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G-protein coupled estrogen receptor 1 (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30)

 GPER1_MACMU             Reviewed;         375 AA.
F7EQ49;
11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 1.
18-JUL-2018, entry version 52.
RecName: Full=G-protein coupled estrogen receptor 1;
AltName: Full=G protein-coupled estrogen receptor 1;
AltName: Full=G-protein coupled receptor 30;
Name=GPER1; Synonyms=GPER, GPR30;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=17431167; DOI=10.1126/science.1139247;
Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C.,
Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W.,
Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E.,
Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y.,
Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T.,
Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J.,
Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A.,
Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M.,
Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D.,
Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J.,
Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E.,
Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S.,
Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X.,
Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E.,
Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M.,
Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M.,
Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y.,
Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J.,
Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A.,
Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B.,
Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S.,
Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V.,
Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A.,
Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C.,
Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P.,
Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E.,
Zwieg A.S.;
"Evolutionary and biomedical insights from the rhesus macaque
genome.";
Science 316:222-234(2007).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19131510; DOI=10.1210/me.2008-0299;
Noel S.D., Keen K.L., Baumann D.I., Filardo E.J., Terasawa E.;
"Involvement of G protein-coupled receptor 30 (GPR30) in rapid action
of estrogen in primate LHRH neurons.";
Mol. Endocrinol. 23:349-359(2009).
-!- 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. 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 (By similarity). Increases
firing activity and intracellular calcium oscillations in
luteinizing hormone-releasing hormone (LHRH) neurons.
{ECO:0000250, ECO:0000269|PubMed:19131510}.
-!- SUBUNIT: Homodimer. Heterodimer; heterodimerizes with other G-
protein-coupled receptor (GPCRs) like CRHR1, HTR1A and PAQR8.
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. 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm,
perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle
membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Cell membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early
endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi
apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus
membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
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=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) (By
similarity). Colocalized with BSN to the active zone of
presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2
PPP1R9B in neuronal synaptosomes (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in olfactory placode and LH-
releasing hormone (LHRH) neurons (at protein level). Expressed in
hypothalamus, cerebellum, olfactory placode and uterus.
{ECO:0000269|PubMed:19131510}.
-!- PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane
and leads to proteasome-mediated degradation. {ECO:0000250}.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; CM001255; EHH17092.1; -; Genomic_DNA.
RefSeq; XP_001084531.1; XM_001084531.3.
UniGene; Mmu.24050; -.
ProteinModelPortal; F7EQ49; -.
STRING; 9544.ENSMMUP00000009453; -.
Ensembl; ENSMMUT00000070839; ENSMMUP00000049453; ENSMMUG00000007209.
GeneID; 696625; -.
KEGG; mcc:696625; -.
CTD; 2852; -.
eggNOG; ENOG410IEGB; Eukaryota.
eggNOG; ENOG4111653; LUCA.
GeneTree; ENSGT00530000063910; -.
InParanoid; F7EQ49; -.
KO; K04246; -.
OMA; QHARLSC; -.
OrthoDB; EOG091G09A2; -.
TreeFam; TF333506; -.
Proteomes; UP000006718; Chromosome 3.
Bgee; ENSMMUG00000007209; -.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS: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; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005622; C:intracellular; ISS:UniProtKB.
GO; GO:0045095; C:keratin filament; ISS:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0048786; C:presynaptic active zone; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0030284; F:estrogen receptor activity; ISS:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; IBA:GO_Central.
GO; GO:0017082; F:mineralocorticoid receptor activity; ISS:UniProtKB.
GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS: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:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
GO; GO:0071157; P:negative regulation of cell cycle arrest; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0051053; P:negative regulation of DNA metabolic process; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0002695; P:negative regulation of leukocyte activation; ISS:UniProtKB.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0019228; P:neuronal action potential; IDA: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:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS: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; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS: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 protein signaling pathway; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISS: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; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS: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; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISS: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; Complete proteome; 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; Postsynaptic cell membrane;
Receptor; Reference proteome; Synapse; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 375 G-protein coupled estrogen receptor 1.
/FTId=PRO_0000424543.
TOPO_DOM 1 66 Extracellular. {ECO:0000255}.
TRANSMEM 67 87 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 88 96 Cytoplasmic. {ECO:0000255}.
TRANSMEM 97 117 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 118 127 Extracellular. {ECO:0000255}.
TRANSMEM 128 148 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 149 175 Cytoplasmic. {ECO:0000255}.
TRANSMEM 176 196 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 197 217 Extracellular. {ECO:0000255}.
TRANSMEM 218 238 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 239 260 Cytoplasmic. {ECO:0000255}.
TRANSMEM 261 281 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 282 307 Extracellular. {ECO:0000255}.
TRANSMEM 308 328 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 329 375 Cytoplasmic. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q99527}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 32 32 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 130 207 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 375 AA; 42326 MW; 400DA0A3AD7CFA02 CRC64;
MEVTSQARGM GLEMYPGTMQ PAAPNTTSPE LNLSHPLLGA SLANGTGELS EHQQYVIGLF
LSCLYTIFLF PIGFVGNILI LVVNISFREK MTIPDLYFIN LAVADLILVA DSLIEVFNLH
EQYYDIAVLC TFMSLFLQVN MYSSVFFLTW MSFDRYIALA RAMRCSLFRT KHHARLSCGL
IWMASVSATL VPFTAVHLQH TDEACFCFAD VREVQWLEVT LGFIVPFAII GLCYSLIVRV
LVRAHRHRGL RPRRQKALRM ILAVVLVFFV CWLPENVFIS VHLLQRTQPG AAPCKQSFRH
AHPLTGHIVN LAAFSNSCLN PLIYSFLGET FREKLRLYIE QKTNLPALNR FCHAALKAVI
PDSTEQSDVR FSSAV


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