ID GPER1_HUMAN Reviewed; 375 AA. AC Q99527; A8K6C5; B5BUJ1; O00143; O43494; Q13631; Q6FHL1; Q96F42; Q99981; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 02-SEP-2026, entry version 211. DE RecName: Full=G protein-coupled estrogen receptor 1 {ECO:0000305}; DE AltName: Full=Chemoattractant receptor-like 2; DE AltName: Full=Flow-induced endothelial G protein-coupled receptor 1; DE Short=FEG-1; DE AltName: Full=G protein-coupled receptor 30 {ECO:0000303|PubMed:17379646, ECO:0000303|PubMed:18566127}; DE AltName: Full=GPCR-Br; DE AltName: Full=IL8-related receptor DRY12; DE AltName: Full=Lymphocyte-derived G protein-coupled receptor; DE Short=LYGPR; DE AltName: Full=Membrane estrogen receptor; DE Short=mER; GN Name=GPER1 {ECO:0000312|HGNC:HGNC:4485}; GN Synonyms=CEPR, CMKRL2, DRY12, GPER, GPR30 GN {ECO:0000303|PubMed:17379646, ECO:0000303|PubMed:18566127}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8920907; DOI=10.1006/bbrc.1996.1654; RA Owman C.S.O., Blay P., Nilsson C., Lolait S.J.; RT "Cloning of human cDNA encoding a novel heptahelix receptor expressed in RT Burkitt's lymphoma and widely distributed in brain and peripheral RT tissues."; RL Biochem. Biophys. Res. Commun. 228:285-292(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9070864; DOI=10.1006/bbrc.1997.6161; RA Feng Y., Gregor P.; RT "Cloning of a novel member of the G protein-coupled receptor family related RT to peptide receptors."; RL Biochem. Biophys. Res. Commun. 231:651-654(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9398636; DOI=10.1006/bbrc.1997.7734; RA Takada Y., Kato C., Kondo S., Korenaga R., Ando J.; RT "Cloning of cDNAs encoding G protein-coupled receptor expressed in human RT endothelial cells exposed to fluid shear stress."; RL Biochem. Biophys. Res. Commun. 240:737-741(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9141481; DOI=10.1016/s0014-5793(97)00278-0; RA Kvingedal A.M., Smeland E.B.; RT "A novel putative G-protein-coupled receptor expressed in lung, heart and RT lymphoid tissue."; RL FEBS Lett. 407:59-62(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9367686; DOI=10.1006/geno.1997.4972; RA Carmeci C., Thompson D.A., Ring H.Z., Francke U., Weigel R.J.; RT "Identification of a gene (GPR30) with homology to the G-protein-coupled RT receptor superfamily associated with estrogen receptor expression in breast RT cancer."; RL Genomics 45:607-617(1997). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9479505; DOI=10.1006/geno.1998.5095; RA O'Dowd B.F., Nguyen T., Marchese A., Cheng R., Lynch K.R., Heng H.H.Q., RA Kolakowski L.F. Jr., George S.R.; RT "Discovery of three novel G-protein-coupled receptor genes."; RL Genomics 47:310-313(1998). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA McCoy R.L., Perlmutter D.H.; RT "Cloning of novel IL8-related receptors from human hepatic tissue."; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-16. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-16. RC TISSUE=Uterus; 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 [14] RP FUNCTION. RX PubMed=11043579; DOI=10.1210/mend.14.10.0532; RA Filardo E.J., Quinn J.A., Bland K.I., Frackelton A.R. Jr.; RT "Estrogen-induced activation of Erk-1 and Erk-2 requires the G protein- RT coupled receptor homolog, GPR30, and occurs via trans-activation of the RT epidermal growth factor receptor through release of HB-EGF."; RL Mol. Endocrinol. 14:1649-1660(2000). RN [15] RP INDUCTION. RX PubMed=12027886; DOI=10.1046/j.1432-1033.2002.02912.x; RA Ahola T.M., Purmonen S., Pennanen P., Zhuang Y.H., Tuohimaa P., Ylikomi T.; RT "Progestin upregulates G-protein-coupled receptor 30 in breast cancer RT cells."; RL Eur. J. Biochem. 