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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.
11-DEC-2019, entry version 180.
RecName: Full=G-protein coupled estrogen receptor 1 {ECO:0000305};
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 {ECO:0000303|PubMed:17379646, ECO:0000303|PubMed:18566127};
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 {ECO:0000312|HGNC:HGNC:4485};
Synonyms=CEPR, CMKRL2, DRY12, GPER, GPR30 {ECO:0000303|PubMed:17379646,
ECO:0000303|PubMed:18566127};
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
{ECO:0000269|PubMed:18566127}; 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
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";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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; -.
DrugBank; DB00783; Estradiol.
DrugBank; DB13952; Estradiol acetate.
DrugBank; DB13953; Estradiol benzoate.
DrugBank; DB13954; Estradiol cypionate.
DrugBank; DB13955; Estradiol dienanthate.
DrugBank; DB13956; Estradiol valerate.
DrugBank; DB01645; Genistein.
DrugBank; DB05939; MK-0354.
DrugCentral; Q99527; -.
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; -.
EuPathDB; HostDB:ENSG00000164850.14; -.
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; -.
Pharos; Q99527; Tchem.
PRO; PR:Q99527; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; Q99527; protein.
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:0005623; C:cell; IEA:GOC.
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; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IDA:UniProtKB.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0043401; P:steroid hormone mediated signaling pathway; IDA:UniProtKB.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Cell cycle; Cell junction; Cell membrane;
Cell projection; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Differentiation; Disulfide bond; Endoplasmic reticulum; Endosome;
G-protein coupled receptor; Glycoprotein; Golgi apparatus; Immunity;
Inflammatory response; Innate immunity; Membrane; Mitochondrion;
Neurogenesis; Nucleus; Polymorphism; Postsynaptic cell membrane; Receptor;
Reference proteome; Synapse; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1..375
/note="G-protein coupled estrogen receptor 1"
/id="PRO_0000069310"
TOPO_DOM 1..62
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 63..84
/note="Helical; Name=1"
/evidence="ECO:0000255"
TOPO_DOM 85..96
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 97..120
/note="Helical; Name=2"
/evidence="ECO:0000255"
TOPO_DOM 121..132
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 133..153
/note="Helical; Name=3"
/evidence="ECO:0000255"
TOPO_DOM 154..175
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 176..194
/note="Helical; Name=4"
/evidence="ECO:0000255"
TOPO_DOM 195..220
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 221..236
/note="Helical; Name=5"
/evidence="ECO:0000255"
TOPO_DOM 237..259
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 260..280
/note="Helical; Name=6"
/evidence="ECO:0000255"
TOPO_DOM 281..306
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 307..327
/note="Helical; Name=7"
/evidence="ECO:0000255"
TOPO_DOM 328..375
/note="Cytoplasmic"
/evidence="ECO:0000255"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000244|PubMed:22814378"
CARBOHYD 25
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 32
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 44
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 130..207
/evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
VARIANT 16
/note="P -> L (in dbSNP:rs11544331)"
/evidence="ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19054851"
/id="VAR_033319"
CONFLICT 20..21
/note="QP -> HA (in Ref. 6; AAC52027)"
/evidence="ECO:0000305"
CONFLICT 32..49
/note="Missing (in Ref. 7; AAB02736)"
/evidence="ECO:0000305"
CONFLICT 104
/note="A -> G (in Ref. 7; AAB02736)"
/evidence="ECO:0000305"
CONFLICT 140..146
/note="NMYSSVF -> QHVQAASS (in Ref. 7; AAB02736)"
/evidence="ECO:0000305"
CONFLICT 179
/note="G -> A (in Ref. 7; AAB02736)"
/evidence="ECO:0000305"
CONFLICT 184
/note="A -> S (in Ref. 7; AAB02736)"
/evidence="ECO:0000305"
CONFLICT 312
/note="A -> T (in Ref. 2; AAC51173)"
/evidence="ECO:0000305"
CONFLICT 320
/note="N -> T (in Ref. 7; AAB02736)"
/evidence="ECO:0000305"
CONFLICT 355
/note="A -> V (in Ref. 7; AAB02736)"
/evidence="ECO:0000305"
CONFLICT 358
/note="A -> V (in Ref. 7; AAB02736)"
/evidence="ECO:0000305"
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


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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP2118: Arrhythmogenic right ventricular cardiomyopathy
WP474: Endochondral Ossification
WP897: Androgen receptor signaling pathway
WP1004: Kit Receptor Signaling Pathway
WP1918: Signaling by Robo receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP252: Androgen Receptor Signaling Pathway
WP780: T Cell Receptor Signaling Pathway
WP1183: Toll-like receptor signaling pathway
WP566: canonical wnt - zebrafish
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1025: B Cell Receptor Signaling Pathway
WP1345: T Cell Receptor Signaling Pathway
WP590: Cardiovascular Signaling
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1367: TGF-beta Receptor Signaling Pathway
WP274: B Cell Receptor Signaling Pathway
WP809: TGF-beta Receptor Signaling Pathway
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1249: EPO Receptor Signaling
WP1869: Neuroransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell
WP996: EPO Receptor Signaling
WP1384: Toll-like receptor signaling pathway

Related Genes :
[GPER1 CEPR CMKRL2 DRY12 GPER GPR30] 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 Cmkrl2 Gper Gpr30 Gpr41] G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (G-protein coupled receptor 41) (Membrane estrogen receptor) (mER)
[Gper1 Cmkrl2 Gper Gpr30] G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (Membrane estrogen receptor) (mER)
[GPER1 GPER GPR30] G-protein coupled estrogen receptor 1 (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30)
[CCR7 CMKBR7 EBI1 EVI1] C-C chemokine receptor type 7 (C-C CKR-7) (CC-CKR-7) (CCR-7) (BLR2) (CDw197) (Epstein-Barr virus-induced G-protein coupled receptor 1) (EBI1) (EBV-induced G-protein coupled receptor 1) (MIP-3 beta receptor) (CD antigen CD197)
[Ffar2 Gpr43 Lssig] Free fatty acid receptor 2 (G-protein coupled receptor 43) (Leukocyte-specific STAT-induced GPCR)
[GPR183 EBI2] G-protein coupled receptor 183 (Epstein-Barr virus-induced G-protein coupled receptor 2) (EBI2) (EBV-induced G-protein coupled receptor 2) (hEBI2)
[F2RL1 GPR11 PAR2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) [Cleaved into: Proteinase-activated receptor 2, alternate cleaved 1; Proteinase-activated receptor 2, alternate cleaved 2]
[LTB4R BLT BLT1 BLTR CMKRL1 GPR16 P2RY7] Leukotriene B4 receptor 1 (LTB4-R 1) (LTB4-R1) (Chemoattractant receptor-like 1) (G-protein coupled receptor 16) (P2Y purinoceptor 7) (P2Y7)
[S1PR2 EDG5] Sphingosine 1-phosphate receptor 2 (S1P receptor 2) (S1P2) (Endothelial differentiation G-protein coupled receptor 5) (Sphingosine 1-phosphate receptor Edg-5) (S1P receptor Edg-5)
[Gpr183 Ebi2] G-protein coupled receptor 183 (Epstein-Barr virus-induced G-protein coupled receptor 2 homolog) (EBI2) (EBV-induced G-protein coupled receptor 2 homolog)
