GPER1_MOUSE
ID GPER1_MOUSE Reviewed; 375 AA.
AC Q8BMP4; B2RRW0; Q9D392;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
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;
DE AltName: Full=Membrane estrogen receptor;
DE Short=mER;
GN Name=Gper1; Synonyms=Cmkrl2, Gper, Gpr30;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Pituitary;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18063692; DOI=10.1210/me.2007-0359;
RA Wang C., Dehghani B., Magrisso I.J., Rick E.A., Bonhomme E., Cody D.B.,
RA Elenich L.A., Subramanian S., Murphy S.J., Kelly M.J., Rosenbaum J.S.,
RA Vandenbark A.A., Offner H.;
RT "GPR30 contributes to estrogen-induced thymic atrophy.";
RL Mol. Endocrinol. 22:636-648(2008).
RN [4]
RP ABSENCE OF ESTROGEN-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=18799753; DOI=10.1095/biolreprod.108.071175;
RA Otto C., Fuchs I., Kauselmann G., Kern H., Zevnik B., Andreasen P.,
RA Schwarz G., Altmann H., Klewer M., Schoor M., Vonk R., Fritzemeier K.H.;
RT "GPR30 does not mediate estrogenic responses in reproductive organs in
RT mice.";
RL Biol. Reprod. 80:34-41(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18845638; DOI=10.1210/en.2008-0623;
RA Martensson U.E., Salehi S.A., Windahl S., Gomez M.F., Sward K.,
RA Daszkiewicz-Nilsson J., Wendt A., Andersson N., Hellstrand P., Grande P.O.,
RA Owman C., Rosen C.J., Adamo M.L., Lundquist I., Rorsman P., Nilsson B.O.,
RA Ohlsson C., Olde B., Leeb-Lundberg L.M.;
RT "Deletion of the G protein-coupled receptor 30 impairs glucose tolerance,
RT reduces bone growth, increases blood pressure, and eliminates estradiol-
RT stimulated insulin release in female mice.";
RL Endocrinology 150:687-698(2009).
RN [7]
RP SUBCELLULAR LOCATION, AND 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 [8]
RP FUNCTION.
RX PubMed=19430488; DOI=10.1038/nchembio.168;
RA Dennis M.K., Burai R., Ramesh C., Petrie W.K., Alcon S.N., Nayak T.K.,
RA Bologa C.G., Leitao A., Brailoiu E., Deliu E., Dun N.J., Sklar L.A.,
RA Hathaway H.J., Arterburn J.B., Oprea T.I., Prossnitz E.R.;
RT "In vivo effects of a GPR30 antagonist.";
RL Nat. Chem. Biol. 5:421-427(2009).
RN [9]
RP FUNCTION.
RX PubMed=21673097; DOI=10.1210/en.2011-0091;
RA Sharma G., Prossnitz E.R.;
RT "Mechanisms of estradiol-induced insulin secretion by the G protein-coupled
RT estrogen receptor GPR30/GPER in pancreatic beta-cells.";
RL Endocrinology 152:3030-3039(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20734455; DOI=10.1002/jbmr.209;
RA Ford J., Hajibeigi A., Long M., Hahner L., Gore C., Hsieh J.T., Clegg D.,
RA Zerwekh J., Oz O.K.;
RT "GPR30 deficiency causes increased bone mass, mineralization, and growth
RT plate proliferative activity in male mice.";
RL J. Bone Miner. Res. 26:298-307(2011).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21273787; DOI=10.1159/000322578;
RA Holm A., Baldetorp B., Olde B., Leeb-Lundberg L.M., Nilsson B.O.;
RT "The GPER1 agonist G-1 attenuates endothelial cell proliferation by
RT inhibiting DNA synthesis and accumulating cells in the S and G2 phases of
RT the cell cycle.";
RL J. Vasc. Res. 48:327-335(2011).
RN [12]
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=21149639; DOI=10.1124/mol.110.069500;
RA Sanden C., Broselid S., Cornmark L., Andersson K., Daszkiewicz-Nilsson J.,
RA Martensson U.E., Olde B., Leeb-Lundberg L.M.;
RT "G protein-coupled estrogen receptor 1/G protein-coupled receptor 30
RT localizes in the plasma membrane and traffics intracellularly on
RT cytokeratin intermediate filaments.";
RL Mol. Pharmacol. 79:400-410(2011).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22492045; DOI=10.1523/jneurosci.5828-11.2012;
RA Liu S.B., Zhang N., Guo Y.Y., Zhao R., Shi T.Y., Feng S.F., Wang S.Q.,
RA Yang Q., Li X.Q., Wu Y.M., Ma L., Hou Y., Xiong L.Z., Zhang W., Zhao M.G.;
RT "G-protein-coupled receptor 30 mediates rapid neuroprotective effects of
RT estrogen via depression of NR2B-containing NMDA receptors.";
RL J. Neurosci. 32:4887-4900(2012).
RN [14]
RP TISSUE SPECIFICITY.