269:2485-2490(2002). RN [16] RP FUNCTION, ESTROGEN-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR RP LOCATION. RX PubMed=15539556; DOI=10.1210/en.2004-1064; RA Thomas P., Pang Y., Filardo E.J., Dong J.; RT "Identity of an estrogen membrane receptor coupled to a G protein in human RT breast cancer cells."; RL Endocrinology 146:624-632(2005). RN [17] RP FUNCTION, ESTROGEN-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR RP LOCATION. RX PubMed=15705806; DOI=10.1126/science.1106943; RA Revankar C.M., Cimino D.F., Sklar L.A., Arterburn J.B., Prossnitz E.R.; RT "A transmembrane intracellular estrogen receptor mediates rapid cell RT signaling."; RL Science 307:1625-1630(2005). RN [18] RP ABSENCE OF ESTROGEN-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=16645038; DOI=10.1210/me.2005-0525; RA Pedram A., Razandi M., Levin E.R.; RT "Nature of functional estrogen receptors at the plasma membrane."; RL Mol. Endocrinol. 20:1996-2009(2006). RN [19] RP SUBCELLULAR LOCATION. RX PubMed=17379646; DOI=10.1210/en.2006-1605; RA Filardo E., Quinn J., Pang Y., Graeber C., Shaw S., Dong J., Thomas P.; RT "Activation of the novel estrogen receptor G protein-coupled receptor 30 RT (GPR30) at the plasma membrane."; RL Endocrinology 148:3236-3245(2007). RN [20] RP ABSENCE OF ESTROGEN-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=18566127; DOI=10.1210/en.2008-0269; RA Otto C., Rohde-Schulz B., Schwarz G., Fuchs I., Klewer M., Brittain D., RA Langer G., Bader B., Prelle K., Nubbemeyer R., Fritzemeier K.H.; RT "G protein-coupled receptor 30 localizes to the endoplasmic reticulum and RT is not activated by estradiol."; RL Endocrinology 149:4846-4856(2008). RN [21] 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 [22] RP FUNCTION. RX PubMed=19342448; DOI=10.1210/me.2008-0262; RA Quinn J.A., Graeber C.T., Frackelton A.R. Jr., Kim M., Schwarzbauer J.E., RA Filardo E.J.; RT "Coordinate regulation of estrogen-mediated fibronectin matrix assembly and RT epidermal growth factor receptor transactivation by the G protein-coupled RT receptor, GPR30."; RL Mol. Endocrinol. 23:1052-1064(2009). RN [23] RP INTERACTION WITH EGFR AND ESR1, AND INDUCTION. RX PubMed=19749156; DOI=10.1210/me.2009-0120; RA Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F., RA Fuqua S.A., Ando S., Maggiolini M.; RT "G protein-coupled receptor 30 expression is up-regulated by EGF and TGF RT alpha in estrogen receptor alpha-positive cancer cells."; RL Mol. Endocrinol. 23:1815-1826(2009). RN [24] RP FUNCTION, INTERACTION WITH EGFR, ASSOCIATION WITH CHROMATIN, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=20551055; DOI=10.1158/0008-5472.can-10-0408; RA Madeo A., Maggiolini M.; RT "Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol- RT induced gene expression and migration in breast cancer-associated RT fibroblasts."; RL Cancer Res. 70:6036-6046(2010). RN [25] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=20203690; DOI=10.1038/cdd.2010.20; RA Chan Q.K., Lam H.M., Ng C.F., Lee A.Y., Chan E.S., Ng H.K., Ho S.M., RA Lau K.M.; RT "Activation of GPR30 inhibits the growth of prostate cancer cells through RT sustained activation of Erk1/2, c-jun/c-fos-dependent upregulation of p21, RT and induction of G(2) cell-cycle arrest."; RL Cell Death Differ. 