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Q8BMP4

- GPER1_MOUSE

UniProt

Q8BMP4 - GPER1_MOUSE

Protein

G-protein coupled estrogen receptor 1

Gene

Gper1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.11 Publications

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. estrogen receptor activity Source: UniProtKB
    3. G-protein coupled receptor activity Source: UniProtKB-KW
    4. mineralocorticoid receptor activity Source: UniProtKB
    5. steroid binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic chromosome condensation Source: UniProtKB
    2. cell cycle Source: UniProtKB-KW
    3. cellular response to estradiol stimulus Source: UniProtKB
    4. cellular response to glucose stimulus Source: UniProtKB
    5. cellular response to mineralocorticoid stimulus Source: UniProtKB
    6. cellular response to peptide hormone stimulus Source: UniProtKB
    7. cellular response to tumor necrosis factor Source: UniProtKB
    8. cytosolic calcium ion homeostasis Source: UniProtKB
    9. inflammatory response Source: UniProtKB-KW
    10. innate immune response Source: UniProtKB-KW
    11. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
    12. mineralocorticoid receptor signaling pathway Source: GOC
    13. negative regulation of cell cycle arrest Source: UniProtKB
    14. negative regulation of cell proliferation Source: UniProtKB
    15. negative regulation of DNA metabolic process Source: UniProtKB
    16. negative regulation of fat cell differentiation Source: UniProtKB
    17. negative regulation of gene expression Source: UniProtKB
    18. negative regulation of inflammatory response Source: UniProtKB
    19. negative regulation of leukocyte activation Source: UniProtKB
    20. negative regulation of lipid biosynthetic process Source: UniProtKB
    21. neuronal action potential Source: UniProtKB
    22. nuclear fragmentation involved in apoptotic nuclear change Source: UniProtKB
    23. positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: UniProtKB
    24. positive regulation of apoptotic process Source: UniProtKB
    25. positive regulation of cAMP biosynthetic process Source: UniProtKB
    26. positive regulation of cell migration Source: UniProtKB
    27. positive regulation of cell proliferation Source: UniProtKB
    28. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    29. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    30. positive regulation of endothelial cell apoptotic process Source: UniProtKB
    31. positive regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    32. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    33. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
    34. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    35. positive regulation of gene expression Source: UniProtKB
    36. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    37. positive regulation of inositol trisphosphate biosynthetic process Source: UniProtKB
    38. positive regulation of insulin secretion Source: UniProtKB
    39. positive regulation of MAPK cascade Source: UniProtKB
    40. positive regulation of neurogenesis Source: UniProtKB
    41. positive regulation of neurotransmitter secretion Source: UniProtKB
    42. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    43. positive regulation of protein phosphorylation Source: UniProtKB
    44. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
    45. positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
    46. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    47. positive regulation of uterine smooth muscle contraction Source: UniProtKB
    48. positive regulation of vasodilation Source: UniProtKB
    49. steroid hormone mediated signaling pathway Source: GOC

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Apoptosis, Cell cycle, Differentiation, Immunity, Inflammatory response, Innate immunity, Neurogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Gper1
    Synonyms:Cmkrl2, Gper, Gpr30
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1924104. Gper1.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm. Cytoplasmperinuclear region By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity. Golgi apparatus membrane By similarity; Multi-pass membrane protein By similarity. Cell projectiondendrite By similarity. Cytoplasmic vesicle membrane By similarity; Multi-pass membrane protein By similarity. Early endosome By similarity. Recycling endosome By similarity. Golgi apparatustrans-Golgi network By similarity. Cell projectiondendritic spine membrane By similarity; Multi-pass membrane protein By similarity. Cell projectionaxon By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Mitochondrion membrane By similarity; 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.By similarity

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. axon terminus Source: UniProtKB
    3. cell junction Source: UniProtKB-KW
    4. cytoplasm Source: UniProtKB
    5. cytoplasmic vesicle membrane Source: UniProtKB
    6. dendrite Source: UniProtKB
    7. dendritic shaft Source: UniProtKB
    8. dendritic spine head Source: UniProtKB
    9. dendritic spine membrane Source: UniProtKB
    10. early endosome Source: UniProtKB
    11. endoplasmic reticulum Source: UniProtKB
    12. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    13. Golgi apparatus Source: UniProtKB
    14. Golgi membrane Source: UniProtKB-SubCell
    15. integral component of membrane Source: UniProtKB-KW
    16. intracellular Source: UniProtKB
    17. keratin filament Source: UniProtKB
    18. mitochondrial membrane Source: UniProtKB
    19. neuronal postsynaptic density Source: UniProtKB
    20. nuclear envelope Source: UniProtKB
    21. nucleus Source: UniProtKB
    22. perinuclear region of cytoplasm Source: UniProtKB
    23. plasma membrane Source: UniProtKB
    24. postsynaptic density Source: UniProtKB
    25. postsynaptic membrane Source: UniProtKB-KW
    26. presynaptic active zone Source: UniProtKB
    27. presynaptic membrane Source: UniProtKB
    28. recycling endosome Source: UniProtKB
    29. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Mitochondrion, Nucleus, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Disruption phenotypei

