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G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (Flow-induced endothelial G-protein coupled receptor 1) (FEG-1) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (GPCR-Br) (IL8-related receptor DRY12) (Lymphocyte-derived G-protein coupled receptor) (LYGPR) (Membrane estrogen receptor) (mER)

 GPER1_HUMAN             Reviewed;         375 AA.
Q99527; A8K6C5; B5BUJ1; O00143; O43494; Q13631; Q6FHL1; Q96F42;
Q99981;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
31-JUL-2019, entry version 176.
RecName: Full=G-protein coupled estrogen receptor 1;
AltName: Full=Chemoattractant receptor-like 2;
AltName: Full=Flow-induced endothelial G-protein coupled receptor 1;
Short=FEG-1;
AltName: Full=G protein-coupled estrogen receptor 1;
AltName: Full=G-protein coupled receptor 30;
AltName: Full=GPCR-Br;
AltName: Full=IL8-related receptor DRY12;
AltName: Full=Lymphocyte-derived G-protein coupled receptor;
Short=LYGPR;
AltName: Full=Membrane estrogen receptor;
Short=mER;
Name=GPER1; Synonyms=CEPR, CMKRL2, DRY12, GPER, GPR30;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8920907; DOI=10.1006/bbrc.1996.1654;
Owman C.S.O., Blay P., Nilsson C., Lolait S.J.;
"Cloning of human cDNA encoding a novel heptahelix receptor expressed
in Burkitt's lymphoma and widely distributed in brain and peripheral
tissues.";
Biochem. Biophys. Res. Commun. 228:285-292(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9070864; DOI=10.1006/bbrc.1997.6161;
Feng Y., Gregor P.;
"Cloning of a novel member of the G protein-coupled receptor family
related to peptide receptors.";
Biochem. Biophys. Res. Commun. 231:651-654(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9398636; DOI=10.1006/bbrc.1997.7734;
Takada Y., Kato C., Kondo S., Korenaga R., Ando J.;
"Cloning of cDNAs encoding G protein-coupled receptor expressed in
human endothelial cells exposed to fluid shear stress.";
Biochem. Biophys. Res. Commun. 240:737-741(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9141481; DOI=10.1016/S0014-5793(97)00278-0;
Kvingedal A.M., Smeland E.B.;
"A novel putative G-protein-coupled receptor expressed in lung, heart
and lymphoid tissue.";
FEBS Lett. 407:59-62(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9367686; DOI=10.1006/geno.1997.4972;
Carmeci C., Thompson D.A., Ring H.Z., Francke U., Weigel R.J.;
"Identification of a gene (GPR30) with homology to the G-protein-
coupled receptor superfamily associated with estrogen receptor
expression in breast cancer.";
Genomics 45:607-617(1997).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9479505; DOI=10.1006/geno.1998.5095;
O'Dowd B.F., Nguyen T., Marchese A., Cheng R., Lynch K.R.,
Heng H.H.Q., Kolakowski L.F. Jr., George S.R.;
"Discovery of three novel G-protein-coupled receptor genes.";
Genomics 47:310-313(1998).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
McCoy R.L., Perlmutter D.H.;
"Cloning of novel IL8-related receptors from human hepatic tissue.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-16.
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-16.
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
FUNCTION.
PubMed=11043579; DOI=10.1210/mend.14.10.0532;
Filardo E.J., Quinn J.A., Bland K.I., Frackelton A.R. Jr.;
"Estrogen-induced activation of Erk-1 and Erk-2 requires the G
protein-coupled receptor homolog, GPR30, and occurs via trans-
activation of the epidermal growth factor receptor through release of
HB-EGF.";
Mol. Endocrinol. 14:1649-1660(2000).
[15]
INDUCTION.
PubMed=12027886; DOI=10.1046/j.1432-1033.2002.02912.x;
Ahola T.M., Purmonen S., Pennanen P., Zhuang Y.H., Tuohimaa P.,
Ylikomi T.;
"Progestin upregulates G-protein-coupled receptor 30 in breast cancer
cells.";
Eur. J. Biochem. 269:2485-2490(2002).
[16]
FUNCTION, ESTROGEN-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
PubMed=15539556; DOI=10.1210/en.2004-1064;
Thomas P., Pang Y., Filardo E.J., Dong J.;
"Identity of an estrogen membrane receptor coupled to a G protein in
human breast cancer cells.";
Endocrinology 146:624-632(2005).
