GABRA1
entrez
2554
canonical
uniprot
P14867
canonical
ensembl
ENSG00000022355
resolver
ensp
ENSP00000023897
resolver
ensp
ENSP00000377517
resolver
ensp
ENSP00000393097
resolver
ensp
ENSP00000415441
resolver
ensp
ENSP00000489738
resolver
ensp
ENSP00000489839
resolver
ensp
ENSP00000490320
resolver
ensp
ENSP00000490804
resolver
ensp
ENSP00000628988
resolver
ensp
ENSP00000628989
resolver
enst
ENST00000023897
resolver
enst
ENST00000393943
resolver
enst
ENST00000428797
resolver
enst
ENST00000437025
resolver
enst
ENST00000635880
resolver
enst
ENST00000636573
resolver
enst
ENST00000637827
resolver
enst
ENST00000638112
resolver
enst
ENST00000958929
resolver
enst
ENST00000958930
resolver
genesymbol
GABRA1
resolver
hgnc
HGNC:4075
resolver
uniprot
A8K177
resolver
uniprot
D3DQK6
resolver
uniprot
Q8N629
resolver
uniprot_entry
A8K177_HUMAN
resolver
uniprot_entry
GBRA1_HUMAN
resolver
uniprot_sec
D3DQK6
resolver
uniprot_sec
Q8N629
resolver
activity_regulation
ACTIVITY REGULATION: Allosterically activated by benzodiazepines and the anesthetic alphaxalone (PubMed:29950725, PubMed:30266951). Allosterically activated by pentobarbital (By similarity). Inhibited by the antagonist bicuculline (PubMed:29950725). Potentiated by histamine (By similarity). {ECO:0000250|UniProtKB:P62813, ECO:0000269|PubMed:29950725, ECO:0000269|PubMed:30266951}.
uniprot
proteins
amino_acid_sequence
MRKSPGLSDCLWAWILLLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGYAWDGKSVVPEKPKKVKDPLIKKNNTYAPTATSYTPNLARGDPGLATIAKSATIEPKEVKPETKPPEPKKTFNSVSKIDRLSRIAFPLLFGIFNLVYWATYLNREPQLKAPTPHQ
uniprot
proteins
disease_involvement
DISEASE: Epilepsy, childhood absence 4 (ECA4) [MIM:611136]: A subtype of idiopathic generalized epilepsy characterized by an onset at age 6-7 years, frequent absence seizures (several per day) and bilateral, synchronous, symmetric 3-Hz spike waves on EEG. Tonic-clonic seizures often develop in adolescence. Absence seizures may either remit or persist into adulthood. {ECO:0000269|PubMed:16718694}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Epilepsy, idiopathic generalized 13 (EIG13) [MIM:611136]: A disorder characterized by recurring generalized seizures in the absence of detectable brain lesions and/or metabolic abnormalities. Generalized seizures arise diffusely and simultaneously from both hemispheres of the brain. Seizure types include juvenile myoclonic seizures, absence seizures, and generalized tonic-clonic seizures. {ECO:0000269|PubMed:21714819}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Juvenile myoclonic epilepsy 5 (EJM5) [MIM:611136]: A subtype of idiopathic generalized epilepsy. Patients have afebrile seizures only, with onset in adolescence (rather than in childhood) and myoclonic jerks which usually occur after awakening and are triggered by sleep deprivation and fatigue. {ECO:0000269|PubMed:11992121}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 19 (DEE19) [MIM:615744]: A severe neurologic disorder characterized by onset of seizures in the first months of life and usually associated with EEG abnormalities. Affected infants have convulsive seizures (hemiclonic or generalized) that are often prolonged and triggered by fever. Other seizure types include focal, myoclonic, absence seizures, and drop attacks. Development is normal in the first year of life with later slowing and intellectual disability. {ECO:0000269|PubMed:24623842, ECO:0000269|PubMed:27864847}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Alpha subunit of the heteropentameric ligand-gated chloride channel gated by Gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:23909897, PubMed:25489750, PubMed:29950725, PubMed:30602789). 