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Q99527

- GPER1_HUMAN

UniProt

Q99527 - GPER1_HUMAN

Protein

G-protein coupled estrogen receptor 1

Gene

GPER1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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.14 Publications

    Kineticsi

    1. KM=3.3 mM for 17-beta-estradiol3 Publications
    2. KM=6.6 mM for 17-beta-estradiol3 Publications
    3. KM=3.3 mM for 17-beta-estradiol3 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. estrogen receptor activity Source: UniProtKB
    3. G-protein coupled receptor activity Source: ProtInc
    4. mineralocorticoid receptor activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. 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. G-protein coupled receptor signaling pathway Source: ProtInc
    10. inflammatory response Source: UniProtKB-KW
    11. innate immune response Source: UniProtKB-KW
    12. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
    13. mineralocorticoid receptor signaling pathway Source: GOC
    14. negative regulation of cell cycle arrest Source: UniProtKB
    15. negative regulation of cell proliferation Source: UniProtKB
    16. negative regulation of DNA metabolic process Source: UniProtKB
    17. negative regulation of fat cell differentiation Source: UniProtKB
    18. negative regulation of gene expression Source: UniProtKB
    19. negative regulation of inflammatory response Source: UniProtKB
    20. negative regulation of leukocyte activation Source: UniProtKB
    21. negative regulation of lipid biosynthetic process Source: UniProtKB
    22. neuronal action potential Source: UniProtKB
    23. nuclear fragmentation involved in apoptotic nuclear change Source: UniProtKB
    24. positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: UniProtKB
    25. positive regulation of apoptotic process Source: UniProtKB
    26. positive regulation of cAMP biosynthetic process Source: UniProtKB
    27. positive regulation of cell migration Source: UniProtKB
    28. positive regulation of cell proliferation Source: UniProtKB
    29. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    30. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    31. positive regulation of endothelial cell apoptotic process Source: UniProtKB
    32. positive regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    33. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    34. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
    35. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    36. positive regulation of gene expression Source: UniProtKB
    37. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    38. positive regulation of inositol trisphosphate biosynthetic process Source: UniProtKB
    39. positive regulation of insulin secretion Source: UniProtKB
    40. positive regulation of MAPK cascade Source: UniProtKB
    41. positive regulation of neurogenesis Source: UniProtKB
    42. positive regulation of neurotransmitter secretion Source: UniProtKB
    43. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    44. positive regulation of protein phosphorylation Source: UniProtKB
    45. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
    46. positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
    47. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    48. positive regulation of uterine smooth muscle contraction Source: UniProtKB
    49. positive regulation of vasodilation Source: UniProtKB
    50. 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

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G-protein coupled estrogen receptor 1
    Alternative name(s):
    Chemoattractant receptor-like 2
    Flow-induced endothelial G-protein coupled receptor 1
    Short name:
    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
    Short name:
    LYGPR
    Membrane estrogen receptor
    Short name:
    mER
    Gene namesi
    Name:GPER1
    Synonyms:CEPR, CMKRL2, DRY12, GPER, GPR30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:4485. GPER1.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity. Cytoplasmperinuclear region. Cytoplasmcytoskeleton. 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 By similarity; Multi-pass membrane protein By similarity. Golgi apparatustrans-Golgi network. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell projectiondendrite 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 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).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 plasma membrane Source: ProtInc
    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. presynaptic active zone Source: UniProtKB
    26. presynaptic membrane Source: UniProtKB
    27. recycling endosome Source: UniProtKB
    28. 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

    Organism-specific databases

    PharmGKBiPA28873.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375G-protein coupled estrogen receptor 1PRO_0000069310Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
    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.1 Publication
    Glycosylated.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ99527.
    PaxDbiQ99527.
    PRIDEiQ99527.

    Expressioni

    Tissue specificityi

    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.6 Publications

    Inductioni

    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.2 Publications

    Gene expression databases

    ArrayExpressiQ99527.
    BgeeiQ99527.
    CleanExiHS_GPER.
    GenevestigatoriQ99527.

    Organism-specific databases

    HPAiHPA027052.

    Interactioni

    Subunit structurei

    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.By similarity4 PublicationsCurated

    Protein-protein interaction databases

    IntActiQ99527. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99527.
    SMRiQ99527. Positions 19-338.
    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.
    HOVERGENiHBG005351.
    KOiK04246.
    OMAiQHARLSC.
    OrthoDBiEOG7WX08J.
    PhylomeDBiQ99527.
    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.