[17]
FUNCTION, ESTROGEN-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
PubMed=15705806; DOI=10.1126/science.1106943;
Revankar C.M., Cimino D.F., Sklar L.A., Arterburn J.B.,
Prossnitz E.R.;
"A transmembrane intracellular estrogen receptor mediates rapid cell
signaling.";
Science 307:1625-1630(2005).
[18]
ABSENCE OF ESTROGEN-BINDING, AND SUBCELLULAR LOCATION.
PubMed=16645038; DOI=10.1210/me.2005-0525;
Pedram A., Razandi M., Levin E.R.;
"Nature of functional estrogen receptors at the plasma membrane.";
Mol. Endocrinol. 20:1996-2009(2006).
[19]
SUBCELLULAR LOCATION.
PubMed=17379646; DOI=10.1210/en.2006-1605;
Filardo E., Quinn J., Pang Y., Graeber C., Shaw S., Dong J.,
Thomas P.;
"Activation of the novel estrogen receptor G protein-coupled receptor
30 (GPR30) at the plasma membrane.";
Endocrinology 148:3236-3245(2007).
[20]
ABSENCE OF ESTROGEN-BINDING, AND SUBCELLULAR LOCATION.
PubMed=18566127; DOI=10.1210/en.2008-0269;
Otto C., Rohde-Schulz B., Schwarz G., Fuchs I., Klewer M.,
Brittain D., Langer G., Bader B., Prelle K., Nubbemeyer R.,
Fritzemeier K.H.;
"G protein-coupled receptor 30 localizes to the endoplasmic reticulum
and is not activated by estradiol.";
Endocrinology 149:4846-4856(2008).
[21]
FUNCTION.
PubMed=19179659; DOI=10.1161/CIRCRESAHA.108.190892;
Haas E., Bhattacharya I., Brailoiu E., Damjanovic M., Brailoiu G.C.,
Gao X., Mueller-Guerre L., Marjon N.A., Gut A., Minotti R.,
Meyer M.R., Amann K., Ammann E., Perez-Dominguez A., Genoni M.,
Clegg D.J., Dun N.J., Resta T.C., Prossnitz E.R., Barton M.;
"Regulatory role of G protein-coupled estrogen receptor for vascular
function and obesity.";
Circ. Res. 104:288-291(2009).
[22]
FUNCTION.
PubMed=19342448; DOI=10.1210/me.2008-0262;
Quinn J.A., Graeber C.T., Frackelton A.R. Jr., Kim M.,
Schwarzbauer J.E., Filardo E.J.;
"Coordinate regulation of estrogen-mediated fibronectin matrix
assembly and epidermal growth factor receptor transactivation by the G
protein-coupled receptor, GPR30.";
Mol. Endocrinol. 23:1052-1064(2009).
[23]
INTERACTION WITH EGFR AND ESR1, AND INDUCTION.
PubMed=19749156; DOI=10.1210/me.2009-0120;
Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S.,
De Amicis F., Fuqua S.A., Ando S., Maggiolini M.;
"G protein-coupled receptor 30 expression is up-regulated by EGF and
TGF alpha in estrogen receptor alpha-positive cancer cells.";
Mol. Endocrinol. 23:1815-1826(2009).
[24]
FUNCTION, INTERACTION WITH EGFR, ASSOCIATION WITH CHROMATIN,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20551055; DOI=10.1158/0008-5472.CAN-10-0408;
Madeo A., Maggiolini M.;
"Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-
induced gene expression and migration in breast cancer-associated
fibroblasts.";
Cancer Res. 70:6036-6046(2010).
[25]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=20203690; DOI=10.1038/cdd.2010.20;
Chan Q.K., Lam H.M., Ng C.F., Lee A.Y., Chan E.S., Ng H.K., Ho S.M.,
Lau K.M.;
"Activation of GPR30 inhibits the growth of prostate cancer cells
through sustained activation of Erk1/2, c-jun/c-fos-dependent
upregulation of p21, and induction of G(2) cell-cycle arrest.";
Cell Death Differ. 17:1511-1523(2010).
[26]
ESTROGEN-BINDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19931550; DOI=10.1016/j.steroids.2009.11.005;
Thomas P., Alyea R., Pang Y., Peyton C., Dong J., Berg A.H.;
"Conserved estrogen binding and signaling functions of the G protein-
coupled estrogen receptor 1 (GPER) in mammals and fish.";
Steroids 75:595-602(2010).
[27]
FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=21427217; DOI=10.1210/en.2010-0979;
Maiti K., Paul J.W., Read M., Chan E.C., Riley S.C., Nahar P.,
Smith R.;
"G-1-activated membrane estrogen receptors mediate increased
contractility of the human myometrium.";
Endocrinology 152:2448-2455(2011).
[28]
ALDOSTERONE-BINDING, AND FUNCTION.
PubMed=21242460; DOI=10.1161/HYPERTENSIONAHA.110.161653;
Gros R., Ding Q., Sklar L.A., Prossnitz E.E., Arterburn J.B.,
Chorazyczewski J., Feldman R.D.;
"GPR30 expression is required for the mineralocorticoid receptor-
independent rapid vascular effects of aldosterone.";
Hypertension 57:442-451(2011).
[29]
SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=21540189; DOI=10.1074/jbc.M111.224071;
Cheng S.B., Quinn J.A., Graeber C.T., Filardo E.J.;
"Down-modulation of the G-protein-coupled estrogen receptor, GPER,
from the cell surface occurs via a trans-Golgi-proteasome pathway.";
J. Biol. Chem. 286:22441-22455(2011).
[30]
FUNCTION, INTERACTION WITH KRT7 AND KRT8, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=21149639; DOI=10.1124/mol.110.069500;
Sanden C., Broselid S., Cornmark L., Andersson K.,
Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.;
"G protein-coupled estrogen receptor 1/G protein-coupled receptor 30
localizes in the plasma membrane and traffics intracellularly on
cytokeratin intermediate filaments.";
Mol. Pharmacol. 79:400-410(2011).
[31]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=21354433; DOI=10.1016/j.steroids.2011.02.018;
Cheng S.B., Graeber C.T., Quinn J.A., Filardo E.J.;
"Retrograde transport of the transmembrane estrogen receptor, G-
protein-coupled-receptor-30 (GPR30/GPER) from the plasma membrane
towards the nucleus.";
Steroids 76:892-896(2011).
[32]
FUNCTION.
PubMed=23135268; DOI=10.1074/jbc.M112.417303;
Santolla M.F., Lappano R., De Marco P., Pupo M., Vivacqua A.,
Sisci D., Abonante S., Iacopetta D., Cappello A.R., Dolce V.,
Maggiolini M.;
"G protein-coupled estrogen receptor mediates the up-regulation of
fatty acid synthase induced by 17beta-estradiol in cancer cells and
cancer-associated fibroblasts.";
J. Biol. Chem. 287:43234-43245(2012).
[33]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23285008; DOI=10.1371/journal.pone.0052357;
Chakrabarti S., Davidge S.T.;
"G-protein coupled receptor 30 (GPR30): a novel regulator of
endothelial inflammation.";
PLoS ONE 7:E52357-E52357(2012).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[35]
ALDOSTERONE-BINDING, AND FUNCTION.
PubMed=23283935; DOI=10.1152/ajpcell.00203.2012;
Gros R., Ding Q., Liu B., Chorazyczewski J., Feldman R.D.;
"Aldosterone mediates its rapid effects in vascular endothelial cells
through GPER activation.";
Am. J. Physiol. 304:C532-C540(2013).
[36]
FUNCTION, INTERACTION WITH RAMP3, AND SUBCELLULAR LOCATION.
PubMed=23674134; DOI=10.1530/JME-13-0021;
Lenhart P.M., Broselid S., Barrick C.J., Leeb-Lundberg L.M.,
Caron K.M.;
"G-protein-coupled receptor 30 interacts with receptor activity-
modifying protein 3 and confers sex-dependent cardioprotection.";
J. Mol. Endocrinol. 51:191-202(2013).
[37]
REVIEW.
PubMed=22521564; DOI=10.1016/j.steroids.2012.04.001;
Barton M.;
"Position paper: The membrane estrogen receptor GPER--Clues and
questions.";
Steroids 77:935-942(2012).
