ID PF2R_SHEEP Reviewed; 362 AA. AC Q28905; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-AUG-2022, entry version 121. 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 Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Western range; TISSUE=Corpus luteum; RX PubMed=7628379; DOI=10.1210/endo.136.8.7628379; RA Graves P.E., Pierce K.L., Bailey T.J., Rueda B.R., Gil D.W., Woodward D.F., RA Yool A.J., Hoyer P.B., Regan J.W.; RT "Cloning of a receptor for prostaglandin F2 alpha from the ovine corpus RT luteum."; RL Endocrinology 136:3430-3436(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RC TISSUE=Corpus luteum; RX PubMed=8995377; DOI=10.1074/jbc.272.2.883; RA Pierce K.L., Bailey T.J., Hoyer P.B., Gil D.W., Woodward D.F., Regan J.W.; RT "Cloning of a carboxyl-terminal isoform of the prostanoid FP receptor."; RL J. Biol. Chem. 272:883-887(1997). 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Isoform FP-A and isoform FP-B have identical ligand binding CC properties but different G protein coupling properties.; CC Name=FP-A; CC IsoId=Q28905-1; Sequence=Displayed; CC Name=FP-B; CC IsoId=Q28905-2; Sequence=VSP_001951; CC -!- DEVELOPMENTAL STAGE: Expression is high in the midluteal phase corpus CC luteum and decreases during luteolysis. CC -!- MISCELLANEOUS: [Isoform FP-B]: Shows agonist-independent constitutive CC activity, but is still responsive to agonist. {ECO:0000305}. 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; U73798; AAB51070.1; -; mRNA. DR RefSeq; NP_001009789.1; NM_001009789.2. DR RefSeq; XP_012017550.1; XM_012162160.2. [Q28905-1] DR RefSeq; XP_012018243.1; XM_012162853.2. [Q28905-1] DR AlphaFoldDB; Q28905; -. DR SMR; Q28905; -. DR STRING; 9940.ENSOARP00000014365; -. DR BindingDB; Q28905; -. DR ChEMBL; CHEMBL1909491; -. DR Ensembl; ENSOART00000014575; ENSOARP00000014365; ENSOARG00000013402. [Q28905-1] DR GeneID; 443366; -. DR KEGG; oas:443366; -. DR CTD; 5737; -. DR eggNOG; KOG3656; Eukaryota. DR HOGENOM; CLU_045991_3_0_1; -. DR OMA; HIEMICQ; -. DR OrthoDB; 972015at2759; -. DR Proteomes; UP000002356; Chromosome 1. DR Bgee; ENSOARG00000013402; Expressed in thyroid gland and 38 other tissues. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. 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; IEA:UniProtKB-SubCell. DR GO; GO:0004958; F:prostaglandin F receptor activity; IEA:Ensembl. DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl. DR GO; GO:0071799; P:cellular response to prostaglandin D stimulus; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. 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; 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 Alternative splicing; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..362 FT /note="Prostaglandin F2-alpha receptor" FT /id="PRO_0000070073" FT TOPO_DOM 1..31 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 32..54 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 55..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..362 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 VAR_SEQ 317..362 FT /note="VCTRRCCGVHVISLHVWELSSIKNSLKVAAISDLPVTEKVTQQTST -> I FT (in isoform FP-B)" FT /evidence="ECO:0000305" FT /id="VSP_001951" FT CONFLICT 6 FT /note="S -> C (in Ref. 2; AAB51070)" FT /evidence="ECO:0000305" SQ SEQUENCE 362 AA; 40985 MW; 83604FC18EADF583 CRC64; MSTNNSVQPV SPASELLSNT TCQLEEDLSI SFSIIFMTVG ILSNSLAIAI LMKAYQRFRQ KYKSSFLLLA SALVITDFFG HLINGTIAVF VYASDKDWIY FDKSNILCSI FGICMVFSGL CPLFLGSLMA IERCIGVTKP IFHSTKITTK HVKMMLSGVC FFAVFVALLP ILGHRDYKIQ ASRTWCFYKT DQIKDWEDRF YLLLFAFLGL LALGISFVCN AITGISLLKV KFRSQQHRQG RSHHFEMVIQ LLGIMCVSCI CWSPFLVTMA SIGMNIQDFK DSCERTLFTL RMATWNQILD PWVYILLRKA VLRNLYVCTR RCCGVHVISL HVWELSSIKN SLKVAAISDL PVTEKVTQQT ST //