GPER1_RAT
ID GPER1_RAT Reviewed; 375 AA.
AC O08878;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=G-protein coupled estrogen receptor 1;
DE AltName: Full=Chemoattractant receptor-like 2;
DE AltName: Full=G protein-coupled estrogen receptor 1;
DE AltName: Full=G-protein coupled receptor 30 {ECO:0000303|PubMed:23300088};
DE AltName: Full=G-protein coupled receptor 41;
DE AltName: Full=Membrane estrogen receptor;
DE Short=mER;
GN Name=Gper1;
GN Synonyms=Cmkrl2, Gper, Gpr30 {ECO:0000303|PubMed:23300088}, Gpr41;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=9168987; DOI=10.1006/bbrc.1997.6591;
RA Bonini J.A., Anderson S.M., Steiner D.F.;
RT "Molecular cloning and tissue expression of a novel orphan G protein-
RT coupled receptor from rat lung.";
RL Biochem. Biophys. Res. Commun. 234:190-193(1997).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=16780796; DOI=10.1016/j.bbrc.2006.05.191;
RA Funakoshi T., Yanai A., Shinoda K., Kawano M.M., Mizukami Y.;
RT "G protein-coupled receptor 30 is an estrogen receptor in the plasma
RT membrane.";
RL Biochem. Biophys. Res. Commun. 346:904-910(2006).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17872373; DOI=10.1210/en.2007-0436;
RA Sakamoto H., Matsuda K., Hosokawa K., Nishi M., Morris J.F.,
RA Prossnitz E.R., Kawata M.;
RT "Expression of G protein-coupled receptor-30, a G protein-coupled membrane
RT estrogen receptor, in oxytocin neurons of the rat paraventricular and
RT supraoptic nuclei.";
RL Endocrinology 148:5842-5850(2007).
RN [4]
RP FUNCTION.
RX PubMed=19179659; DOI=10.1161/circresaha.108.190892;
RA Haas E., Bhattacharya I., Brailoiu E., Damjanovic M., Brailoiu G.C.,
RA Gao X., Mueller-Guerre L., Marjon N.A., Gut A., Minotti R., Meyer M.R.,
RA Amann K., Ammann E., Perez-Dominguez A., Genoni M., Clegg D.J., Dun N.J.,
RA Resta T.C., Prossnitz E.R., Barton M.;
RT "Regulatory role of G protein-coupled estrogen receptor for vascular
RT function and obesity.";
RL Circ. Res. 104:288-291(2009).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=19420011; DOI=10.1677/joe-09-0066;
RA Hazell G.G., Yao S.T., Roper J.A., Prossnitz E.R., O'Carroll A.M.,
RA Lolait S.J.;
RT "Localisation of GPR30, a novel G protein-coupled oestrogen receptor,
RT suggests multiple functions in rodent brain and peripheral tissues.";
RL J. Endocrinol. 202:223-236(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20132863; DOI=10.1016/j.mce.2010.01.035;
RA Chimento A., Sirianni R., Delalande C., Silandre D., Bois C., Ando S.,
RA Maggiolini M., Carreau S., Pezzi V.;
RT "17 beta-estradiol activates rapid signaling pathways involved in rat
RT pachytene spermatocytes apoptosis through GPR30 and ER alpha.";
RL Mol. Cell. Endocrinol. 320:136-144(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=21242460; DOI=10.1161/hypertensionaha.110.161653;
RA Gros R., Ding Q., Sklar L.A., Prossnitz E.E., Arterburn J.B.,
RA Chorazyczewski J., Feldman R.D.;
RT "GPR30 expression is required for the mineralocorticoid receptor-
RT independent rapid vascular effects of aldosterone.";
RL Hypertension 57:442-451(2011).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21354433; DOI=10.1016/j.steroids.2011.02.018;
RA Cheng S.B., Graeber C.T., Quinn J.A., Filardo E.J.;
RT "Retrograde transport of the transmembrane estrogen receptor, G-protein-
RT coupled-receptor-30 (GPR30/GPER) from the plasma membrane towards the
RT nucleus.";
RL Steroids 76:892-896(2011).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22919059; DOI=10.1210/en.2012-1458;
RA Almey A., Filardo E.J., Milner T.A., Brake W.G.;
RT "Estrogen receptors are found in glia and at extranuclear neuronal sites in
RT the dorsal striatum of female rats: evidence for cholinergic but not
RT dopaminergic colocalization.";
RL Endocrinology 153:5373-5383(2012).
RN [10]
RP ESTROGEN-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=22306576; DOI=10.1016/j.steroids.2012.01.015;
RA Ropero A.B., Pang Y., Alonso-Magdalena P., Thomas P., Nadal A.;
RT "Role of ERbeta and GPR30 in the endocrine pancreas: A matter of estrogen
RT dose.";
RL Steroids 77:951-958(2012).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=23283935; DOI=10.1152/ajpcell.00203.2012;
RA Gros R., Ding Q., Liu B., Chorazyczewski J., Feldman R.D.;
RT "Aldosterone mediates its rapid effects in vascular endothelial cells
RT through GPER activation.";
RL Am. J. Physiol. 304:C532-C540(2013).
RN [12]
RP INTERACTION WITH DLG4, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23300088; DOI=10.1074/jbc.m112.412478;
RA Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.;
RT "Post-synaptic density-95 (PSD-95) binding capacity of G-protein-coupled
RT receptor 30 (GPR30), an estrogen receptor that can be identified in
RT hippocampal dendritic spines.";
RL J. Biol. Chem. 288:6438-6450(2013).
RN [13]
RP REVIEW, AND SUBCELLULAR LOCATION.
RX PubMed=23822769; DOI=10.1111/jne.12071;
RA Srivastava D.P., Evans P.D.;
RT "GPER 1: trials and tribulations of a membrane oestrogen receptor.";
RL J. Neuroendocrinol. 25:1219-1230(2013).
CC -!- FUNCTION: G-protein coupled estrogen receptor that binds to 17-beta-
CC estradiol (E2) with high affinity, leading to rapid and transient
CC activation of numerous intracellular signaling pathways. Stimulates
CC cAMP production, calcium mobilization and tyrosine kinase Src inducing
CC the release of heparin-bound epidermal growth factor (HB-EGF) and
CC subsequent transactivation of the epidermal growth factor receptor
CC (EGFR), activating downstream signaling pathways such as PI3K/Akt and
CC ERK/MAPK. Mediates pleiotropic functions among others in the
CC cardiovascular, endocrine, reproductive, immune and central nervous
CC systems. Has a role in cardioprotection by reducing cardiac hypertrophy
CC and perivascular fibrosis in a RAMP3-dependent manner. Regulates
CC arterial blood pressure by stimulating vasodilation and reducing
CC vascular smooth muscle and microvascular endothelial cell
CC proliferation. Plays a role in blood glucose homeostasis contributing
CC to the insulin secretion response by pancreatic beta cells. Triggers
CC mitochondrial apoptosis during pachytene spermatocyte differentiation.
CC Stimulates uterine epithelial cell proliferation. Enhances uterine
CC contractility in response to oxytocin. Contributes to thymic atrophy by
CC inducing apoptosis. Attenuates TNF-mediated endothelial expression of
CC leukocyte adhesion molecules. Promotes neuritogenesis in developing
CC hippocampal neurons. Plays a role in acute neuroprotection against
CC NMDA-induced excitotoxic neuronal death. Increases firing activity and
CC intracellular calcium oscillations in luteinizing hormone-releasing
CC hormone (LHRH) neurons. Inhibits early osteoblast proliferation at
CC growth plate during skeletal development. Inhibits mature adipocyte
CC differentiation and lipid accumulation. Involved in the recruitment of
CC beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells.
CC Functions also as a receptor for aldosterone mediating rapid regulation
CC of vascular contractibility through the PI3K/ERK signaling pathway.
