
RA Olofsson J.I., Leung C.H.B., Bjurulf E., Ohno T., Selstam G., Peng C.,
RA Leung P.C.K.;
RT "Characterization and regulation of a mRNA encoding the prostaglandin
RT F2alpha receptor in the rat ovary.";
RL Mol. Cell. Endocrinol. 123:45-52(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=8804121; DOI=10.1016/s0952-3278(96)90055-1;
RA Orlicky D.J.;
RT "Negative regulatory activity of a prostaglandin F2 alpha receptor
RT associated protein (FPRP).";
RL Prostaglandins Leukot. Essent. Fatty Acids 54:247-259(1996).
CC -!- FUNCTION: Receptor for prostaglandin F2-alpha (PGF2-alpha). The
CC activity of this receptor is mediated by G proteins which activate a
CC phosphatidylinositol-calcium second messenger system. Initiates
CC luteolysis in the corpus luteum.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highest expression in pregnant ovary. Also found in
CC a low extent in the kidney. In the brain, expressed in astrocytes and
CC oligodendrocytes, and meningeal fibroblasts, but not in migroglia
CC cells.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D28581; BAA05917.1; -; mRNA.
DR EMBL; S74898; AAB32739.1; -; mRNA.
DR EMBL; X83856; CAA58736.1; -; mRNA.
DR EMBL; U47287; AAB47872.1; -; mRNA.
DR EMBL; U26663; AAB19233.1; -; mRNA.
DR PIR; S51281; S51281.
DR RefSeq; NP_037247.1; NM_013115.1.
DR RefSeq; XP_006233548.1; XM_006233486.3.
DR RefSeq; XP_006233549.1; XM_006233487.3.
DR AlphaFoldDB; P43118; -.
DR SMR; P43118; -.
DR STRING; 10116.ENSRNOP00000065253; -.
DR BindingDB; P43118; -.
DR ChEMBL; CHEMBL4680028; -.
DR GuidetoPHARMACOLOGY; 344; -.
DR GlyGen; P43118; 2 sites.
DR PhosphoSitePlus; P43118; -.
DR PaxDb; P43118; -.
DR Ensembl; ENSRNOT00000071195; ENSRNOP00000065253; ENSRNOG00000046468.
DR GeneID; 25652; -.
DR KEGG; rno:25652; -.
DR CTD; 5737; -.
DR RGD; 3436; Ptgfr.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234559; -.
DR HOGENOM; CLU_045991_3_0_1; -.
DR InParanoid; P43118; -.
DR OMA; HIEMICQ; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; P43118; -.
DR Reactome; R-RNO-391908; Prostanoid ligand receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P43118; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000046468; Expressed in heart and 14 other tissues.
DR Genevisible; P43118; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0004958; F:prostaglandin F receptor activity; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:RGD.
DR GO; GO:0071799; P:cellular response to prostaglandin D stimulus; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0051239; P:regulation of multicellular organismal process; IEA:UniProt.
DR GO; GO:0032355; P:response to estradiol; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000141; PglndnF_rcpt.
DR InterPro; IPR008365; Prostanoid_rcpt.
DR PANTHER; PTHR11866; PTHR11866; 1.
DR PANTHER; PTHR11866:SF4; PTHR11866:SF4; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01788; PROSTANOIDR.
DR PRINTS; PR00855; PRSTNOIDFPR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..366
FT /note="Prostaglandin F2-alpha receptor"
FT /id="PRO_0000070072"
FT TOPO_DOM 1..31
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 10
FT /note="A -> V (in Ref. 5; AAB19233)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="I -> M (in Ref. 5; AAB19233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 40655 MW; D44C47F18B326FBA CRC64;
MSINSSKQPA SSAAGLIANT TCQTENRLSV FFSIIFMTVG IVSNSLAIAI LMKAYQRFRR
KSKASFLLLA SGLVITDFFG HLINGGIAVF VYASDKDWIR FDQSNILCSV FGISMVFSGL
CPLFLGSTMA IERCIGVTNP LFHSTKITSK HVKMILSGVC MFAVFVALLP ILGHRDYQIQ
ASRTWCFYNT EHIEDWEDRF YLLFFSSLGL LALGISFSCN AVTGVTLLRV KFRSQQHRQG
RSHHLEMVIQ LLAIMCVSCV CWSPFLVTMA NIAINGNNSP VTCETTLFAL RMATWNQILD
PWVYILLRKA VLRNLYKLAS RCCGVNIISL HIWELSSIKN SLKVAAISES PAAEKENQQA
SSEAGL