    Q99527-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVTSQARGV GLEMYPGTAQ PAAPNTTSPE LNLSHPLLGT ALANGTGELS    50
    EHQQYVIGLF LSCLYTIFLF PIGFVGNILI LVVNISFREK MTIPDLYFIN 100
    LAVADLILVA DSLIEVFNLH ERYYDIAVLC TFMSLFLQVN MYSSVFFLTW 150
    MSFDRYIALA RAMRCSLFRT KHHARLSCGL IWMASVSATL VPFTAVHLQH 200
    TDEACFCFAD VREVQWLEVT LGFIVPFAII GLCYSLIVRV LVRAHRHRGL 250
    RPRRQKALRM ILAVVLVFFV CWLPENVFIS VHLLQRTQPG AAPCKQSFRH 300
    AHPLTGHIVN LAAFSNSCLN PLIYSFLGET FRDKLRLYIE QKTNLPALNR 350
    FCHAALKAVI PDSTEQSDVR FSSAV 375
    Length:375
    Mass (Da):42,248
    Last modified:May 1, 1997 - v1
    Checksum:i0A54EED8A698F075
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 212QP → HA in AAC52027. (PubMed:9479505)Curated
    Sequence conflicti32 – 4918Missing in AAB02736. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti104 – 1041A → G in AAB02736. 1 PublicationCurated
    Sequence conflicti140 – 1467NMYSSVF → QHVQAASS in AAB02736. 1 PublicationCurated
    Sequence conflicti179 – 1791G → A in AAB02736. 1 PublicationCurated
    Sequence conflicti184 – 1841A → S in AAB02736. 1 PublicationCurated
    Sequence conflicti312 – 3121A → T in AAC51173. (PubMed:9070864)Curated
    Sequence conflicti320 – 3201N → T in AAB02736. 1 PublicationCurated
    Sequence conflicti355 – 3551A → V in AAB02736. 1 PublicationCurated
    Sequence conflicti358 – 3581A → V in AAB02736. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161P → L.2 Publications
    Corresponds to variant rs11544331 [ dbSNP | Ensembl ].
    VAR_033319

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08162 mRNA. Translation: CAA69354.1.
    U77827 Genomic DNA. Translation: AAC51173.1.
    AF015257 mRNA. Translation: AAC51904.1.
    X98510 mRNA. Translation: CAA67133.1.
    U63917 mRNA. Translation: AAB88017.1.
    AF027956 Genomic DNA. Translation: AAC52027.1.
    U58828 mRNA. Translation: AAB02736.1.
    CR541741 mRNA. Translation: CAG46541.1.
    AK291590 mRNA. Translation: BAF84279.1.
    AB451427 mRNA. Translation: BAG70241.1.
    CH236953 Genomic DNA. Translation: EAL23938.1.
    CH471144 Genomic DNA. Translation: EAW87194.1.
    BC011634 mRNA. Translation: AAH11634.1.
    CCDSiCCDS5322.1.
    PIRiG02670.
    JC5069.
    RefSeqiNP_001035055.1. NM_001039966.1.
    NP_001091671.1. NM_001098201.1.
    NP_001496.1. NM_001505.2.
    UniGeneiHs.20961.

    Genome annotation databases

    EnsembliENST00000297469; ENSP00000297469; ENSG00000164850.
    ENST00000397088; ENSP00000380277; ENSG00000164850.
    ENST00000397092; ENSP00000380281; ENSG00000164850.
    ENST00000401670; ENSP00000385151; ENSG00000164850.
    GeneIDi2852.
    KEGGihsa:2852.
    UCSCiuc003sjz.1. human.

    Polymorphism databases

    DMDMi3023539.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08162 mRNA. Translation: CAA69354.1 .
    U77827 Genomic DNA. Translation: AAC51173.1 .
    AF015257 mRNA. Translation: AAC51904.1 .
    X98510 mRNA. Translation: CAA67133.1 .
    U63917 mRNA. Translation: AAB88017.1 .
    AF027956 Genomic DNA. Translation: AAC52027.1 .
    U58828 mRNA. Translation: AAB02736.1 .
    CR541741 mRNA. Translation: CAG46541.1 .
    AK291590 mRNA. Translation: BAF84279.1 .
    AB451427 mRNA. Translation: BAG70241.1 .
    CH236953 Genomic DNA. Translation: EAL23938.1 .
    CH471144 Genomic DNA. Translation: EAW87194.1 .
    BC011634 mRNA. Translation: AAH11634.1 .
    CCDSi CCDS5322.1.
    PIRi G02670.
    JC5069.
    RefSeqi NP_001035055.1. NM_001039966.1.
    NP_001091671.1. NM_001098201.1.
    NP_001496.1. NM_001505.2.
    UniGenei Hs.20961.

    3D structure databases

    ProteinModelPortali Q99527.
    SMRi Q99527. Positions 19-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99527. 1 interaction.

