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

 GPER1_DANRE             Reviewed;         353 AA.
B3G515;
11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 1.
07-NOV-2018, entry version 71.
RecName: Full=G-protein coupled estrogen receptor 1;
AltName: Full=G protein-coupled estrogen receptor 1;
AltName: Full=G-protein coupled receptor 30;
Name=gper1;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ESTROGEN-BINDING,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Testis;
PubMed=19228597; DOI=10.1095/biolreprod.108.070250;
Liu X., Zhu P., Sham K.W., Yuen J.M., Xie C., Zhang Y., Liu Y., Li S.,
Huang X., Cheng C.H., Lin H.;
"Identification of a membrane estrogen receptor in zebrafish with
homology to mammalian GPER and its high expression in early germ cells
of the testis.";
Biol. Reprod. 80:1253-1261(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[3]
FUNCTION.
PubMed=18420744; DOI=10.1210/en.2007-1663;
Pang Y., Dong J., Thomas P.;
"Estrogen signaling characteristics of Atlantic croaker G protein-
coupled receptor 30 (GPR30) and evidence it is involved in maintenance
of oocyte meiotic arrest.";
Endocrinology 149:3410-3426(2008).
[4]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=23583372; DOI=10.1016/j.bbrc.2013.03.130;
Shi Y., Liu X., Zhu P., Li J., Sham K.W., Cheng S.H., Li S., Zhang Y.,
Cheng C.H., Lin H.;
"G-protein-coupled estrogen receptor 1 is involved in brain
development during zebrafish (Danio rerio) embryogenesis.";
Biochem. Biophys. Res. Commun. 435:21-27(2013).
-!- FUNCTION: Membrane 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.
Plays a role in the embryonic development of sensory and motor
neurons. Specifically induces apoptosis and reduces proliferation
of brain cells. Involved in maintenance of meiotic arrest in
oocytes. {ECO:0000269|PubMed:18420744,
ECO:0000269|PubMed:19228597, ECO:0000269|PubMed:23583372}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Binds 17-beta-estradiol (E2) in plasma membranes with high
affinity and displays rapid kinetics of association and
dissociation. {ECO:0000269|PubMed:19228597};
-!- SUBUNIT: Homodimer. Heterodimer (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm,
perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle
membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Cell membrane {ECO:0000269|PubMed:19228597}; Multi-pass membrane
protein {ECO:0000269|PubMed:19228597}. Basolateral cell membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling
endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network
{ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Cell projection, dendrite
{ECO:0000250}. Cell projection, dendritic spine membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
projection, axon {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}. Note=Colocalized with cadherin at the plasma
membrane. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in brain regions that are known to
control reproduction and sex behavior. Expressed in ovary, muscle
and intestine. Expressed in early germ cells of the testis,
including the spermatogonia, spermatocytes, and somatic cells such
as Sertoli cells. {ECO:0000269|PubMed:19228597}.
-!- DEVELOPMENTAL STAGE: Expressed throughout early embryonic
development from 0 hours post-fertilization (hpf) to 72 hpf.
Expressed in blastomeres at 4 hpf. Expressed in the central
nervous system at 18 hpf. Expressed in head including the anterior
diencephalon, midbrain and hindbrain at 24 hpf. Expressed in
trigeminal ganglia as well as in the heart, pancreas and
intestinal bulb between 36 and 72 hpf (at protein level).
{ECO:0000269|PubMed:23583372}.
-!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein leads to
growth retardation and developmental deformity.
{ECO:0000269|PubMed:23583372}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; EU652771; ACD88749.1; -; mRNA.
EMBL; CR382361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001122195.1; NM_001128723.1.
RefSeq; XP_009298009.1; XM_009299734.2.
UniGene; Dr.148317; -.
ProteinModelPortal; B3G515; -.
STRING; 7955.ENSDARP00000070486; -.
PaxDb; B3G515; -.
Ensembl; ENSDART00000076007; ENSDARP00000070486; ENSDARG00000074661.
Ensembl; ENSDART00000189772; ENSDARP00000156576; ENSDARG00000074661.
GeneID; 565271; -.
KEGG; dre:565271; -.
CTD; 2852; -.
ZFIN; ZDB-GENE-090311-1; gper1.
eggNOG; ENOG410IEGB; Eukaryota.
eggNOG; ENOG4111653; LUCA.
GeneTree; ENSGT00530000063910; -.
HOGENOM; HOG000013114; -.
HOVERGEN; HBG005351; -.
InParanoid; B3G515; -.
KO; K04246; -.
OMA; QHARLSC; -.
OrthoDB; EOG091G09A2; -.
PhylomeDB; B3G515; -.
TreeFam; TF333506; -.
Reactome; R-DRE-375276; Peptide ligand-binding receptors.
Reactome; R-DRE-418594; G alpha (i) signalling events.
PRO; PR:B3G515; -.
Proteomes; UP000000437; Chromosome 3.
Bgee; ENSDARG00000074661; Expressed in 13 organ(s), highest expression level in heart.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0030284; F:estrogen receptor activity; IDA:ZFIN.
GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
GO; GO:0005496; F:steroid binding; IDA:UniProtKB.
GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007420; P:brain development; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
GO; GO:0060047; P:heart contraction; IMP:ZFIN.
GO; GO:0051447; P:negative regulation of meiotic cell cycle; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
GO; GO:1900194; P:negative regulation of oocyte maturation; IDA:UniProtKB.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Apoptosis; Cell cycle; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Developmental protein; Differentiation; Disulfide bond;
Endoplasmic reticulum; Endosome; G-protein coupled receptor;
Golgi apparatus; Membrane; Mitochondrion; Neurogenesis; Nucleus;
Postsynaptic cell membrane; Receptor; Reference proteome; Synapse;
Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 353 G-protein coupled estrogen receptor 1.
/FTId=PRO_0000424544.
TOPO_DOM 1 40 Extracellular. {ECO:0000255}.
TRANSMEM 41 61 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 62 81 Cytoplasmic. {ECO:0000255}.
TRANSMEM 82 102 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 103 112 Extracellular. {ECO:0000255}.
TRANSMEM 113 133 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 134 160 Cytoplasmic. {ECO:0000255}.
TRANSMEM 161 181 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 182 202 Extracellular. {ECO:0000255}.
TRANSMEM 203 223 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 224 245 Cytoplasmic. {ECO:0000255}.
TRANSMEM 246 266 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 267 292 Extracellular. {ECO:0000255}.
TRANSMEM 293 313 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 314 353 Cytoplasmic. {ECO:0000255}.
DISULFID 115 192 {ECO:0000255|PROSITE-ProRule:PRU00521}.
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


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