CC Involved in cancer progression regulation. Stimulates cancer-associated
CC fibroblast (CAF) proliferation by a rapid genomic response through the
CC EGFR/ERK transduction pathway. Associated with EGFR, may act as a
CC transcription factor activating growth regulatory genes (c-fos, cyclin
CC D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix
CC assembly in breast cancer cells. {ECO:0000269|PubMed:19179659,
CC ECO:0000269|PubMed:20132863}.
CC -!- SUBUNIT: Homodimer (Probable). Heterodimer; heterodimerizes with other
CC G-protein-coupled receptor (GPCRs) like CRHR1, HTR1A and PAQR8.
CC Interacts with RAMP3. Interacts with KRT7 and KRT8. Interacts with
CC EGFR; the interaction increases after agonist-induced stimulation in
CC cancer-associated fibroblasts (CAF). Interacts with EGFR and ESR1 (By
CC similarity). Interacts (via C-terminus tail motif) with DLG4 (via N-
CC terminus tandem pair of PDZ domains); the interaction is direct and
CC induces the increase of GPER1 protein levels residing at the plasma
CC membrane surface in a estradiol-independent manner. {ECO:0000250,
CC ECO:0000269|PubMed:23300088, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22919059}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22919059}. Cytoplasmic
CC vesicle membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Basolateral
CC cell membrane; Multi-pass membrane protein. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:21242460}; Multi-pass membrane protein
CC {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome
CC {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:21242460,
CC ECO:0000269|PubMed:22919059}; Multi-pass membrane protein. Cell
CC projection, dendrite. Cell projection, dendritic spine membrane
CC {ECO:0000269|PubMed:22919059, ECO:0000269|PubMed:23300088}; Multi-pass
CC membrane protein. Cell projection, axon {ECO:0000269|PubMed:22919059}.
CC Postsynaptic density {ECO:0000269|PubMed:22919059,
CC ECO:0000269|PubMed:23300088}. Mitochondrion membrane
CC {ECO:0000269|PubMed:22919059}; Multi-pass membrane protein.
CC Note=Endocytosed in an agonist- and arrestin-independent manner.
CC Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane.
CC Colocalized with transferrin receptor at the plasma membrane and
CC perinuclear region. Accumulated and colocalized with RAB11 proteins in
CC recycling endosomes and trans-Golgi network (TGN), but does neither
CC recycle back to the cell surface nor traffics to late endosome or
CC lysosome. Colocalized with calnexin in the endoplasmic reticulum.
CC Traffics to intracellular sites via cytokeratin intermediate filaments
CC like KRT7 and KRT8 after constitutive endocytosis in epithelial cells.
CC Colocalized with EGFR in the nucleus of agonist-induced cancer-
CC associated fibroblasts (CAF) (By similarity). Colocalized with BSN to
CC the active zone of presynaptic density. Colocalized with DLG4/PSD95 and
CC neurabin-2 PPP1R9B in neuronal synaptosomes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain. Expressed in neurons of the
CC hippocampus, hypothalamic paraventricular nucleus (PVN), supraoptic
CC nucleus (SON) and the median eminence. Expressed in magnocellular
CC neurosecretory cells (MNCs) which secrete oxytocin but not in MNCs
CC which secrete vasopressin. Expressed in glial cells. Expressed in the
CC nucleus ambiguous. Expressed in epithelial cells, in pachytene
CC spermatocytes (PS) (at protein level). Expressed strongly in vascular
CC endothelial cells and poorly in vascular smooth muscle cells (VSMC).
CC Expressed in the brain, lung, pituitary gland, adrenal medulla, renal
CC pelvis and ovary. Expressed in CA1 hippocampus. Expressed weakly in
CC heart, skeletal muscle and kidney. {ECO:0000269|PubMed:17872373,
CC ECO:0000269|PubMed:19420011, ECO:0000269|PubMed:20132863,
CC ECO:0000269|PubMed:21242460, ECO:0000269|PubMed:21354433,
CC ECO:0000269|PubMed:22919059, ECO:0000269|PubMed:23283935,
CC ECO:0000269|PubMed:23300088, ECO:0000269|PubMed:9168987}.