    Chemistry

    BindingDBi Q99527.
    ChEMBLi CHEMBL5872.
    GuidetoPHARMACOLOGYi 221.

    Protein family/group databases

    GPCRDBi Search...

    Polymorphism databases

    DMDMi 3023539.

    Proteomic databases

    MaxQBi Q99527.
    PaxDbi Q99527.
    PRIDEi Q99527.

    Protocols and materials databases

    DNASUi 2852.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297469 ; ENSP00000297469 ; ENSG00000164850 .
    ENST00000397088 ; ENSP00000380277 ; ENSG00000164850 .
    ENST00000397092 ; ENSP00000380281 ; ENSG00000164850 .
    ENST00000401670 ; ENSP00000385151 ; ENSG00000164850 .
    GeneIDi 2852.
    KEGGi hsa:2852.
    UCSCi uc003sjz.1. human.

    Organism-specific databases

    CTDi 2852.
    GeneCardsi GC07P001122.
    H-InvDB HIX0167652.
    HGNCi HGNC:4485. GPER1.
    HPAi HPA027052.
    MIMi 601805. gene.
    neXtProti NX_Q99527.
    PharmGKBi PA28873.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG151076.
    HOVERGENi HBG005351.
    KOi K04246.
    OMAi QHARLSC.
    OrthoDBi EOG7WX08J.
    PhylomeDBi Q99527.
    TreeFami TF333506.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    GeneWikii GPR30.
    GenomeRNAii 2852.
    NextBioi 11247.
    PROi Q99527.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99527.
    Bgeei Q99527.
    CleanExi HS_GPER.
    Genevestigatori Q99527.

