GPER1_HUMAN
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 03-AUG-2022, entry version 193.
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 estrogen receptor 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 {ECO:0000303|PubMed:17379646,
GN 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.
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: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. Interacts with KRT7 and KRT8. Interacts with EGFR; the
CC interaction increases after agonist-induced stimulation in cancer-
CC 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 -!- 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:21427217,
CC PubMed:21540189, PubMed:21354433, PubMed:21149639 and 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="http://atlasgeneticsoncology.org/Genes/GPERID44344ch7p22.html";
CC ---------------------------------------------------------------------------
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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_001039966.1.
DR RefSeq; NP_001091671.1; NM_001098201.1.
DR RefSeq; NP_001496.1; NM_001505.2.
DR AlphaFoldDB; Q99527; -.
DR SMR; Q99527; -.
DR BioGRID; 109110; 4.
DR IntAct; Q99527; 1.
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; DB01645; Genistein.
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 GlyGen; Q99527; 3 sites.
DR iPTMnet; Q99527; -.
DR PhosphoSitePlus; Q99527; -.
DR BioMuta; GPER1; -.
DR DMDM; 3023539; -.
DR PaxDb; Q99527; -.
DR PeptideAtlas; Q99527; -.
DR PRIDE; Q99527; -.
DR Antibodypedia; 10887; 426 antibodies from 34 providers.
DR DNASU; 2852; -.
DR Ensembl; ENST00000297469.3; ENSP00000297469.3; ENSG00000164850.16.
DR Ensembl; ENST00000397088.4; ENSP00000380277.3; ENSG00000164850.16.
DR Ensembl; ENST00000397092.5; ENSP00000380281.1; ENSG00000164850.16.
DR Ensembl; ENST00000401670.1; ENSP00000385151.1; ENSG00000164850.16.
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 CTD; 2852; -.
DR DisGeNET; 2852; -.
DR GeneCards; GPER1; -.
DR HGNC; HGNC:4485; GPER1.
DR HPA; ENSG00000164850; Tissue enhanced (stomach).
DR MIM; 601805; gene.
DR neXtProt; NX_Q99527; -.
DR OpenTargets; ENSG00000164850; -.
DR PharmGKB; PA28873; -.
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; 736624at2759; -.
DR PhylomeDB; Q99527; -.
DR TreeFam; TF333506; -.
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 BioGRID-ORCS; 2852; 13 hits in 1057 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 130 other tissues.
DR ExpressionAtlas; Q99527; baseline and differential.
DR Genevisible; Q99527; HS.
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; 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; IEA:UniProtKB-SubCell.
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:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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; TAS:ProtInc.
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: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; 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:0007186; P:G protein-coupled receptor signaling pathway; IMP:AgBase.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
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 protein kinase B signaling; IMP:AgBase.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:AgBase.
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; 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: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; 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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; 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 mediated signaling pathway; IDA:UniProtKB.
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_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"
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