[38]
REVIEW.
PubMed=22495674; DOI=10.1210/en.2012-1061;
Filardo E.J., Thomas P.;
"Minireview: G protein-coupled estrogen receptor-1, GPER-1: its
mechanism of action and role in female reproductive cancer, renal and
vascular physiology.";
Endocrinology 153:2953-2962(2012).
-!- FUNCTION: G-protein coupled estrogen receptor that binds to 17-
beta-estradiol (E2) with high affinity, leading to rapid and
transient activation of numerous intracellular signaling pathways.
Stimulates cAMP production, calcium mobilization and tyrosine
kinase Src inducing the release of heparin-bound epidermal growth
factor (HB-EGF) and subsequent transactivation of the epidermal
growth factor receptor (EGFR), activating downstream signaling
pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic
functions among others in the cardiovascular, endocrine,
reproductive, immune and central nervous systems. Has a role in
cardioprotection by reducing cardiac hypertrophy and perivascular
fibrosis in a RAMP3-dependent manner. Regulates arterial blood
pressure by stimulating vasodilation and reducing vascular smooth
muscle and microvascular endothelial cell proliferation. Plays a
role in blood glucose homeostasis contributing to the insulin
secretion response by pancreatic beta cells. Triggers
mitochondrial apoptosis during pachytene spermatocyte
differentiation. Stimulates uterine epithelial cell proliferation.
Enhances uterine contractility in response to oxytocin.
Contributes to thymic atrophy by inducing apoptosis. Attenuates
TNF-mediated endothelial expression of leukocyte adhesion
molecules. Promotes neuritogenesis in developing hippocampal
neurons. Plays a role in acute neuroprotection against NMDA-
induced excitotoxic neuronal death. Increases firing activity and
intracellular calcium oscillations in luteinizing hormone-
releasing hormone (LHRH) neurons. Inhibits early osteoblast
proliferation at growth plate during skeletal development.
Inhibits mature adipocyte differentiation and lipid accumulation.
Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma
membrane in epithelial cells. Functions also as a receptor for
aldosterone mediating rapid regulation of vascular contractibility
through the PI3K/ERK signaling pathway. Involved in cancer
progression regulation. Stimulates cancer-associated fibroblast
(CAF) proliferation by a rapid genomic response through the
EGFR/ERK transduction pathway. Associated with EGFR, may act as a
transcription factor activating growth regulatory genes (c-fos,
cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN)
matrix assembly in breast cancer cells.
{ECO:0000269|PubMed:11043579, ECO:0000269|PubMed:15539556,
ECO:0000269|PubMed:15705806, ECO:0000269|PubMed:19179659,
ECO:0000269|PubMed:19342448, ECO:0000269|PubMed:20203690,
ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:21149639,
ECO:0000269|PubMed:21242460, ECO:0000269|PubMed:21427217,
ECO:0000269|PubMed:23135268, ECO:0000269|PubMed:23283935,
ECO:0000269|PubMed:23285008, ECO:0000269|PubMed:23674134}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Binds 17-beta-estradiol (E2) in plasma membranes with high
affinity (Kd is 3.3 nM) and displays rapid kinetics of
association and dissociation. {ECO:0000269|PubMed:15539556,
ECO:0000269|PubMed:15705806, ECO:0000269|PubMed:19931550};
-!- SUBUNIT: Homodimer (Probable). Heterodimer; heterodimerizes with
other G-protein-coupled receptor (GPCRs) like CRHR1, HTR1A and
PAQR8. Interacts (via C-terminus tail motif) with DLG4 (via N-
terminus tandem pair of PDZ domains); the interaction is direct
and induces the increase of GPER1 protein levels residing at the
plasma membrane surface in a estradiol-independent manner (By
similarity). Interacts with RAMP3. Interacts with KRT7 and KRT8.
Interacts with EGFR; the interaction increases after agonist-
induced stimulation in cancer-associated fibroblasts (CAF).