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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=23871778; DOI=10.1016/j.ygcen.2013.07.004;
RA Zhu P., Yuen J.M., Sham K.W., Cheng C.H.;
RT "GPER mediates the inhibitory actions of estrogen on adipogenesis in 3T3-L1
RT cells through perturbation of mitotic clonal expansion.";
RL Gen. Comp. Endocrinol. 193:19-26(2013).
RN [16]
RP SUBUNIT, AND MUTAGENESIS OF VAL-375.
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 [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23674134; DOI=10.1530/jme-13-0021;
RA Lenhart P.M., Broselid S., Barrick C.J., Leeb-Lundberg L.M., Caron K.M.;
RT "G-protein-coupled receptor 30 interacts with receptor activity-modifying
RT protein 3 and confers sex-dependent cardioprotection.";
RL J. Mol. Endocrinol. 51:191-202(2013).
RN [18]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23545157; DOI=10.1016/j.mce.2013.03.018;
RA Ruiz-Palmero I., Hernando M., Garcia-Segura L.M., Arevalo M.A.;
RT "G protein-coupled estrogen receptor is required for the neuritogenic
RT mechanism of 17beta-estradiol in developing hippocampal neurons.";
RL Mol. Cell. Endocrinol. 372:105-115(2013).
RN [19]
RP REVIEW.
RX PubMed=20034504; DOI=10.1016/j.steroids.2009.12.006;
RA Langer G., Bader B., Meoli L., Isensee J., Delbeck M., Noppinger P.R.,
RA Otto C.;
RT "A critical review of fundamental controversies in the field of GPR30
RT research.";
RL Steroids 75:603-610(2010).
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:18063692,
CC ECO:0000269|PubMed:18845638, ECO:0000269|PubMed:19179659,
CC ECO:0000269|PubMed:19430488, ECO:0000269|PubMed:20734455,
CC ECO:0000269|PubMed:21273787, ECO:0000269|PubMed:21673097,
CC ECO:0000269|PubMed:22492045, ECO:0000269|PubMed:23545157,
CC ECO:0000269|PubMed:23674134, ECO:0000269|PubMed:23871778}.
CC -!- SUBUNIT: Interacts with RAMP3. Interacts with KRT7 and KRT8. Interacts
CC with EGFR; the interaction increases after agonist-induced stimulation
CC in cancer-associated fibroblasts (CAF). Interacts with EGFR and ESR1.
CC Interacts (via C-terminus tail motif) with DLG4 (via N-terminus tandem
CC pair of PDZ domains); the interaction is direct and induces the
CC increase of GPER1 protein levels residing at the plasma membrane
CC surface in a estradiol-independent manner (By similarity). Homodimer
CC (Probable). Heterodimer; heterodimerizes with other G-protein-coupled
CC receptor (GPCRs) like CRHR1, HTR1A and PAQR8. {ECO:0000250,
CC ECO:0000269|PubMed:23300088, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Cytoplasm,
CC perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Endoplasmic
CC reticulum membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling
CC endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cell projection, axon
CC {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Note=Colocalized with BSN to the active zone of presynaptic density.
CC Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal
CC synaptosomes. Endocytosed in an agonist- and arrestin-independent
CC manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma
CC membrane. Colocalized with transferrin receptor at the plasma membrane
CC and perinuclear region. Accumulated and colocalized with RAB11 proteins
CC in 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). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, spleen, preadipocytes,
CC mature adipocytes and primary hippocampal neurons. Expressed in neurons
CC of the hippocampus, hypothalamic paraventricular nucleus (PVH),
CC supraoptic nucleus (SON) and the median eminence. Expressed in the
CC nucleus ambiguous (at protein level). Expressed in brain, pituitary
CC gland, adrenal medulla, renal pelvis, ovary, endothelial cells,
CC visceral fat tissues and islets of Langerhans.
CC {ECO:0000269|PubMed:19420011, ECO:0000269|PubMed:21273787,
CC ECO:0000269|PubMed:22306576, ECO:0000269|PubMed:23545157,
CC ECO:0000269|PubMed:23674134, ECO:0000269|PubMed:23871778}.
CC -!- INDUCTION: Up-regulated during adipogenesis.
CC {ECO:0000269|PubMed:23871778}.
CC -!- PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and
CC leads to proteasome-mediated degradation. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21149639}.
CC -!- DISRUPTION PHENOTYPE: Strong variations in phenotypes, probably
CC depending on the distinct targeting strategies, genetic background and
CC experimental conditions used in the different experiments. According to
CC PubMed:18063692, mice are viable and fertile and do not display any
CC gross physical, immunological, reproductive and neurological
CC abnormalities, but show 17-beta-estradiol (E2)-induced alleviated
CC thymic atrophy. According to PubMed:20734455, male mice display
CC increased body size, femur length, bone mass and cell proliferative
CC activity within the growth plate. According to PubMed:18845638, female
CC mice, but not male, show reduced body weight and skeletal growth,
CC hyperglycemia, impaired glucose tolerance with reduced glucose-
CC stimulated insulin release and increased blood pressure. According to
CC PubMed:19179659 mice show increased body weight, visceral adiposity,
CC vascular tone and blood pressure. No visible phenotype according to
CC PubMed:18799753. {ECO:0000269|PubMed:18063692,
CC ECO:0000269|PubMed:18799753, ECO:0000269|PubMed:18845638,
CC ECO:0000269|PubMed:19179659, ECO:0000269|PubMed:20734455}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AK018203; BAB31118.1; -; mRNA.