17:1511-1523(2010). RN [26] RP ESTROGEN-BINDING, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=19931550; DOI=10.1016/j.steroids.2009.11.005; RA Thomas P., Alyea R., Pang Y., Peyton C., Dong J., Berg A.H.; RT "Conserved estrogen binding and signaling functions of the G protein- RT coupled estrogen receptor 1 (GPER) in mammals and fish."; RL Steroids 75:595-602(2010). RN [27] RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY. RX PubMed=21427217; DOI=10.1210/en.2010-0979; RA Maiti K., Paul J.W., Read M., Chan E.C., Riley S.C., Nahar P., Smith R.; RT "G-1-activated membrane estrogen receptors mediate increased contractility RT of the human myometrium."; RL Endocrinology 152:2448-2455(2011). RN [28] RP ALDOSTERONE-BINDING, AND FUNCTION. 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 [29] RP SUBCELLULAR LOCATION, AND UBIQUITINATION. RX PubMed=21540189; DOI=10.1074/jbc.m111.224071; RA Cheng S.B., Quinn J.A., Graeber C.T., Filardo E.J.; RT "Down-modulation of the G-protein-coupled estrogen receptor, GPER, from the RT cell surface occurs via a trans-Golgi-proteasome pathway."; RL J. Biol. Chem. 286:22441-22455(2011). RN [30] RP FUNCTION, INTERACTION WITH KRT7 AND KRT8, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. 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 [31] 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 [32] RP FUNCTION. RX PubMed=23135268; DOI=10.1074/jbc.m112.417303; RA Santolla M.F., Lappano R., De Marco P., Pupo M., Vivacqua A., Sisci D., RA Abonante S., Iacopetta D., Cappello A.R., Dolce V., Maggiolini M.; RT "G protein-coupled estrogen receptor mediates the up-regulation of fatty RT acid synthase induced by 17beta-estradiol in cancer cells and cancer- RT associated fibroblasts."; RL J. Biol. Chem. 287:43234-43245(2012). RN [33] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=23285008; DOI=10.1371/journal.pone.0052357; RA Chakrabarti S., Davidge S.T.; RT "G-protein coupled receptor 30 (GPR30): a novel regulator of endothelial RT inflammation."; RL PLoS ONE 7:E52357-E52357(2012). RN [34] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [35] RP ALDOSTERONE-BINDING, AND FUNCTION. 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 [36] RP FUNCTION, INTERACTION WITH RAMP3, AND SUBCELLULAR LOCATION. 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 [37] RP REVIEW. RX PubMed=22521564; DOI=10.1016/j.steroids.2012.04.001; RA Barton M.; RT "Position paper: The membrane estrogen receptor GPER--Clues and RT questions."; RL Steroids 77:935-942(2012). RN [38] RP REVIEW. RX PubMed=22495674; DOI=10.1210/en.2012-1061; RA Filardo E.J., Thomas P.; RT "Minireview: G protein-coupled estrogen receptor-1, GPER-1: its mechanism RT of action and role in female reproductive cancer, renal and vascular RT physiology."; RL Endocrinology 153:2953-2962(2012). 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. Also CC functions as a receptor for aldosterone mediating rapid regulation of CC 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:11043579, CC ECO:0000269|PubMed:15539556, ECO:0000269|PubMed:15705806, CC ECO:0000269|PubMed:19179659, ECO:0000269|PubMed:19342448, CC ECO:0000269|PubMed:20203690, ECO:0000269|PubMed:20551055, CC ECO:0000269|PubMed:21149639, ECO:0000269|PubMed:21242460, CC ECO:0000269|PubMed:21427217, ECO:0000269|PubMed:23135268, CC ECO:0000269|PubMed:23283935, ECO:0000269|PubMed:23285008, CC ECO:0000269|PubMed:23674134}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Note=Binds 17-beta-estradiol (E2) in plasma membranes with high CC affinity (Kd is 3.3 nM) and displays rapid kinetics of association CC and dissociation. {ECO:0000269|PubMed:15539556, CC ECO:0000269|PubMed:15705806, ECO:0000269|PubMed:19931550}; CC -!- SUBUNIT: Homodimer (Probable). Heterodimer; heterodimerizes with other CC G protein-coupled receptor (GPCRs) like CRHR1, HTR1A and PAQR8. 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). Interacts CC with RAMP3; the interaction confers proper subcellular localization and CC function in cardioprotection. 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 {ECO:0000250, ECO:0000269|PubMed:19749156, ECO:0000269|PubMed:20551055, CC ECO:0000269|PubMed:21149639, ECO:0000269|PubMed:23674134, ECO:0000305}. CC -!- INTERACTION: CC Q99527; P08588: ADRB1; NbExp=6; IntAct=EBI-2833021, EBI-991009; CC Q99527; P24588: AKAP5; NbExp=2; IntAct=EBI-2833021, EBI-703640; CC Q99527; O14745: NHERF1; NbExp=6; IntAct=EBI-2833021, EBI-349787; CC Q99527; O60894: RAMP1; NbExp=3; IntAct=EBI-2833021, EBI-962893; CC Q99527; O60895: RAMP2; NbExp=3; IntAct=EBI-2833021, EBI-9009040; CC Q99527; O60896: RAMP3; NbExp=4; IntAct=EBI-2833021, EBI-720447; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, CC perinuclear region. Cytoplasm, cytoskeleton. Cell membrane; Multi-pass CC membrane protein. Basolateral cell membrane; Multi-pass membrane CC protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. CC Early endosome. Recycling endosome. Golgi apparatus membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi CC apparatus, trans-Golgi network. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:18566127}; Multi-pass membrane protein. Cell CC projection, dendrite {ECO:0000250}. Cell projection, dendritic spine CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell CC projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. CC Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein CC {ECO:0000250}. Note=Colocalized with BSN to the active zone of CC presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B CC in neuronal synaptosomes (By similarity). Endocytosed in a agonist- and CC arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated CC pits at the plasma membrane. Colocalized with transferrin receptor at CC the plasma membrane and perinuclear region. Accumulated and colocalized CC with RAB11 proteins in recycling endosomes and trans-Golgi network CC (TGN), but does neither recycle back to the cell surface nor traffics CC to late endosome or lysosome. Colocalized with calnexin in the CC endoplasmic reticulum. Traffics to intracellular sites via cytokeratin CC intermediate filaments like KRT7 and KRT8 after constitutive CC endocytosis in epithelial cells. Colocalized with EGFR in the nucleus CC of agonist-induced cancer-associated fibroblasts (CAF). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in placenta, endothelial and epithelial CC cells, non laboring and laboring term myometrium, fibroblasts and CC cancer-associated fibroblasts (CAF), prostate cancer cells and invasive CC adenocarcinoma (at protein level). Ubiquitously expressed, but is most CC abundant in placenta. In brain regions, expressed as a 2.8 kb CC transcript in basal forebrain, frontal cortex, thalamus, hippocampus, CC caudate and putamen. {ECO:0000269|PubMed:20203690, CC ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:21149639, CC ECO:0000269|PubMed:21354433, ECO:0000269|PubMed:21427217, CC ECO:0000269|PubMed:23285008}. CC -!- INDUCTION: Up-regulated by EGF and TGF-alpha in endometrial, ovarian CC and breast tumor cells. Up-regulated by progestin and by phorbol 12- CC myristate 13-acetate (PMA) in breast cancer cell lines. CC {ECO:0000269|PubMed:12027886, ECO:0000269|PubMed:19749156}. CC -!- PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and CC leads to proteasome-mediated degradation. CC {ECO:0000269|PubMed:21540189}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:21427217}. CC -!- MISCELLANEOUS: Does not bind estradiol according to PubMed:18566127 and CC PubMed:16645038. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- CAUTION: Data is conflicting regarding whether it fulfills the criteria CC of a membrane-bound estrogen receptor (PubMed:15705806, CC PubMed:17379646). Other reports suggest that it is not CC (PubMed:16645038, PubMed:18566127). {ECO:0000305|PubMed:15705806, CC ECO:0000305|PubMed:16645038, ECO:0000305|PubMed:17379646, CC ECO:0000305|PubMed:18566127}. CC -!- CAUTION: Data is conflicting regarding whether it is localized either CC at the cell membrane (PM) (PubMed:15539556, PubMed:21149639, CC PubMed:21354433, PubMed:21427217, PubMed:21540189, PubMed:23674134). CC Other reports suggest that it localizes at the endoplasmic reticulum CC (ER) (PubMed:15705806, PubMed:18566127). {ECO:0000305|PubMed:15539556, CC ECO:0000305|PubMed:15705806, ECO:0000305|PubMed:18566127, CC ECO:0000305|PubMed:21149639, ECO:0000305|PubMed:21354433, CC ECO:0000305|PubMed:21427217, ECO:0000305|PubMed:21540189, CC ECO:0000305|PubMed:23674134}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44344/GPER"; 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; Y08162; CAA69354.1; -; mRNA. DR EMBL; U77827; AAC51173.1; -; Genomic_DNA. DR EMBL; AF015257; AAC51904.1; -; mRNA. DR EMBL; X98510; CAA67133.1; -; mRNA. DR EMBL; U63917; AAB88017.1; -; mRNA. DR EMBL; AF027956; AAC52027.1; -; Genomic_DNA. DR EMBL; U58828; AAB02736.1; -; mRNA. DR EMBL; CR541741; CAG46541.1; -; mRNA. DR EMBL; AK291590; BAF84279.1; -; mRNA. DR EMBL; AB451427; BAG70241.1; -; mRNA. DR EMBL; CH236953; EAL23938.1; -; Genomic_DNA. DR EMBL; CH471144; EAW87194.1; -; Genomic_DNA. DR EMBL; BC011634; AAH11634.1; -; mRNA. DR CCDS; CCDS5322.1; -. DR PIR; G02670; G02670. DR PIR; JC5069; JC5069. DR RefSeq; NP_001035055.1; NM_001039966.2. DR RefSeq; NP_001091671.1; NM_001098201.3. DR RefSeq; NP_001496.1; NM_001505.3. DR PDB; 8XOF; EM; 2.60 A; R=1-375. DR PDB; 8XOG; EM; 2.90 A; R=1-375. DR PDB; 8XOH; EM; 3.20 A; R=1-375. DR PDB; 8XOI; EM; 3.20 A; R=1-375. DR PDB; 8XOJ; EM; 3.10 A; R=1-375. DR AlphaFoldDB; Q99527; -. DR EMDB; EMD-38527; -. DR EMDB; EMD-38528; -. DR EMDB; EMD-38529; -. DR EMDB; EMD-38530; -. DR EMDB; EMD-38531; -. DR SMR; Q99527; -. DR BioGRID; 109110; 4. DR CORUM; Q99527; -. DR FunCoup; Q99527; 533. DR IntAct; Q99527; 9. DR NDEx; IQUERY-CP-GPER1; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000380281; -. DR BindingDB; Q99527; -. DR ChEMBL; CHEMBL5872; -. DR DrugBank; DB00783; Estradiol. DR DrugBank; DB13952; Estradiol acetate. DR DrugBank; DB13953; Estradiol benzoate. DR DrugBank; DB13954; Estradiol cypionate. DR DrugBank; DB13955; Estradiol dienanthate. DR DrugBank; DB13956; Estradiol valerate. DR DrugBank; DB16547; Furvina. DR DrugBank; DB01645; Genistein. DR DrugBank; DB18091; LNS-8801. DR DrugBank; DB05939; MK-0354. DR DrugCentral; Q99527; -. DR GuidetoPHARMACOLOGY; 221; -. DR TCDB; 9.A.14.13.19; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; Q99527; 3 sites, No reported glycans. DR GlyGen; Q99527; 3 sites. DR iPTMnet; Q99527; -. DR PhosphoSitePlus; Q99527; -. DR BioMuta; GPER1; -. DR DMDM; 3023539; -. DR MassIVE; Q99527; -. DR PaxDb; 9606-ENSP00000380281; -. DR PeptideAtlas; Q99527; -. DR Antibodypedia; 10887; 436 antibodies from 36 providers. DR DNASU; 2852; -. DR Ensembl; ENST00000297469.3; ENSP00000297469.3; ENSG00000164850.17. DR Ensembl; ENST00000397088.4; ENSP00000380277.3; ENSG00000164850.17. DR Ensembl; ENST00000397092.5; ENSP00000380281.1; ENSG00000164850.17. DR Ensembl; ENST00000401670.1; ENSP00000385151.1; ENSG00000164850.17. DR Ensembl; ENST00000853504.1; ENSP00000523563.1; ENSG00000164850.17. DR Ensembl; ENST00000853505.1; ENSP00000523564.1; ENSG00000164850.17. DR Ensembl; ENST00000853506.1; ENSP00000523565.1; ENSG00000164850.17. DR Ensembl; ENST00000853507.1; ENSP00000523566.1; ENSG00000164850.17. DR Ensembl; ENST00000853508.1; ENSP00000523567.1; ENSG00000164850.17. DR