    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. "Cloning of human cDNA encoding a novel heptahelix receptor expressed in Burkitt's lymphoma and widely distributed in brain and peripheral tissues."
      Owman C.S.O., Blay P., Nilsson C., Lolait S.J.
      Biochem. Biophys. Res. Commun. 228:285-292(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of a novel member of the G protein-coupled receptor family related to peptide receptors."
      Feng Y., Gregor P.
      Biochem. Biophys. Res. Commun. 231:651-654(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of cDNAs encoding G protein-coupled receptor expressed in human endothelial cells exposed to fluid shear stress."
      Takada Y., Kato C., Kondo S., Korenaga R., Ando J.
      Biochem. Biophys. Res. Commun. 240:737-741(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "A novel putative G-protein-coupled receptor expressed in lung, heart and lymphoid tissue."
      Kvingedal A.M., Smeland E.B.
      FEBS Lett. 407:59-62(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Identification of a gene (GPR30) with homology to the G-protein-coupled receptor superfamily associated with estrogen receptor expression in breast cancer."
      Carmeci C., Thompson D.A., Ring H.Z., Francke U., Weigel R.J.
      Genomics 45:607-617(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Cloning of novel IL8-related receptors from human hepatic tissue."
      McCoy R.L., Perlmutter D.H.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    10. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      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.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-16.
    11. "Human chromosome 7: DNA sequence and biology."
      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.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "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], VARIANT LEU-16.
      Tissue: Uterus.
    14. "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."
      Filardo E.J., Quinn J.A., Bland K.I., Frackelton A.R. Jr.
      Mol. Endocrinol. 14:1649-1660(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Progestin upregulates G-protein-coupled receptor 30 in breast cancer cells."
      Ahola T.M., Purmonen S., Pennanen P., Zhuang Y.H., Tuohimaa P., Ylikomi T.
      Eur. J. Biochem. 269:2485-2490(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    16. "Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells."
      Thomas P., Pang Y., Filardo E.J., Dong J.
      Endocrinology 146:624-632(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ESTROGEN-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    17. "A transmembrane intracellular estrogen receptor mediates rapid cell signaling."
      Revankar C.M., Cimino D.F., Sklar L.A., Arterburn J.B., Prossnitz E.R.
      Science 307:1625-1630(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ESTROGEN-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    18. "Nature of functional estrogen receptors at the plasma membrane."
      Pedram A., Razandi M., Levin E.R.
      Mol. Endocrinol. 20:1996-2009(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF ESTROGEN-BINDING, SUBCELLULAR LOCATION.
    19. "Activation of the novel estrogen receptor G protein-coupled receptor 30 (GPR30) at the plasma membrane."
      Filardo E., Quinn J., Pang Y., Graeber C., Shaw S., Dong J., Thomas P.
      Endocrinology 148:3236-3245(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    20. "G protein-coupled receptor 30 localizes to the endoplasmic reticulum and is not activated by estradiol."
      Otto C., Rohde-Schulz B., Schwarz G., Fuchs I., Klewer M., Brittain D., Langer G., Bader B., Prelle K., Nubbemeyer R., Fritzemeier K.H.
      Endocrinology 149:4846-4856(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF ESTROGEN-BINDING, SUBCELLULAR LOCATION.
    21. Cited for: FUNCTION.
    22. "Coordinate regulation of estrogen-mediated fibronectin matrix assembly and epidermal growth factor receptor transactivation by the G protein-coupled receptor, GPR30."
      Quinn J.A., Graeber C.T., Frackelton A.R. Jr., Kim M., Schwarzbauer J.E., Filardo E.J.
      Mol. Endocrinol. 23:1052-1064(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "G protein-coupled receptor 30 expression is up-regulated by EGF and TGF alpha in estrogen receptor alpha-positive cancer cells."
      Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F., Fuqua S.A., Ando S., Maggiolini M.
      Mol. Endocrinol. 23:1815-1826(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EGFR AND ESR1, INDUCTION.
    24. "Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts."
      Madeo A., Maggiolini M.
      Cancer Res. 70:6036-6046(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EGFR, ASSOCIATION WITH CHROMATIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    25. "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."
      Chan Q.K., Lam H.M., Ng C.F., Lee A.Y., Chan E.S., Ng H.K., Ho S.M., Lau K.M.
      Cell Death Differ. 17:1511-1523(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    26. "Conserved estrogen binding and signaling functions of the G protein-coupled estrogen receptor 1 (GPER) in mammals and fish."
      Thomas P., Alyea R., Pang Y., Peyton C., Dong J., Berg A.H.
      Steroids 75:595-602(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ESTROGEN-BINDING, BIOPHYSICOCHEMICAL PROPERTIES.
    27. "G-1-activated membrane estrogen receptors mediate increased contractility of the human myometrium."
      Maiti K., Paul J.W., Read M., Chan E.C., Riley S.C., Nahar P., Smith R.
      Endocrinology 152:2448-2455(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
    28. "GPR30 expression is required for the mineralocorticoid receptor-independent rapid vascular effects of aldosterone."
      Gros R., Ding Q., Sklar L.A., Prossnitz E.E., Arterburn J.B., Chorazyczewski J., Feldman R.D.
      Hypertension 57:442-451(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALDOSTERONE-BINDING, FUNCTION.
    29. "Down-modulation of the G-protein-coupled estrogen receptor, GPER, from the cell surface occurs via a trans-Golgi-proteasome pathway."
      Cheng S.B., Quinn J.A., Graeber C.T., Filardo E.J.
      J. Biol. Chem. 286:22441-22455(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, UBIQUITINATION.
    30. "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: FUNCTION, INTERACTION WITH KRT7 AND KRT8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    31. "Retrograde transport of the transmembrane estrogen receptor, G-protein-coupled-receptor-30 (GPR30/GPER) from the plasma membrane towards the nucleus."
      Cheng S.B., Graeber C.T., Quinn J.A., Filardo E.J.
      Steroids 76:892-896(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    32. "G protein-coupled estrogen receptor mediates the up-regulation of fatty acid synthase induced by 17beta-estradiol in cancer cells and cancer-associated fibroblasts."
      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.
      J. Biol. Chem. 287:43234-43245(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    33. "G-protein coupled receptor 30 (GPR30): a novel regulator of endothelial inflammation."
      Chakrabarti S., Davidge S.T.
      PLoS ONE 7:E52357-E52357(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    34. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "Aldosterone mediates its rapid effects in vascular endothelial cells through GPER activation."
      Gros R., Ding Q., Liu B., Chorazyczewski J., Feldman R.D.
      Am. J. Physiol. 304:C532-C540(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALDOSTERONE-BINDING, FUNCTION.
    36. "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, INTERACTION WITH RAMP3, SUBCELLULAR LOCATION.
    37. "Position paper: The membrane estrogen receptor GPER--Clues and questions."
      Barton M.
      Steroids 77:935-942(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    38. "Minireview: G protein-coupled estrogen receptor-1, GPER-1: its mechanism of action and role in female reproductive cancer, renal and vascular physiology."
      Filardo E.J., Thomas P.
      Endocrinology 153:2953-2962(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiGPER1_HUMAN
    AccessioniPrimary (citable) accession number: Q99527
    Secondary accession number(s): A8K6C5
    , B5BUJ1, O00143, O43494, Q13631, Q6FHL1, Q96F42, Q99981
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Does not bind estradiol according to PubMed:18566127 and PubMed:16645038.

    Caution

    Data is conflicting regarding whether it fulfills the criteria of a membrane-bound estrogen receptor (PubMed:15705806, PubMed:17379646) or not (PubMed:16645038, PubMed:18566127).4 Publications
    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) or at the endoplasmic reticulum (ER) (PubMed:15705806 and PubMed:18566127).Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3