Interacts with EGFR and ESR1. {ECO:0000250,
ECO:0000269|PubMed:19749156, ECO:0000269|PubMed:20551055,
ECO:0000269|PubMed:21149639, ECO:0000269|PubMed:23674134,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm,
perinuclear region. Cytoplasm, cytoskeleton. Cell membrane; Multi-
pass membrane protein. Basolateral cell membrane; Multi-pass
membrane protein. Cytoplasmic vesicle membrane; Multi-pass
membrane protein. Early endosome. Recycling endosome. Golgi
apparatus membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}. Golgi apparatus, trans-Golgi network. Endoplasmic
reticulum membrane; Multi-pass membrane protein. Cell projection,
dendrite {ECO:0000250}. Cell projection, dendritic spine membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
projection, axon {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}. Note=Colocalized with BSN to the active zone of
presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2
PPP1R9B in neuronal synaptosomes (By similarity). Endocytosed in a
agonist- and arrestin-independent manner. Colocalized with RAMP3
and clathrin-coated pits at the plasma membrane. Colocalized with
transferrin receptor at the plasma membrane and perinuclear
region. Accumulated and colocalized with RAB11 proteins in
recycling endosomes and trans-Golgi network (TGN), but does
neither recycle back to the cell surface nor traffics to late
endosome or lysosome. Colocalized with calnexin in the endoplasmic
reticulum. Traffics to intracellular sites via cytokeratin
intermediate filaments like KRT7 and KRT8 after constitutive
endocytosis in epithelial cells. Colocalized with EGFR in the
nucleus of agonist-induced cancer-associated fibroblasts (CAF).
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in placenta, endothelial and
epithelial cells, non laboring and laboring term myometrium,
fibroblasts and cancer-associated fibroblasts (CAF), prostate
cancer cells and invasive adenocarcinoma (at protein level).
Ubiquitously expressed, but is most abundant in placenta. In brain
regions, expressed as a 2.8 kb transcript in basal forebrain,
frontal cortex, thalamus, hippocampus, caudate and putamen.
{ECO:0000269|PubMed:20203690, ECO:0000269|PubMed:20551055,
ECO:0000269|PubMed:21149639, ECO:0000269|PubMed:21354433,
ECO:0000269|PubMed:21427217, ECO:0000269|PubMed:23285008}.
-!- INDUCTION: Up-regulated by EGF and TGF-alpha in endometrial,
ovarian and breast tumor cells. Up-regulated by progestin and by
phorbol 12-myristate 13-acetate (PMA) in breast cancer cell lines.
{ECO:0000269|PubMed:12027886, ECO:0000269|PubMed:19749156}.
-!- PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane
and leads to proteasome-mediated degradation.
{ECO:0000269|PubMed:21540189}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:21427217}.
-!- MISCELLANEOUS: Does not bind estradiol according to
PubMed:18566127 and PubMed:16645038.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- CAUTION: Data is conflicting regarding whether it fulfills the
criteria of a membrane-bound estrogen receptor (PubMed:15705806,
PubMed:17379646). Other reports suggest that it is not
(PubMed:16645038, PubMed:18566127). {ECO:0000305|PubMed:15705806,
ECO:0000305|PubMed:16645038, ECO:0000305|PubMed:17379646,
ECO:0000305|PubMed:18566127}.
-!- CAUTION: Data is conflicting regarding whether it is localized
either at the cell membrane (PM) (PubMed:15539556,
PubMed:21427217, PubMed:21540189, PubMed:21354433, PubMed:21149639
and PubMed:23674134). Other reports suggest that it localizes at
the endoplasmic reticulum (ER) (PubMed:15705806, PubMed:18566127).
{ECO:0000305|PubMed:15539556, ECO:0000305|PubMed:15705806,
ECO:0000305|PubMed:18566127, ECO:0000305|PubMed:21149639,
ECO:0000305|PubMed:21354433, ECO:0000305|PubMed:21427217,
ECO:0000305|PubMed:21540189, ECO:0000305|PubMed:23674134}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GPERID44344ch7p22.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Y08162; CAA69354.1; -; mRNA.
EMBL; U77827; AAC51173.1; -; Genomic_DNA.
EMBL; AF015257; AAC51904.1; -; mRNA.
EMBL; X98510; CAA67133.1; -; mRNA.
EMBL; U63917; AAB88017.1; -; mRNA.
EMBL; AF027956; AAC52027.1; -; Genomic_DNA.
EMBL; U58828; AAB02736.1; -; mRNA.
EMBL; CR541741; CAG46541.1; -; mRNA.
EMBL; AK291590; BAF84279.1; -; mRNA.