Ensembl; ENST00000853509.1; ENSP00000523568.1; ENSG00000164850.17. DR Ensembl; ENST00000853510.1; ENSP00000523569.1; ENSG00000164850.17. DR Ensembl; ENST00000853511.1; ENSP00000523570.1; ENSG00000164850.17. DR Ensembl; ENST00000853512.1; ENSP00000523571.1; ENSG00000164850.17. DR Ensembl; ENST00000853513.1; ENSP00000523572.1; ENSG00000164850.17. DR Ensembl; ENST00000964574.1; ENSP00000634633.1; ENSG00000164850.17. DR Ensembl; ENST00000964575.1; ENSP00000634634.1; ENSG00000164850.17. DR GeneID; 2852; -. DR KEGG; hsa:2852; -. DR MANE-Select; ENST00000397088.4; ENSP00000380277.3; NM_001098201.3; NP_001091671.1. DR UCSC; uc003sjz.1; human. DR AGR; HGNC:4485; -. DR ClinPGx; PA28873; -. DR CTD; 2852; -. DR DisGeNET; 2852; -. DR GeneCards; GPER1; -. DR HGNC; HGNC:4485; GPER1. DR HPA; ENSG00000164850; Tissue enhanced (stomach). DR MIM; 601805; gene. DR OpenTargets; ENSG00000164850; -. DR VEuPathDB; HostDB:ENSG00000164850; -. DR eggNOG; ENOG502QU56; Eukaryota. DR GeneTree; ENSGT00940000154307; -. DR HOGENOM; CLU_009579_8_3_1; -. DR InParanoid; Q99527; -. DR OMA; FRTKQHA; -. DR OrthoDB; 5957382at2759; -. DR PAN-GO; Q99527; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q99527; -. DR PathwayCommons; Q99527; -. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-9634597; GPER1 signaling. DR SignaLink; Q99527; -. DR SIGNOR; Q99527; -. DR Agora; ENSG00000164850; -. DR BioGRID-ORCS; 2852; 13 hits in 1132 CRISPR screens. DR GeneWiki; GPR30; -. DR GenomeRNAi; 2852; -. DR Pharos; Q99527; Tchem. DR PRO; PR:Q99527; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q99527; protein. DR Bgee; ENSG00000164850; Expressed in body of stomach and 131 other cell types or tissues. DR ExpressionAtlas; Q99527; baseline and differential. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; EXP:UniProtKB. 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; IEA:Ensembl. DR GO; GO:0045095; C:keratin filament; IDA:UniProtKB. DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0038054; F:G protein-coupled estrogen receptor activity; ISS:UniProtKB. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:UniProtKB. DR GO; GO:0005496; F:steroid binding; IDA:UniProtKB. DR GO; GO:1990239; F:steroid hormone binding; IDA: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: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; ISS:UniProtKB. DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IDA:UniProtKB. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB. DR GO; GO:0030520; P:estrogen receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:AgBase. DR GO; GO:0010948; P:negative regulation of cell cycle process; IMP:AgBase. 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; IMP:AgBase. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:AgBase. DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB. DR GO; GO:0002695; P:negative regulation of leukocyte activation; IDA:UniProtKB. DR GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISS:UniProtKB. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:AgBase. DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:AgBase. 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:0030518; P:nuclear receptor-mediated steroid hormone signaling pathway; IDA: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; IMP:AgBase. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP: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; 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; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase. DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IDA: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:UniProtKB. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA: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; IDA: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; IDA:UniProtKB. 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:0043401; P:steroid hormone receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0042311; P:vasodilation; ISS:UniProtKB. DR CDD; cd14989; 7tmA_GPER1; 1. DR FunFam; 1.20.1070.10:FF:000093; G-protein coupled estrogen receptor 1; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR047143; GPER1-like. DR PANTHER; PTHR24226:SF2; G-PROTEIN COUPLED ESTROGEN RECEPTOR 1; 1. DR PANTHER; PTHR24226; G-PROTEIN COUPLED RECEPTOR 182 AND ESTROGEN RECEPTOR 1; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PDBsum; 8XOF; -. DR PDBsum; 8XOG; -. DR PDBsum; 8XOH; -. DR PDBsum; 8XOI; -. DR PDBsum; 8XOJ; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Apoptosis; Cell cycle; Cell membrane; KW Cell projection; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; KW Differentiation; 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_0000069310" 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:0007744|PubMed:22814378" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" 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 VARIANT 16 FT /note="P -> L (in dbSNP:rs11544331)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:19054851" FT /id="VAR_033319" FT CONFLICT 20..21 FT /note="QP -> HA (in Ref. 6; AAC52027)" FT /evidence="ECO:0000305" FT CONFLICT 32..49 FT /note="Missing (in Ref. 7; AAB02736)" FT /evidence="ECO:0000305" FT CONFLICT 104 FT /note="A -> G (in Ref. 7; AAB02736)" FT /evidence="ECO:0000305" FT CONFLICT 140..146 FT /note="NMYSSVF -> QHVQAASS (in Ref. 7; AAB02736)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="G -> A (in Ref. 7; AAB02736)" FT /evidence="ECO:0000305" FT CONFLICT 184 FT /note="A -> S (in Ref. 7; AAB02736)" FT /evidence="ECO:0000305" FT CONFLICT 312 FT /note="A -> T (in Ref. 2; AAC51173)" FT /evidence="ECO:0000305" FT CONFLICT 320 FT /note="N -> T (in Ref. 7; AAB02736)" FT /evidence="ECO:0000305" FT CONFLICT 355 FT /note="A -> V (in Ref. 7; AAB02736)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="A -> V (in Ref. 7; AAB02736)" FT /evidence="ECO:0000305" FT HELIX 51..86 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 93..116 FT /evidence="ECO:0007829|PDB:8XOF" FT TURN 117..120 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:8XOG" FT HELIX 126..130 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 131..160 FT /evidence="ECO:0007829|PDB:8XOF" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:8XOF" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 171..197 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 212..219 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 220..224 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 225..245 FT /evidence="ECO:0007829|PDB:8XOF" FT TURN 246..248 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 251..282 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 303..321 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 322..326 FT /evidence="ECO:0007829|PDB:8XOF" FT HELIX 329..341 FT /evidence="ECO:0007829|PDB:8XOF" SQ SEQUENCE 375 AA; 42248 MW; 0A54EED8A698F075 CRC64; MDVTSQARGV GLEMYPGTAQ PAAPNTTSPE LNLSHPLLGT ALANGTGELS EHQQYVIGLF LSCLYTIFLF PIGFVGNILI LVVNISFREK MTIPDLYFIN LAVADLILVA DSLIEVFNLH ERYYDIAVLC TFMSLFLQVN MYSSVFFLTW MSFDRYIALA RAMRCSLFRT KHHARLSCGL IWMASVSATL VPFTAVHLQH TDEACFCFAD VREVQWLEVT LGFIVPFAII GLCYSLIVRV LVRAHRHRGL RPRRQKALRM ILAVVLVFFV CWLPENVFIS VHLLQRTQPG AAPCKQSFRH AHPLTGHIVN LAAFSNSCLN PLIYSFLGET FRDKLRLYIE QKTNLPALNR FCHAALKAVI PDSTEQSDVR FSSAV //