CC -!- PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and
CC leads to proteasome-mediated degradation. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U92802; AAC53208.1; -; mRNA.
DR PIR; JC5509; JC5509.
DR RefSeq; NP_598257.1; NM_133573.1.
DR AlphaFoldDB; O08878; -.
DR SMR; O08878; -.
DR STRING; 10116.ENSRNOP00000001732; -.
DR BindingDB; O08878; -.
DR ChEMBL; CHEMBL3309103; -.
DR GlyGen; O08878; 2 sites.
DR PhosphoSitePlus; O08878; -.
DR PaxDb; O08878; -.
DR GeneID; 171104; -.
DR KEGG; rno:171104; -.
DR UCSC; RGD:619845; rat.
DR CTD; 2852; -.
DR RGD; 619845; Gper1.
DR eggNOG; ENOG502QU56; Eukaryota.
DR InParanoid; O08878; -.
DR OrthoDB; 736624at2759; -.
DR PhylomeDB; O08878; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:O08878; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0044327; C:dendritic spine head; IDA:UniProtKB.
DR GO; GO:0032591; C:dendritic spine membrane; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045095; C:keratin filament; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:1903924; F:estradiol binding; IMP:RGD.
DR GO; GO:0038054; F:G protein-coupled estrogen receptor activity; IDA:UniProtKB.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; ISO:RGD.
DR GO; GO:0005496; F:steroid binding; ISO:RGD.
DR GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030263; P:apoptotic chromosome condensation; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0071389; P:cellular response to mineralocorticoid stimulus; IDA:UniProtKB.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:RGD.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0010948; P:negative regulation of cell cycle process; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0002695; P:negative regulation of leukocyte activation; ISS:UniProtKB.
DR GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:1900121; P:negative regulation of receptor binding; IMP:RGD.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0019228; P:neuronal action potential; ISS:UniProtKB.
DR GO; GO:0030264; P:nuclear fragmentation involved in apoptotic nuclear change; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2000724; P:positive regulation of cardiac vascular smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:1905152; P:positive regulation of voltage-gated sodium channel activity; IMP:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:RGD.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISO:RGD.
DR GO; GO:0042311; P:vasodilation; IDA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Acetylation; Apoptosis; Cell cycle; Cell membrane; Cell projection;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Differentiation;
KW Disulfide bond; Endoplasmic reticulum; Endosome;
KW G-protein coupled receptor; Glycoprotein; Golgi apparatus; Immunity;
KW Inflammatory response; Innate immunity; Membrane; Mitochondrion;
KW Neurogenesis; Nucleus; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..375
FT /note="G-protein coupled estrogen receptor 1"
FT /id="PRO_0000069312"
FT TOPO_DOM 1..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..120
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..132
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..194
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..236
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99527"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 375 AA; 42260 MW; 08B60576B0DBE314 CRC64;
MAATTPAQDV GVEIYLGPVW PAPSNSTPLA LNLSLALRED APGNLTGDLS EHQQYVIALF
LSCLYTIFLF PIGFVGNILI LVVNISFREK MTIPDLYFIN LAAADLILVA DSLIEVFNLD
EQYYDIAVLC TFMSLFLQIN MYSSVFFLTW MSFDRYLALA KAMRCGLFRT KHHARLSCGL
IWMASVSATL VPFTAVHLRH TEEACFCFAD VREVQWLEVT LGFIVPFAII GLCYSLIVRA
LIRAHRHRGL RPRRQKALRM IFAVVLVFFI CWLPENVFIS VHLLQWAQPG DTPCKQSFRH
AYPLTGHIVN LAAFSNSCLS PLIYSFLGET FRDKLRLYVA QKTSLPALNR FCHATLKAVI
PDSTEQSDVK FSSAV
