PF2R_MOUSE
ID PF2R_MOUSE Reviewed; 366 AA.
AC P43117;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
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 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].
RC STRAIN=ddY; TISSUE=Ovary;
RX PubMed=8288601; DOI=10.1016/s0021-9258(17)42265-4;
RA Sugimoto Y., Hasumoto K.Y., Namba T., Irie A., Katsuyama M., Negishi M.,
RA Kakizuka A., Narumiya S., Ichikawa A.;
RT "Cloning and expression of a cDNA for mouse prostaglandin F receptor.";
RL J. Biol. Chem. 269:1356-1360(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D17433; BAA04251.1; -; mRNA.
DR EMBL; AK087833; BAC40021.1; -; mRNA.
DR EMBL; BC064794; AAH64794.1; -; mRNA.
DR CCDS; CCDS17913.1; -.
DR PIR; A49877; A49877.
DR RefSeq; NP_032992.1; NM_008966.3.
DR AlphaFoldDB; P43117; -.
DR SMR; P43117; -.
DR STRING; 10090.ENSMUSP00000029670; -.
DR BindingDB; P43117; -.
DR ChEMBL; CHEMBL5000; -.
DR DrugCentral; P43117; -.
DR GuidetoPHARMACOLOGY; 344; -.
DR GlyGen; P43117; 2 sites.
DR PhosphoSitePlus; P43117; -.
DR PaxDb; P43117; -.
DR PRIDE; P43117; -.
DR ProteomicsDB; 287685; -.
DR Antibodypedia; 19743; 190 antibodies from 27 providers.
DR DNASU; 19220; -.
DR Ensembl; ENSMUST00000029670; ENSMUSP00000029670; ENSMUSG00000028036.
DR Ensembl; ENSMUST00000106126; ENSMUSP00000101732; ENSMUSG00000028036.
DR GeneID; 19220; -.
DR KEGG; mmu:19220; -.
DR UCSC; uc008rsm.1; mouse.
DR CTD; 5737; -.
DR MGI; MGI:97796; Ptgfr.
DR VEuPathDB; HostDB:ENSMUSG00000028036; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234559; -.
DR HOGENOM; CLU_045991_3_0_1; -.
DR InParanoid; P43117; -.
DR OMA; HIEMICQ; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; P43117; -.
DR TreeFam; TF324982; -.
DR Reactome; R-MMU-391908; Prostanoid ligand receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 19220; 2 hits in 72 CRISPR screens.
DR PRO; PR:P43117; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P43117; protein.
DR Bgee; ENSMUSG00000028036; Expressed in lumbar dorsal root ganglion and 90 other tissues.
DR ExpressionAtlas; P43117; baseline and differential.
DR Genevisible; P43117; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004958; F:prostaglandin F receptor activity; ISO:MGI.
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:MGI.
DR GO; GO:0071799; P:cellular response to prostaglandin D stimulus; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
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; IDA:CACAO.
DR GO; GO:0032355; P:response to estradiol; IDA:CACAO.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000141; PglndnF_rcpt.
DR InterPro; IPR008365; Prostanoid_rcpt.
DR InterPro; IPR001244; Prostglndn_DP_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; PR00428; PROSTAGLNDNR.
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_0000070071"
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"
SQ SEQUENCE 366 AA; 40700 MW; B01CB3B271007582 CRC64;
MSMNSSKQPV SPAAGLIANT TCQTENRLSV FFSIIFMTVG ILSNSLAIAI LMKAYQRFRQ
KSKASFLLLA SGLVITDFFG HLINGGIAVF VYASDKDWIR FDQSNILCSI FGISMVFSGL
CPLFLGSAMA IERCIGVTNP IFHSTKITSK HVKMILSGVC MFAVFVAVLP ILGHRDYQIQ
ASRTWCFYNT EHIEDWEDRF YLLFFSFLGL LALGVSFSCN AVTGVTLLRV KFRSQQHRQG
RSHHLEMIIQ LLAIMCVSCV CWSPFLVTMA NIAINGNNSP VTCETTLFAL RMATWNQILD
PWVYILLRKA VLRNLYKLAS RCCGVNIISL HIWELSSIKN SLKVAAISES PAAEKESQQA
SSEAGL