    Strong variations in phenotypes, probably depending on the distinct targeting strategies, genetic background and experimental conditions used in the different experiments. According to PubMed:18063692, 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 PubMed:20734455, male mice display increased body size, femur length, bone mass and cell proliferative activity within the growth plate. According to PubMed:18845638, 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 PubMed:19179659 mice show increased body weight, visceral adiposity, vascular tone and blood pressure. No visible phenotype according to PubMed:18799753.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi375 – 3751V → A: Loss of interaction with DLG4. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375G-protein coupled estrogen receptor 1PRO_0000069311Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi130 ↔ 207PROSITE-ProRule annotation

    Post-translational modificationi

    Ubiquitinated; ubiquitination occurs at the plasma membrane and leads to proteasome-mediated degradation.By similarity
    N-glycosylated.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ8BMP4.

    Expressioni

    Tissue specificityi

    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.6 Publications

    Inductioni

    Up-regulated during adipogenesis.1 Publication

    Gene expression databases

    BgeeiQ8BMP4.
    CleanExiMM_GPER.
    GenevestigatoriQ8BMP4.

    Interactioni

    Subunit structurei

    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.By similarity1 PublicationCurated

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BMP4.
    SMRiQ8BMP4. Positions 57-336.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6262ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini85 – 9612CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini121 – 13212ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini154 – 17522CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini195 – 22026ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini237 – 25923CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini281 – 30626ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini328 – 37548CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei63 – 8422Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei97 – 12024Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei133 – 15321Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei176 – 19419Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei221 – 23616Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei260 – 28021Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei307 – 32721Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG151076.
    GeneTreeiENSGT00530000063910.
    HOGENOMiHOG000013114.
    HOVERGENiHBG005351.
    InParanoidiB2RRW0.
    KOiK04246.
    OMAiQHARLSC.
    OrthoDBiEOG7WX08J.
    TreeFamiTF333506.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BMP4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDATTPAQTV GVEIYLGPVW PAPSNSTPLA LNLSLALRED APGNLTGDLS    50
    EHQQYVIALF LSCLYTIFLF PIGFVGNILI LVVNISFREK MTIPDLYFIN 100
    LAAADLILVA DSLIEVFNLD EQYYDIAVLC TFMSLFLQIN MYSSVFFLTW 150
    MSFDRYLALA KAMRCGLFRT KHHARLSCGL IWMASVSATL VPFTAVHLRH 200
    TEEACFCFAD VREVQWLEVT LGFIMPFAII GLCYSLIVRA LIRAHRHRGL 250
    RPRRQKALRM IFAVVLVFFI CWLPENVFIS VHLLQWTQPG DTPCKQSFRH 300
    AYPLTGHIVN LAAFSNSCLN PLIYSFLGET FRDKLRLYVE QKTSLPALNR 350
    FCHATLKAVI PDSTEQSEVR FSSAV 375
    Length:375
    Mass (Da):42,479
    Last modified:July 27, 2011 - v2
    Checksum:iAF7E4795C3A9A405
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti314 – 3141F → I in BAC26930. (PubMed:16141072)Curated
    Sequence conflicti369 – 3691V → I in BAB31118. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS19811.1.
    RefSeqiNP_084047.2. NM_029771.3.
    XP_006504820.1. XM_006504757.1.
    UniGeneiMm.389706.

    Genome annotation databases

    EnsembliENSMUST00000066211; ENSMUSP00000080370; ENSMUSG00000053647.
    GeneIDi76854.
    KEGGimmu:76854.
    UCSCiuc009agr.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS19811.1.
    RefSeqi NP_084047.2. NM_029771.3.
    XP_006504820.1. XM_006504757.1.
    UniGenei Mm.389706.

    3D structure databases

    ProteinModelPortali Q8BMP4.
    SMRi Q8BMP4. Positions 57-336.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    GuidetoPHARMACOLOGYi 221.

    Protein family/group databases

    GPCRDBi Search...

    Proteomic databases

    PRIDEi Q8BMP4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000066211 ; ENSMUSP00000080370 ; ENSMUSG00000053647 .
    GeneIDi 76854.
    KEGGi mmu:76854.
    UCSCi uc009agr.2. mouse.

    Organism-specific databases

    CTDi 2852.
    MGIi MGI:1924104. Gper1.

    Phylogenomic databases

    eggNOGi NOG151076.
    GeneTreei ENSGT00530000063910.
    HOGENOMi HOG000013114.
    HOVERGENi HBG005351.
    InParanoidi B2RRW0.
    KOi K04246.
    OMAi QHARLSC.
    OrthoDBi EOG7WX08J.
    TreeFami TF333506.

    Miscellaneous databases

    NextBioi 345931.
    PROi Q8BMP4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BMP4.
    CleanExi MM_GPER.
    Genevestigatori Q8BMP4.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    4. Cited for: ABSENCE OF ESTROGEN-BINDING, DISRUPTION PHENOTYPE.
    5. 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. 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.

    Entry informationi

    Entry nameiGPER1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BMP4
    Secondary accession number(s): B2RRW0, Q9D392
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3