GPER1_MICUN
ID GPER1_MICUN Reviewed; 354 AA.
AC B0F9W3;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
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 Micropogonias undulatus (Atlantic croaker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Micropogonias.
OX NCBI_TaxID=29154;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ESTROGEN-BINDING, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 [2]
RP FUNCTION, ESTROGEN-BINDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19931550; DOI=10.1016/j.steroids.2009.11.005;
RA Thomas P., Alyea R., Pang Y., Peyton C., Dong J., Berg A.H.;
RT "Conserved estrogen binding and signaling functions of the G protein-
RT coupled estrogen receptor 1 (GPER) in mammals and fish.";
RL Steroids 75:595-602(2010).
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 May induce apoptosis and reduce proliferation of brain cells. Involved
CC in maintenance of meiotic arrest in oocytes.
CC {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19931550}.
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:18420744, ECO:0000269|PubMed:19931550};
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:18420744}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18420744}. 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 -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level). Highly
CC expressed in brain, heart, testis and ovary. Weakly expressed in muscle
CC and intestine. {ECO:0000269|PubMed:18420744}.
CC -!- DEVELOPMENTAL STAGE: Expressed during oocyte development.
CC {ECO:0000269|PubMed:18420744}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU274298; ABY51613.1; -; mRNA.
DR AlphaFoldDB; B0F9W3; -.
DR SMR; B0F9W3; -.
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:UniProtKB.
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:0005496; F:steroid binding; IDA:UniProtKB.
DR GO; GO:1990239; F:steroid hormone binding; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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:0071371; P:cellular response to gonadotropin stimulus; IDA:UniProtKB.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IDA:UniProtKB.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; 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; Synapse;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..354
FT /note="G-protein coupled estrogen receptor 1"
FT /id="PRO_0000424545"
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 354 AA; 40771 MW; FBDBCDA55E965D8E CRC64;
MEEQTTSLVW IYVNSTEQLN TSYEYNTTYL IEDSDKYQSY VIGLFLSCLY TILLFPIGFI
GNILILVVNL NHRGKMAIPD LYFVNLAVAD LILVADSLIE VFNLNEKYYD YAVLCTFMSL
FLQVNMYSSI FFLTWMSFDR YIALANSMSS SPLRTMQHAK LSCGLIWMAS ILATLLPFTI
VQTQHRGEVH FCFANVFEIQ WLEVTIGFLV PFSIIGLCYS LIGRILMRSQ KHRGLWPRRQ
KALRMIVVVV LVFFICWLPE NVFISIQLLQ GTADPSQRTA TTLRHDYPLT GHIVNLAAFS
NSCLNPIIYS FLGETFRDKL RLFIKQKASW SVVNRFCHHG LDLHLPVRSE VSEV