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:29950725, PubMed:30602789). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:23909897, PubMed:29950725, PubMed:30602789). Alpha-1/GABRA1-containing GABAARs are largely synaptic (By similarity). Chloride influx into the postsynaptic neuron following GABAAR opening decreases the neuron ability to generate a new action potential, thereby reducing nerve transmission (By similarity). GABAARs containing alpha-1 and beta-2 or -3 subunits exhibit synaptogenic activity; the gamma-2 subunit being necessary but not sufficient to induce rapid synaptic contacts formation (PubMed:23909897, PubMed:25489750). GABAARs function also as histamine receptor where histamine binds at the interface of two neighboring beta subunits and potentiates GABA response (By similarity). GABAARs containing alpha, beta and epsilon subunits also permit spontaneous chloride channel activity while preserving the structural information required for GABA-gated openings (By similarity). Alpha-1-mediated plasticity in the orbitofrontal cortex regulates context-dependent action selection (By similarity). Together with rho subunits, may also control neuronal and glial GABAergic transmission in the cerebellum (By similarity). {ECO:0000250|UniProtKB:P08219, ECO:0000250|UniProtKB:P62812, ECO:0000250|UniProtKB:P62813, ECO:0000269|PubMed:23909897, ECO:0000269|PubMed:25489750, ECO:0000269|PubMed:29950725, ECO:0000269|PubMed:30602789}.
uniprot
proteins
mass_dalton
51802
uniprot
proteins
mutagenesis
MUTAGEN 269; /note="Q->L: Reduced potentiation and activation by the agonist alphaxalone."; /evidence="ECO:0000269|PubMed:30266951"; MUTAGEN 273; /note="W->L: Completely abolishes potentiation and activation by the agonist alphaxalone."; /evidence="ECO:0000269|PubMed:30266951"; MUTAGEN 333; /note="T->A: Reduced potentiation and activation by the agonist alphaxalone."; /evidence="ECO:0000269|PubMed:30266951
uniprot
proteins
protein_family
GABRA1 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
11992121
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16718694
uniprot
proteins
pubmed
21714819
uniprot
proteins
pubmed
23909897
uniprot
proteins
pubmed
24623842
uniprot
proteins
pubmed
2465923
uniprot
proteins
pubmed
25489750
uniprot
proteins
pubmed
27864847
uniprot
proteins
pubmed
2847710
uniprot
proteins
pubmed
28978485
uniprot
proteins
pubmed
29742426
uniprot
proteins
pubmed
29950725
uniprot
proteins
pubmed
30266951
uniprot
proteins
pubmed
30602789
uniprot
proteins
sequence_length
456
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P08219}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Cell membrane {ECO:0000269|PubMed:2465923, ECO:0000269|PubMed:25489750}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P62813}; Multi-pass membrane protein {ECO:0000269|PubMed:29950725}. Note=Mainly located in GABAergic synapses in granule cells, and also in the extrasynaptic membrane at a lower concentration. {ECO:0000250|UniProtKB:P62813}.
uniprot
proteins
transmembrane_region
TRANSMEM 254..274; /note="Helical"; /evidence="ECO:0000269|PubMed:29950725, ECO:0007744|PDB:6D6T, ECO:0007744|PDB:6D6U"; TRANSMEM 280..301; /note="Helical"; /evidence="ECO:0000269|PubMed:29950725, ECO:0007744|PDB:6D6T, ECO:0007744|PDB:6D6U"; TRANSMEM 312..333; /note="Helical"; /evidence="ECO:0000269|PubMed:29950725, ECO:0007744|PDB:6D6T, ECO:0007744|PDB:6D6U"; TRANSMEM 422..441; /note="Helical"; /evidence="ECO:0000269|PubMed:29950725, ECO:0007744|PDB:6D6T, ECO:0007744|PDB:6D6U
uniprot
proteins