P28473 · GBRG3_RAT
- ProteinGamma-aminobutyric acid receptor subunit gamma-3
- GeneGabrg3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids467 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Gamma subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:10462548, PubMed:1311098, PubMed:1660002).
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) (By similarity).
When activated by GABA, GABAARs selectively allow the flow of chloride across the cell membrane down their electrochemical gradient (PubMed:10462548, PubMed:1311098, PubMed:1660002).
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) (By similarity).
When activated by GABA, GABAARs selectively allow the flow of chloride across the cell membrane down their electrochemical gradient (PubMed:10462548, PubMed:1311098, PubMed:1660002).
Catalytic activity
- chloride(in) = chloride(out)
Activity regulation
Allosterically potentiated by alphaxalone. Allosterically inhibited by pregnenolone sulfate. Inhibited by zinc and lanthanum.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGamma-aminobutyric acid receptor subunit gamma-3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP28473
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Postsynaptic cell membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 18-256 | Extracellular | ||||
Sequence: RSRRVEEDDSEDSPSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDAHACPLTFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYF | ||||||
Transmembrane | 257-277 | Helical | ||||
Sequence: TIQTYIPCILTVVLSWVSFWI | ||||||
Topological domain | 278-283 | Cytoplasmic | ||||
Sequence: KKDATP | ||||||
Transmembrane | 284-303 | Helical | ||||
Sequence: ARTTLGITTVLTMTTLSTIA | ||||||
Topological domain | 304-311 | Extracellular | ||||
Sequence: RKSLPRVS | ||||||
Transmembrane | 312-332 | Helical | ||||
Sequence: YVTAMDLFVTVCFLFVFAALM | ||||||
Topological domain | 333-446 | Cytoplasmic | ||||
Sequence: EYATLNYYSSCRKPTIRKKKTSLLHPDSTRWIPDRISLQAPSNYSLLDMRPPPPVMITLNNSMYWQEFEDTCVYECLDGKDCQSFFCCYEECKSGSWRRGRIHIDVSELDSYSR | ||||||
Transmembrane | 447-467 | Helical | ||||
Sequence: VFFPTSFLLFNLVYWVGYLYL |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MAAKLLLLLCLFSGLHA | ||||||
Chain | PRO_0000000483 | 18-467 | Gamma-aminobutyric acid receptor subunit gamma-3 | |||
Sequence: RSRRVEEDDSEDSPSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDAHACPLTFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYFTIQTYIPCILTVVLSWVSFWIKKDATPARTTLGITTVLTMTTLSTIARKSLPRVSYVTAMDLFVTVCFLFVFAALMEYATLNYYSSCRKPTIRKKKTSLLHPDSTRWIPDRISLQAPSNYSLLDMRPPPPVMITLNNSMYWQEFEDTCVYECLDGKDCQSFFCCYEECKSGSWRRGRIHIDVSELDSYSRVFFPTSFLLFNLVYWVGYLYL | ||||||
Glycosylation | 110 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 171↔185 | |||||
Sequence: CQLQLHNFPMDAHAC | ||||||
Glycosylation | 228 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
May be palmitoylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Heteropentamer, formed by a combination of alpha (GABRA1-6), beta (GABRB1-3), gamma (GABRG1-3), delta (GABRD), epsilon (GABRE), rho (GABRR1-3), pi (GABRP) and theta (GABRQ) chains, each subunit exhibiting distinct physiological and pharmacological properties.
Protein-protein interaction databases
Structure
Family & Domains
Domain
GABAARs subunits share a common topological structure: a peptide sequence made up of a long extracellular N-terminal, four transmembrane domains, intracellular or cytoplasmic domain located between the third and the fourth transmembrane domains.
Sequence similarities
Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRG3 sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length467
- Mass (Da)54,293
- Last updated1992-12-01 v1
- Checksum14959F565649D67D
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A0MXX6 | A0A0A0MXX6_RAT | Gabrg3 | 428 | ||
A0A8I5ZZR3 | A0A8I5ZZR3_RAT | Gabrg3 | 141 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 416 | in Ref. 2; CAA44930 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M81142 EMBL· GenBank· DDBJ | AAA41181.1 EMBL· GenBank· DDBJ | mRNA | ||
X63324 EMBL· GenBank· DDBJ | CAA44930.1 EMBL· GenBank· DDBJ | mRNA |