EMBL; AB451427; BAG70241.1; -; mRNA.
EMBL; CH236953; EAL23938.1; -; Genomic_DNA.
EMBL; CH471144; EAW87194.1; -; Genomic_DNA.
EMBL; BC011634; AAH11634.1; -; mRNA.
CCDS; CCDS5322.1; -.
PIR; G02670; G02670.
PIR; JC5069; JC5069.
RefSeq; NP_001035055.1; NM_001039966.1.
RefSeq; NP_001091671.1; NM_001098201.1.
RefSeq; NP_001496.1; NM_001505.2.
BioGrid; 109110; 2.
IntAct; Q99527; 1.
STRING; 9606.ENSP00000380281; -.
BindingDB; Q99527; -.
ChEMBL; CHEMBL5872; -.
GuidetoPHARMACOLOGY; 221; -.
TCDB; 9.A.14.13.19; the g-protein-coupled receptor (gpcr) family.
iPTMnet; Q99527; -.
PhosphoSitePlus; Q99527; -.
BioMuta; GPER1; -.
DMDM; 3023539; -.
PaxDb; Q99527; -.
PeptideAtlas; Q99527; -.
PRIDE; Q99527; -.
ProteomicsDB; 78311; -.
DNASU; 2852; -.
Ensembl; ENST00000297469; ENSP00000297469; ENSG00000164850.
Ensembl; ENST00000397088; ENSP00000380277; ENSG00000164850.
Ensembl; ENST00000397092; ENSP00000380281; ENSG00000164850.
Ensembl; ENST00000401670; ENSP00000385151; ENSG00000164850.
GeneID; 2852; -.
KEGG; hsa:2852; -.
UCSC; uc003sjz.1; human.
CTD; 2852; -.
DisGeNET; 2852; -.
GeneCards; GPER1; -.
HGNC; HGNC:4485; GPER1.
HPA; HPA027052; -.
MIM; 601805; gene.
neXtProt; NX_Q99527; -.
OpenTargets; ENSG00000164850; -.
PharmGKB; PA28873; -.
eggNOG; ENOG410IEGB; Eukaryota.
eggNOG; ENOG4111653; LUCA.
GeneTree; ENSGT00940000154307; -.
InParanoid; Q99527; -.
KO; K04246; -.
OMA; FCFADVK; -.
OrthoDB; 646662at2759; -.
PhylomeDB; Q99527; -.
TreeFam; TF333506; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
SIGNOR; Q99527; -.
GeneWiki; GPR30; -.
GenomeRNAi; 2852; -.
PRO; PR:Q99527; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000164850; Expressed in 154 organ(s), highest expression level in fundus of stomach.
ExpressionAtlas; Q99527; baseline and differential.
Genevisible; Q99527; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
GO; GO:0044327; C:dendritic spine head; ISS:UniProtKB.
GO; GO:0032591; C:dendritic spine membrane; ISS:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0048786; C:presynaptic active zone; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0030284; F:estrogen receptor activity; IDA:UniProtKB.
GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
GO; GO:0005496; F:steroid binding; IDA:UniProtKB.
GO; GO:1990239; F:steroid hormone binding; IDA:UniProtKB.
GO; GO:0003707; F:steroid hormone receptor activity; ISS:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030263; P:apoptotic chromosome condensation; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0071389; P:cellular response to mineralocorticoid stimulus; ISS:UniProtKB.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:AgBase.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
GO; GO:0071157; P:negative regulation of cell cycle arrest; ISS:UniProtKB.
GO; GO:0010948; P:negative regulation of cell cycle process; IMP:AgBase.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:0051053; P:negative regulation of DNA metabolic process; ISS:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:AgBase.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:AgBase.
GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
GO; GO:0002695; P:negative regulation of leukocyte activation; IDA:UniProtKB.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:AgBase.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IMP:AgBase.
GO; GO:0019228; P:neuronal action potential; ISS:UniProtKB.
GO; GO:0030264; P:nuclear fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0097755; P:positive regulation of blood vessel diameter; ISS:UniProtKB.
GO; GO:2000724; P:positive regulation of cardiac vascular smooth muscle cell differentiation; IMP:AgBase.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISS:UniProtKB.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IDA:UniProtKB.
GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO;