GBRG1_RAT
ID GBRG1_RAT Reviewed; 465 AA.
AC P23574;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit gamma-1;
DE AltName: Full=GABA(A) receptor subunit gamma-1;
DE Flags: Precursor;
GN Name=Gabrg1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2170110; DOI=10.1002/j.1460-2075.1990.tb07525.x;
RA Ymer S., Draguhn A., Wisden W., Werner P., Keinaenen K., Schofield P.R.,
RA Sprengel R., Pritchett D.B., Seeburg P.H.;
RT "Structural and functional characterization of the gamma 1 subunit of
RT GABAA/benzodiazepine receptors.";
RL EMBO J. 9:3261-3267(1990).
CC -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate
CC brain, mediates neuronal inhibition by binding to the
CC GABA/benzodiazepine receptor and opening an integral chloride channel.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- PTM: May be palmitoylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: This subunit carries the benzodiazepine binding site.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRG1 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X57514; CAA40739.1; -; mRNA.
DR PIR; S12056; S12056.
DR RefSeq; NP_542153.1; NM_080586.1.
DR AlphaFoldDB; P23574; -.
DR SMR; P23574; -.
DR BioGRID; 250833; 1.
DR CORUM; P23574; -.
DR STRING; 10116.ENSRNOP00000003240; -.
DR BindingDB; P23574; -.
DR ChEMBL; CHEMBL296; -.
DR DrugCentral; P23574; -.
DR CarbonylDB; P23574; -.
DR GlyGen; P23574; 3 sites.
DR PaxDb; P23574; -.
DR PRIDE; P23574; -.
DR Ensembl; ENSRNOT00000003240; ENSRNOP00000003240; ENSRNOG00000002360.
DR GeneID; 140674; -.
DR KEGG; rno:140674; -.
DR UCSC; RGD:621732; rat.
DR CTD; 2565; -.
DR RGD; 621732; Gabrg1.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000160193; -.
DR HOGENOM; CLU_010920_2_0_1; -.
DR InParanoid; P23574; -.
DR OMA; GMRNTTD; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; P23574; -.
DR TreeFam; TF315453; -.
DR PRO; PR:P23574; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002360; Expressed in frontal cortex and 3 other tissues.
DR Genevisible; P23574; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0050811; F:GABA receptor binding; IPI:RGD.
DR GO; GO:0004890; F:GABA-A receptor activity; IDA:RGD.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IBA:GO_Central.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR005438; GABBAg1_rcpt.
DR InterPro; IPR005437; GABRG-1/4.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR01620; GABAARGAMMA.
DR PRINTS; PR01621; GABAARGAMMA1.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
KW Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..465
FT /note="Gamma-aminobutyric acid receptor subunit gamma-1"
FT /id="PRO_0000000475"
FT TOPO_DOM 36..272
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 299..320
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 355..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000305"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 188..202
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 53551 MW; 7EC2CE8FBF04663B CRC64;
MGSGKVFLFS PSLLWSQTRG VRLIFLLLTL HLGNCIDKAD DEDDEDLTMN KTWVLAPKIH
EGDITQILNS LLQGYDNKLR PDIGVRPTVI ETDVYVNSIG PVDPINMEYT IDIIFAQTWF
DSRLKFNSTM KVLMLNSNMV GKIWIPDTFF RNSRKSDAHW ITTPNRLLRI WSDGRVLYTL
RLTINAECYL QLHNFPMDEH SCPLEFSSYG YPKNEIEYKW KKPSVEVADP KYWRLYQFAF
VGLRNSTEIS HTISGDYIIM TIFFDLSRRM GYFTIQTYIP CILTVVLSWV SFWINKDAVP
ARTSLGITTV LTMTTLSTIA RKSLPKVSYV TAMDLFVSVC FIFVFAALME YGTLHYFTSN
NKGKTTRDRK LKSKTSVSPG LHAGSTLIPM NNISMPQGED DYGYQCLEGK DCATFFCCFE
DCRTGSWREG RIHIRIAKID SYSRIFFPTA FALFNLVYWV GYLYL
