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Q8BMP4 (GPER1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G-protein coupled estrogen receptor 1
Alternative name(s):
Chemoattractant receptor-like 2
G protein-coupled estrogen receptor 1
G-protein coupled receptor 30
Membrane estrogen receptor
Short name=mER
Gene names
Name:Gper1
Synonyms:Cmkrl2, Gper, Gpr30
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.17 Ref.18

Subunit structure

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. Homodimer Probable. Heterodimer; heterodimerizes with other G-protein-coupled receptor (GPCRs) like CRHR1, HTR1A and PAQR8. Ref.16

Subcellular location

Nucleus By similarity. Cytoplasm. Cytoplasmperinuclear region By similarity. Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Golgi apparatus membrane; Multi-pass membrane protein By similarity. Cell projectiondendrite By similarity. Cytoplasmic vesicle membrane; Multi-pass membrane protein By similarity. Early endosome By similarity. Recycling endosome By similarity. Golgi apparatustrans-Golgi network By similarity. Cell projectiondendritic spine membrane; Multi-pass membrane protein By similarity. Cell projectionaxon By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Mitochondrion membrane; Multi-pass membrane protein By similarity. Note: Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes. 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. Ref.7 Ref.12 Ref.13 Ref.15 Ref.17

Tissue specificity

Expressed in brain, heart, spleen, preadipocytes, mature adipocytes and primary hippocampal neurons. Expressed in neurons of the hippocampus, hypothalamic paraventricular nucleus (PVH), supraoptic nucleus (SON) and the median eminence. Expressed in the nucleus ambiguous (at protein level). Expressed in brain, pituitary gland, adrenal medulla, renal pelvis, ovary, endothelial cells, visceral fat tissues and islets of Langerhans. Ref.7 Ref.11 Ref.14 Ref.15 Ref.17 Ref.18

Induction

Up-regulated during adipogenesis. Ref.15

Post-translational modification

Ubiquitinated; ubiquitination occurs at the plasma membrane and leads to proteasome-mediated degradation By similarity.

N-glycosylated. Ref.12

Disruption phenotype

Strong variations in phenotypes, probably depending on the distinct targeting strategies, genetic background and experimental conditions used in the different experiments. According to Ref.3, mice are viable and fertile and do not display any gross physical, immunological, reproductive and neurological abnormalities, but show 17-beta-estradiol (E2)-induced alleviated thymic atrophy. According to Ref.10, male mice display increased body size, femur length, bone mass and cell proliferative activity within the growth plate. According to Ref.6, female mice, but not male, show reduced body weight and skeletal growth, hyperglycemia, impaired glucose tolerance with reduced glucose-stimulated insulin release and increased blood pressure. According to Ref.5 mice show increased body weight, visceral adiposity, vascular tone and blood pressure. No visible phenotype according to Ref.4. Ref.3 Ref.4 Ref.5 Ref.6 Ref.10

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Differentiation
Immunity
Inflammatory response
Innate immunity
Neurogenesis
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
Mitochondrion
Nucleus
Postsynaptic cell membrane
Synapse
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMAcetylation
Disulfide bond
Glycoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic chromosome condensation

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to estradiol stimulus

Inferred from direct assay Ref.12Ref.9Ref.18Ref.15. Source: UniProtKB

cellular response to glucose stimulus

Inferred from direct assay Ref.9. Source: UniProtKB

cellular response to mineralocorticoid stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to peptide hormone stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to tumor necrosis factor

Inferred from sequence or structural similarity. Source: UniProtKB

cytosolic calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular steroid hormone receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

mineralocorticoid receptor signaling pathway

Inferred from sequence or structural similarity. Source: GOC

negative regulation of DNA metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell cycle arrest

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fat cell differentiation

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of leukocyte activation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of lipid biosynthetic process

Inferred from direct assay Ref.15. Source: UniProtKB

neuronal action potential

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear fragmentation involved in apoptotic nuclear change

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.9Ref.18. Source: UniProtKB

positive regulation of G-protein coupled receptor protein signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP biosynthetic process

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of endothelial cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epidermal growth factor receptor signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of establishment of protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of inositol trisphosphate biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin secretion

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of neurogenesis

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of neurotransmitter secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from direct assay Ref.9Ref.18Ref.15. Source: UniProtKB

positive regulation of release of cytochrome c from mitochondria

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of uterine smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vasodilation

Inferred from sequence or structural similarity. Source: UniProtKB

steroid hormone mediated signaling pathway

Inferred from direct assay Ref.18. Source: GOC

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

axon

Inferred from sequence or structural similarity. Source: UniProtKB

axon terminus

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.12Ref.15. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic shaft

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine head

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine membrane

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular

Inferred from direct assay Ref.9. Source: UniProtKB

keratin filament

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear envelope

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.12Ref.17. Source: UniProtKB