[F2rl1 Gpcr11 Gpr11 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1)
[ADGRA2 GPR124 KIAA1531 TEM5] Adhesion G protein-coupled receptor A2 (G-protein coupled receptor 124) (Tumor endothelial marker 5)
[PROKR2 GPR73L1 PKR2] Prokineticin receptor 2 (PK-R2) (G-protein coupled receptor 73-like 1) (G-protein coupled receptor I5E) (GPR73b) (GPRg2)
[ACKR3 CMKOR1 CXCR7 GPR159 RDC1] Atypical chemokine receptor 3 (C-X-C chemokine receptor type 7) (CXC-R7) (CXCR-7) (Chemokine orphan receptor 1) (G-protein coupled receptor 159) (G-protein coupled receptor RDC1 homolog) (RDC-1)
[ADGRG6 DREG GPR126 VIGR] Adhesion G-protein coupled receptor G6 (Developmentally regulated G-protein-coupled receptor) (G-protein coupled receptor 126) (Vascular inducible G protein-coupled receptor) [Cleaved into: ADGRG6 N-terminal fragment (ADGRG6-NTF); ADGRG6 C-terminal fragment (ADGRG6-CTF)]
[ADGRV1 GPR98 KIAA0686 KIAA1943 MASS1 VLGR1] Adhesion G-protein coupled receptor V1 (ADGRV1) (EC 3.4.-.-) (G-protein coupled receptor 98) (Monogenic audiogenic seizure susceptibility protein 1 homolog) (Usher syndrome type-2C protein) (Very large G-protein coupled receptor 1) [Cleaved into: ADGRV1 subunit alpha; ADGRV1 subunit beta]
[CXCR3 GPR9] C-X-C chemokine receptor type 3 (CXC-R3) (CXCR-3) (CKR-L2) (G protein-coupled receptor 9) (Interferon-inducible protein 10 receptor) (IP-10 receptor) (CD antigen CD183)
[ADGRG1 GPR56 TM7LN4 TM7XN1 UNQ540/PRO1083] Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) (Protein TM7XN1) [Cleaved into: ADGRG1 N-terminal fragment (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); ADGRG1 C-terminal fragment (ADGRG1 CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)]
[ADGRD1 GPR133 PGR25] Adhesion G-protein coupled receptor D1 (G-protein coupled receptor 133) (G-protein coupled receptor PGR25)
[HCAR2 GPR109A HCA2 HM74A NIACR1] Hydroxycarboxylic acid receptor 2 (G-protein coupled receptor 109A) (G-protein coupled receptor HM74A) (Niacin receptor 1) (Nicotinic acid receptor)
[Adgra2 Gpr124 Tem5] Adhesion G protein-coupled receptor A2 (G-protein coupled receptor 124) (Tumor endothelial marker 5)
[KISS1R AXOR12 GPR54] KiSS-1 receptor (KiSS-1R) (G-protein coupled receptor 54) (G-protein coupled receptor OT7T175) (hOT7T175) (Hypogonadotropin-1) (Kisspeptins receptor) (Metastin receptor)
[MRGPRX1 MRGX1 SNSR3 SNSR4] Mas-related G-protein coupled receptor member X1 (Sensory neuron-specific G-protein coupled receptor 3/4)
[Adgrg1 Cyt28 Gpr56] Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) (Serpentine receptor cyt28) [Cleaved into: ADGRG1 N-terminal fragment (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); ADGRG1 C-terminal fragment (ADGRG1-CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)]
[Kiss1r Gpr54] KiSS-1 receptor (KiSS-1R) (G-protein coupled receptor 54) (G-protein coupled receptor OT7T175) (mOT7T175) (Kisspeptins receptor) (Metastin receptor)
[Adgrg1 Gpr56] Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) [Cleaved into: ADGRG1 N-terminal fragment (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); ADGRG1 C-terminal fragment (ADGRG1 CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)]
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ADGRE2 EMR2] Adhesion G protein-coupled receptor E2 (EGF-like module receptor 2) (EGF-like module-containing mucin-like hormone receptor-like 2) (CD antigen CD312)
[ADGRG1 GPR56] Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) [Cleaved into: ADGRG1 N-terminal fragment (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); ADGRG1 C-terminal fragment (ADGRG1 CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)]

Bibliography :
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