DR EMBL; AK030375; BAC26930.1; -; mRNA.
DR EMBL; CH466529; EDL19153.1; -; Genomic_DNA.
DR EMBL; BC138598; AAI38599.1; -; mRNA.
DR EMBL; BC138616; AAI38617.1; -; mRNA.
DR CCDS; CCDS19811.1; -.
DR RefSeq; NP_084047.2; NM_029771.3.
DR RefSeq; XP_006504820.1; XM_006504757.3.
DR AlphaFoldDB; Q8BMP4; -.
DR SMR; Q8BMP4; -.
DR STRING; 10090.ENSMUSP00000080370; -.
DR GlyGen; Q8BMP4; 2 sites.
DR PhosphoSitePlus; Q8BMP4; -.
DR PaxDb; Q8BMP4; -.
DR PRIDE; Q8BMP4; -.
DR Antibodypedia; 10887; 426 antibodies from 34 providers.
DR DNASU; 76854; -.
DR Ensembl; ENSMUST00000066211; ENSMUSP00000080370; ENSMUSG00000053647.
DR GeneID; 76854; -.
DR KEGG; mmu:76854; -.
DR UCSC; uc009agr.2; mouse.
DR CTD; 2852; -.
DR MGI; MGI:1924104; Gper1.
DR VEuPathDB; HostDB:ENSMUSG00000053647; -.
DR eggNOG; ENOG502QU56; Eukaryota.
DR GeneTree; ENSGT00940000154307; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; Q8BMP4; -.
DR OMA; FRTKQHA; -.
DR OrthoDB; 736624at2759; -.
DR PhylomeDB; Q8BMP4; -.
DR TreeFam; TF333506; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-9634597; GPER1 signaling.
DR BioGRID-ORCS; 76854; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8BMP4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BMP4; protein.
DR Bgee; ENSMUSG00000053647; Expressed in external carotid artery and 180 other tissues.
DR Genevisible; Q8BMP4; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR GO; GO:0044327; C:dendritic spine head; ISS:UniProtKB.
DR GO; GO:0032591; C:dendritic spine membrane; ISS: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; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045095; C:keratin filament; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0048786; C:presynaptic active zone; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS: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:MGI.
DR GO; GO:1903924; F:estradiol binding; ISO:MGI.
DR GO; GO:0038054; F:G protein-coupled estrogen receptor activity; ISS:UniProtKB.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:UniProtKB.
DR GO; GO:0003707; F:nuclear steroid receptor activity; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
DR GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0030263; P:apoptotic chromosome condensation; ISS: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; IDA:UniProtKB.
DR GO; GO:0071389; P:cellular response to mineralocorticoid stimulus; ISS: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:MGI.
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; ISO:MGI.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0010948; P:negative regulation of cell cycle process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS: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; IDA:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1900121; P:negative regulation of receptor binding; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2000724; P:positive regulation of cardiac vascular smooth muscle cell differentiation; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
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; ISS: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; ISS: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; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IDA: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; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS: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; IDA: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; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; ISO:MGI.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISO:MGI.
DR GO; GO:0042311; P:vasodilation; ISS:UniProtKB.
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_0000069311"
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"
FT MUTAGEN 375
FT /note="V->A: Loss of interaction with DLG4."
FT /evidence="ECO:0000269|PubMed:23300088"
FT CONFLICT 314
FT /note="F -> I (in Ref. 1; BAC26930)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="V -> I (in Ref. 1; BAB31118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42479 MW; AF7E4795C3A9A405 CRC64;
MDATTPAQTV GVEIYLGPVW PAPSNSTPLA LNLSLALRED APGNLTGDLS EHQQYVIALF
LSCLYTIFLF PIGFVGNILI LVVNISFREK MTIPDLYFIN LAAADLILVA DSLIEVFNLD
EQYYDIAVLC TFMSLFLQIN MYSSVFFLTW MSFDRYLALA KAMRCGLFRT KHHARLSCGL
IWMASVSATL VPFTAVHLRH TEEACFCFAD VREVQWLEVT LGFIMPFAII GLCYSLIVRA
LIRAHRHRGL RPRRQKALRM IFAVVLVFFI CWLPENVFIS VHLLQWTQPG DTPCKQSFRH
AYPLTGHIVN LAAFSNSCLN PLIYSFLGET FRDKLRLYVE QKTSLPALNR FCHATLKAVI
PDSTEQSEVR FSSAV