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

presynaptic active zone

Inferred from sequence or structural similarity. Source: UniProtKB

presynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome

Inferred from sequence or structural similarity. Source: UniProtKB

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionG-protein coupled receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from electronic annotation. Source: Ensembl

estrogen receptor activity

Inferred from direct assay Ref.18. Source: UniProtKB

mineralocorticoid receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

steroid binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375G-protein coupled estrogen receptor 1
PRO_0000069311

Regions

Topological domain1 – 6262Extracellular Potential
Transmembrane63 – 8422Helical; Name=1; Potential
Topological domain85 – 9612Cytoplasmic Potential
Transmembrane97 – 12024Helical; Name=2; Potential
Topological domain121 – 13212Extracellular Potential
Transmembrane133 – 15321Helical; Name=3; Potential
Topological domain154 – 17522Cytoplasmic Potential
Transmembrane176 – 19419Helical; Name=4; Potential
Topological domain195 – 22026Extracellular Potential
Transmembrane221 – 23616Helical; Name=5; Potential
Topological domain237 – 25923Cytoplasmic Potential
Transmembrane260 – 28021Helical; Name=6; Potential
Topological domain281 – 30626Extracellular Potential
Transmembrane307 – 32721Helical; Name=7; Potential
Topological domain328 – 37548Cytoplasmic Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Glycosylation321N-linked (GlcNAc...) Potential
Glycosylation441N-linked (GlcNAc...) Potential
Disulfide bond130 ↔ 207 Potential

Experimental info

Mutagenesis3751V → A: Loss of interaction with DLG4. Ref.16
Sequence conflict3141F → I in BAC26930. Ref.1
Sequence conflict3691V → I in BAB31118. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BMP4 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: AF7E4795C3A9A405

FASTA37542,479
        10         20         30         40         50         60 
MDATTPAQTV GVEIYLGPVW PAPSNSTPLA LNLSLALRED APGNLTGDLS EHQQYVIALF 

        70         80         90        100        110        120 
LSCLYTIFLF PIGFVGNILI LVVNISFREK MTIPDLYFIN LAAADLILVA DSLIEVFNLD 

       130        140        150        160        170        180 
EQYYDIAVLC TFMSLFLQIN MYSSVFFLTW MSFDRYLALA KAMRCGLFRT KHHARLSCGL 

       190        200        210        220        230        240 
IWMASVSATL VPFTAVHLRH TEEACFCFAD VREVQWLEVT LGFIMPFAII GLCYSLIVRA 

       250        260        270        280        290        300 
LIRAHRHRGL RPRRQKALRM IFAVVLVFFI CWLPENVFIS VHLLQWTQPG DTPCKQSFRH 

       310        320        330        340        350        360 
AYPLTGHIVN LAAFSNSCLN PLIYSFLGET FRDKLRLYVE QKTSLPALNR FCHATLKAVI 

