GPER1_DANRE
ID GPER1_DANRE Reviewed; 353 AA.
AC B3G515;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=G-protein coupled estrogen receptor 1;
DE AltName: Full=G protein-coupled estrogen receptor 1;
DE AltName: Full=G-protein coupled receptor 30;
GN Name=gper1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ESTROGEN-BINDING, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=19228597; DOI=10.1095/biolreprod.108.070250;
RA Liu X., Zhu P., Sham K.W., Yuen J.M., Xie C., Zhang Y., Liu Y., Li S.,
RA Huang X., Cheng C.H., Lin H.;
RT "Identification of a membrane estrogen receptor in zebrafish with homology
RT to mammalian GPER and its high expression in early germ cells of the
RT testis.";
RL Biol. Reprod. 80:1253-1261(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP FUNCTION.
RX PubMed=18420744; DOI=10.1210/en.2007-1663;
RA Pang Y., Dong J., Thomas P.;
RT "Estrogen signaling characteristics of Atlantic croaker G protein-coupled
RT receptor 30 (GPR30) and evidence it is involved in maintenance of oocyte
RT meiotic arrest.";
RL Endocrinology 149:3410-3426(2008).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=23583372; DOI=10.1016/j.bbrc.2013.03.130;
RA Shi Y., Liu X., Zhu P., Li J., Sham K.W., Cheng S.H., Li S., Zhang Y.,
RA Cheng C.H., Lin H.;
RT "G-protein-coupled estrogen receptor 1 is involved in brain development
RT during zebrafish (Danio rerio) embryogenesis.";
RL Biochem. Biophys. Res. Commun. 435:21-27(2013).
CC -!- FUNCTION: Membrane G-protein coupled estrogen receptor that binds to
CC 17-beta-estradiol (E2) with high affinity, leading to rapid and
CC transient activation of numerous intracellular signaling pathways.
CC Plays a role in the embryonic development of sensory and motor neurons.
CC Specifically induces apoptosis and reduces proliferation of brain
CC cells. Involved in maintenance of meiotic arrest in oocytes.
CC {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19228597,
CC ECO:0000269|PubMed:23583372}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Binds 17-beta-estradiol (E2) in plasma membranes with high
CC affinity and displays rapid kinetics of association and dissociation.
CC {ECO:0000269|PubMed:19228597};
CC -!- SUBUNIT: Homodimer. Heterodimer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:19228597}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19228597}. Basolateral cell membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
CC projection, dendrite {ECO:0000250}. Cell projection, dendritic spine
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
CC projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}.
CC Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=Colocalized with cadherin at the plasma membrane.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain regions that are known to
CC control reproduction and sex behavior. Expressed in ovary, muscle and
CC intestine. Expressed in early germ cells of the testis, including the
CC spermatogonia, spermatocytes, and somatic cells such as Sertoli cells.
CC {ECO:0000269|PubMed:19228597}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout early embryonic development
CC from 0 hours post-fertilization (hpf) to 72 hpf. Expressed in
CC blastomeres at 4 hpf. Expressed in the central nervous system at 18
CC hpf. Expressed in head including the anterior diencephalon, midbrain
CC and hindbrain at 24 hpf. Expressed in trigeminal ganglia as well as in
CC the heart, pancreas and intestinal bulb between 36 and 72 hpf (at
CC protein level). {ECO:0000269|PubMed:23583372}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein leads to
CC growth retardation and developmental deformity.
CC {ECO:0000269|PubMed:23583372}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; EU652771; ACD88749.1; -; mRNA.
DR EMBL; CR382361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001122195.1; NM_001128723.1.
DR RefSeq; XP_009298009.1; XM_009299734.2.
DR AlphaFoldDB; B3G515; -.
DR SMR; B3G515; -.
DR STRING; 7955.ENSDARP00000070486; -.
DR PaxDb; B3G515; -.
DR Ensembl; ENSDART00000076007; ENSDARP00000070486; ENSDARG00000074661.
DR Ensembl; ENSDART00000189772; ENSDARP00000156576; ENSDARG00000074661.
DR GeneID; 565271; -.
DR KEGG; dre:565271; -.
DR CTD; 2852; -.
DR ZFIN; ZDB-GENE-090311-1; gper1.
DR eggNOG; ENOG502QU56; Eukaryota.
DR GeneTree; ENSGT00940000154307; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; B3G515; -.
DR OMA; FRTKQHA; -.
DR OrthoDB; 736624at2759; -.
DR PhylomeDB; B3G515; -.
DR TreeFam; TF333506; -.
DR Reactome; R-DRE-375276; Peptide ligand-binding receptors.
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR Reactome; R-DRE-9634597; GPER1 signaling.
DR PRO; PR:B3G515; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000074661; Expressed in male germ cell and 35 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:ZFIN.
DR GO; GO:0005496; F:steroid binding; IDA:UniProtKB.
DR GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR GO; GO:0060047; P:heart contraction; IMP:ZFIN.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; IDA:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell cycle; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Developmental protein; Differentiation;
KW Disulfide bond; Endoplasmic reticulum; Endosome;
KW G-protein coupled receptor; Golgi apparatus; Membrane; Mitochondrion;
KW Neurogenesis; Nucleus; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..353
FT /note="G-protein coupled estrogen receptor 1"
FT /id="PRO_0000424544"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 115..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 353 AA; 40859 MW; B88913B13954D4B2 CRC64;
MEEQTTNVIQ IYVNGTEQFN ASFDFNITDV KESTDTYEFY IIGLFLSCLY TIFLFPIGFI
GNILILVVNL NHRERMTIPD LYFVNLAVAD LILVADSLIE VFNLNEKYYD YAVLCTFMSL
FLQVNMYSSI FFLTWMSFDR YVALTSSMSS SPLRTMQHAK LSCSLIWMAS ILATLLPFTI
VQTQHTGEVH FCFANVFEIQ WLEVTIGFLI PFSIIGLCYS LIVRTLMRAQ KHKGLWPRRQ
KALRMIVVVV LVFFICWLPE NVFISIQLLQ GTADPSKRTD TTLWHDYPLT GHIVNLAAFS
NSCLNPIIYS FLGETFRDKL RLFIKRKASW SVVYRFCNHT LDLQIPVRSE SEV
