Gabrb3
entrez
24922
canonical
uniprot
P63079
canonical
ensembl
ENSRNOG00000060599
resolver
ensembl
ENSRNOG00055014837
resolver
ensembl
ENSRNOG00060000098
resolver
ensembl
ENSRNOG00065003735
resolver
ensp
ENSRNOP00000085111
resolver
ensp
ENSRNOP00055020756
resolver
ensp
ENSRNOP00060000084
resolver
ensp
ENSRNOP00065003981
resolver
enst
ENSRNOT00055025431
resolver
enst
ENSRNOT00060000138
resolver
enst
ENSRNOT00065005454
resolver
genesymbol
Gabrb3
resolver
genesymbol_syn
Gabrb-3
resolver
uniprot
P15433
resolver
uniprot_entry
GBRB3_RAT
resolver
uniprot_sec
P15433
resolver
activity_regulation
ACTIVITY REGULATION: Potentiated by pentobarbital, loreclezole and alphaxalone (PubMed:10462548, PubMed:9882711). Potentiated by histamine (By similarity). Allosterically inhibited by pregnenolone sulfate (PubMed:10462548). Inhibited by zinc and furosemide (PubMed:10462548, PubMed:9882711). Beta-3-containing GABAAR are potentiated by lanthanum when associated with alpha-1 subunit and inhibited by lanthanum when associated with alpha-5 subunit (PubMed:10462548, PubMed:9882711). {ECO:0000250|UniProtKB:P28472, ECO:0000269|PubMed:10462548, ECO:0000269|PubMed:9882711}.
uniprot
proteins
amino_acid_sequence
MWGFAGGRLFGIFSAPVLVAVVCCAQSVNDPGNMSFVKETVDKLLKGYDIRLRPDFGGPPVCVGMNIDIASIDMVSEVNMDYTLTMYFQQYWRDKRLAYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGGDKAVTGVERIELPQFSIVEHRLVSRNVVFATGAYPRLSLSFRLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFLALLEYAFVNYIFFGRGPQRQKKLAEKTAKAKNDRSKSEINRVDAHGNILLAPMDVHNEMNEVAGSVGDTRNSAISFDNSGIQYRKQSMPKEGHGRYMGDRSIPHKKTHLRRRSSQLKIKIPDLTDVNAIDRWSRIVFPFTFSLFNLVYWLYYVN
uniprot
proteins
function
FUNCTION: Beta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:10462548, PubMed:2540033, PubMed:2548852, PubMed:9882711). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s) (PubMed:9092594). GABAARs containing beta-3/GABRB3 subunit are found at both synaptic and extrasynaptic sites (PubMed:9464994). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:10462548, PubMed:2540033, PubMed:9882711). Chloride influx into the postsynaptic neuron following GABAAR opening decreases the neuron ability to generate a new action potential, thereby reducing nerve transmission (PubMed:2540033). GABAARs containing alpha-1 and beta-3 subunits exhibit synaptogenic activity; the gamma-2 subunit being necessary but not sufficient to induce rapid synaptic contacts formation (By similarity). Extrasynaptic beta-3 receptors contribute to the tonic GABAergic inhibition (PubMed:9464994). GABAARs containing alpha-1, beta-3 and epsilon subunits may permit spontaneous chloride channel activity while preserving the structural information required for GABA-gated openings (PubMed:9882711). Beta-containing GABAARs can simultaneously bind GABA and histamine where histamine binds at the interface of two neighboring beta subunits, which may be involved in the regulation of sleep and wakefulness (By similarity). Plays an important role in somatosensation and in the production of antinociception (By similarity). {ECO:0000250|UniProtKB:P28472, ECO:0000250|UniProtKB:P63080, ECO:0000269|PubMed:10462548, ECO:0000269|PubMed:2540033, ECO:0000269|PubMed:2548852, ECO:0000269|PubMed:9092594, ECO:0000269|PubMed:9464994, ECO:0000269|PubMed:9882711}.
uniprot
proteins
mass_dalton
54166
uniprot
proteins
protein_family
GABRB3 sub-subfamily
uniprot
proteins
protein_family
Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily
uniprot
proteins
protein_family
Ligand-gated ion channel (TC 1.A.9) family
uniprot
proteins
pubmed
10462548
uniprot
proteins
pubmed
11528422
uniprot
proteins
pubmed
16641100
uniprot
proteins
pubmed
25172774
uniprot
proteins
pubmed
25284783
uniprot
proteins
pubmed
2540033
uniprot
proteins
pubmed
2548852
uniprot
proteins
pubmed
28279354
uniprot
proteins
pubmed
8382702
uniprot
proteins
pubmed
9092594
uniprot
proteins
pubmed
9464994
uniprot
proteins
pubmed
9882711
uniprot
proteins
sequence_length
473
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P28472}. Cell membrane {ECO:0000269|PubMed:2540033, ECO:0000269|PubMed:2548852, ECO:0000269|PubMed:9092594, ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P28472}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25172774}. Note=The beta-3 subunits are present in Golgi synapses and on the extrasynaptic membranes (when coassembled with alpha-1/6 and gamma-2 subunits), and in some of the mossy fiber to granule cell synapses (when coassembled with alpha-6 and gamma-2 subunits) (PubMed:9464994). The beta-3 subunits, when coassembled with alpha-6 and delta subunits, are found only on the extrasynaptic somatic and dendritic membranes (PubMed:9464994). {ECO:0000269|PubMed:9464994}.
uniprot
proteins
transmembrane_region
TRANSMEM 247..267; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P28472"; TRANSMEM 272..292; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P28472"; TRANSMEM 305..328; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P28472"; TRANSMEM 448..470; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P28472
uniprot
proteins