       370 
PDSTEQSEVR FSSAV 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Medulla oblongata and Pituitary.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"GPR30 contributes to estrogen-induced thymic atrophy."
Wang C., Dehghani B., Magrisso I.J., Rick E.A., Bonhomme E., Cody D.B., Elenich L.A., Subramanian S., Murphy S.J., Kelly M.J., Rosenbaum J.S., Vandenbark A.A., Offner H.
Mol. Endocrinol. 22:636-648(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]"GPR30 does not mediate estrogenic responses in reproductive organs in mice."
Otto C., Fuchs I., Kauselmann G., Kern H., Zevnik B., Andreasen P., Schwarz G., Altmann H., Klewer M., Schoor M., Vonk R., Fritzemeier K.H.
Biol. Reprod. 80:34-41(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ABSENCE OF ESTROGEN-BINDING, DISRUPTION PHENOTYPE.
[5]"Regulatory role of G protein-coupled estrogen receptor for vascular function and obesity."
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.
Circ. Res. 104:288-291(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Deletion of the G protein-coupled receptor 30 impairs glucose tolerance, reduces bone growth, increases blood pressure, and eliminates estradiol-stimulated insulin release in female mice."
Martensson U.E., Salehi S.A., Windahl S., Gomez M.F., Sward K., Daszkiewicz-Nilsson J., Wendt A., Andersson N., Hellstrand P., Grande P.O., Owman C., Rosen C.J., Adamo M.L., Lundquist I., Rorsman P., Nilsson B.O., Ohlsson C., Olde B., Leeb-Lundberg L.M.
Endocrinology 150:687-698(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"Localisation of GPR30, a novel G protein-coupled oestrogen receptor, suggests multiple functions in rodent brain and peripheral tissues."
Hazell G.G., Yao S.T., Roper J.A., Prossnitz E.R., O'Carroll A.M., Lolait S.J.
J. Endocrinol. 202:223-236(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"In vivo effects of a GPR30 antagonist."
Dennis M.K., Burai R., Ramesh C., Petrie W.K., Alcon S.N., Nayak T.K., Bologa C.G., Leitao A., Brailoiu E., Deliu E., Dun N.J., Sklar L.A., Hathaway H.J., Arterburn J.B., Oprea T.I., Prossnitz E.R.
Nat. Chem. Biol. 5:421-427(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Mechanisms of estradiol-induced insulin secretion by the G protein-coupled estrogen receptor GPR30/GPER in pancreatic beta-cells."
Sharma G., Prossnitz E.R.
Endocrinology 152:3030-3039(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"GPR30 deficiency causes increased bone mass, mineralization, and growth plate proliferative activity in male mice."
Ford J., Hajibeigi A., Long M., Hahner L., Gore C., Hsieh J.T., Clegg D., Zerwekh J., Oz O.K.
J. Bone Miner. Res. 26:298-307(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]"The GPER1 agonist G-1 attenuates endothelial cell proliferation by inhibiting DNA synthesis and accumulating cells in the S and G2 phases of the cell cycle."
Holm A., Baldetorp B., Olde B., Leeb-Lundberg L.M., Nilsson B.O.
J. Vasc. Res. 48:327-335(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"G protein-coupled estrogen receptor 1/G protein-coupled receptor 30 localizes in the plasma membrane and traffics intracellularly on cytokeratin intermediate filaments."
Sanden C., Broselid S., Cornmark L., Andersson K., Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.
Mol. Pharmacol. 79:400-410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
[13]"G-protein-coupled receptor 30 mediates rapid neuroprotective effects of estrogen via depression of NR2B-containing NMDA receptors."
Liu S.B., Zhang N., Guo Y.Y., Zhao R., Shi T.Y., Feng S.F., Wang S.Q., Yang Q., Li X.Q., Wu Y.M., Ma L., Hou Y., Xiong L.Z., Zhang W., Zhao M.G.
J. Neurosci. 32:4887-4900(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"Role of ERbeta and GPR30 in the endocrine pancreas: A matter of estrogen dose."
Ropero A.B., Pang Y., Alonso-Magdalena P., Thomas P., Nadal A.
Steroids 77:951-958(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[15]"GPER mediates the inhibitory actions of estrogen on adipogenesis in 3T3-L1 cells through perturbation of mitotic clonal expansion."
Zhu P., Yuen J.M., Sham K.W., Cheng C.H.
Gen. Comp. Endocrinol. 193:19-26(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[16]"Post-synaptic density-95 (PSD-95) binding capacity of G-protein-coupled receptor 30 (GPR30), an estrogen receptor that can be identified in hippocampal dendritic spines."
Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.
J. Biol. Chem. 288:6438-6450(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF VAL-375.
[17]"G-protein-coupled receptor 30 interacts with receptor activity-modifying protein 3 and confers sex-dependent cardioprotection."
Lenhart P.M., Broselid S., Barrick C.J., Leeb-Lundberg L.M., Caron K.M.
J. Mol. Endocrinol. 51:191-202(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[18]"G protein-coupled estrogen receptor is required for the neuritogenic mechanism of 17beta-estradiol in developing hippocampal neurons."
Ruiz-Palmero I., Hernando M., Garcia-Segura L.M., Arevalo M.A.
Mol. Cell. Endocrinol. 372:105-115(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[19]"A critical review of fundamental controversies in the field of GPR30 research."
Langer G., Bader B., Meoli L., Isensee J., Delbeck M., Noppinger P.R., Otto C.
Steroids 75:603-610(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK018203 mRNA. Translation: BAB31118.1.
AK030375 mRNA. Translation: BAC26930.1.
CH466529 Genomic DNA. Translation: EDL19153.1.
BC138598 mRNA. Translation: AAI38599.1.
BC138616 mRNA. Translation: AAI38617.1.
RefSeqNP_084047.2. NM_029771.3.
XP_006504820.1. XM_006504757.1.
UniGeneMm.389706.

3D structure databases

ProteinModelPortalQ8BMP4.
SMRQ8BMP4. Positions 40-342.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY221.

Protein family/group databases

GPCRDBSearch...

Proteomic databases

PRIDEQ8BMP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066211; ENSMUSP00000080370; ENSMUSG00000053647.
GeneID76854.
KEGGmmu:76854.
UCSCuc009agr.2. mouse.

Organism-specific databases

CTD2852.
MGIMGI:1924104. Gper1.

Phylogenomic databases

eggNOGNOG151076.
GeneTreeENSGT00530000063910.
HOGENOMHOG000013114.
HOVERGENHBG005351.
InParanoidB2RRW0.
KOK04246.
OMAQHARLSC.
OrthoDBEOG7WX08J.
TreeFamTF333506.

Gene expression databases

BgeeQ8BMP4.
CleanExMM_GPER.
GenevestigatorQ8BMP4.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio345931.
PROQ8BMP4.
SOURCESearch...

Entry information

Entry nameGPER1_MOUSE
AccessionPrimary (citable) accession number: Q8BMP4
Secondary accession number(s): B2RRW0, Q9D392
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries