Glra1
entrez
14654
canonical
uniprot
Q64018
canonical
ensembl
ENSMUSG00000000263
resolver
ensp
ENSMUSP00000075032
resolver
ensp
ENSMUSP00000099777
resolver
genesymbol
Glra1
resolver
uniprot
Q5NCT8
resolver
uniprot
Q5NCT9
resolver
uniprot
Q64019
resolver
uniprot
Q9R0Y6
resolver
uniprot
Q9R0Y7
resolver
uniprot_entry
GLRA1_MOUSE
resolver
uniprot_entry
Q5NCT9_MOUSE
resolver
uniprot_sec
Q5NCT8
resolver
uniprot_sec
Q64019
resolver
uniprot_sec
Q9R0Y6
resolver
uniprot_sec
Q9R0Y7
resolver
activity_regulation
ACTIVITY REGULATION: Channel opening is triggered by extracellular glycine (PubMed:16672662, PubMed:17114051). Channel characteristics depend on the subunit composition; heteropentameric channels are activated by lower glycine levels and display faster desensitization (By similarity). Channel opening is also triggered by taurine and beta-alanine (By similarity). Inhibited by strychnine. Strychnine binding locks the channel in a closed conformation and prevents channel opening in response to extracellular glycine (By similarity). Inhibited by picrotoxin (PubMed:16672662). Channel activity is enhanced by 5 uM Zn(2+) and inhibited by 100 uM Zn(2+) (PubMed:17114051). {ECO:0000250|UniProtKB:P23415, ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051}.
uniprot
proteins
amino_acid_sequence
MYSFNTLRFYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQDDEGGEGRFNFSAYGMGPACLQAKDGISVKGANNNNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNK
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Glra1 are the cause of the spasmodic (spd) phenotype, a mouse mutant which resembles the human neurological disease, hyperekplexia (or startle disease (STHE)) (PubMed:7920629). Defects in Glra1 are the cause of the lethal oscillator (spd-ot) phenotype. Mutant mice display a fine motor tremor and muscle spasms that begin at 2 weeks of age and progressively worsen, resulting in death by 3 weeks of age (PubMed:7874121). Heterozygous mice show an increased acoustic startle response (PubMed:9145798). Neurons from homozygous oscillator mice have dramatically reduced amplitude and frequency of glycinergic inhibitory postsynaptic currents (PubMed:16672662). The oscillator phenotype is due to the complete absence of Glra1 protein (PubMed:9145798). {ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:7874121, ECO:0000269|PubMed:7920629, ECO:0000269|PubMed:9145798}.
uniprot
proteins
function
FUNCTION: Subunit of heteromeric glycine-gated chloride channels (PubMed:16672662, PubMed:17114051, PubMed:24801766). Plays an important role in the down-regulation of neuronal excitability (PubMed:9145798). Contributes to the generation of inhibitory postsynaptic currents (PubMed:16672662, PubMed:17114051, PubMed:24801766). Channel activity is potentiated by ethanol. Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol (PubMed:24801766). {ECO:0000250|UniProtKB:P23415, ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051, ECO:0000269|PubMed:24801766, ECO:0000269|PubMed:9145798}.
uniprot
proteins
mass_dalton
52657
uniprot
proteins
mutagenesis
MUTAGEN 108; /note="D->A: Eliminates potentiation of glycine-mediated currents by Zn(2+) and causes neuromotor defects similar to human startle disease."; /evidence="ECO:0000269|PubMed:17114051"; MUTAGEN 421..422; /note="KK->AA: Reduces the increase of channel activity in response to ethanol and improves tolerance of intoxicating levels of alcohol."; /evidence="ECO:0000269|PubMed:24801766
uniprot
proteins
protein_family
GLRA1 sub-subfamily
uniprot
proteins
protein_family
Glycine receptor (TC 1.A.9.3) subfamily
uniprot
proteins
protein_family
Ligand-gated ion channel (TC 1.A.9) family
uniprot
proteins
pubmed
12975813
uniprot
proteins
pubmed
16672662
uniprot
proteins
pubmed
17114051
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
24801766
uniprot
proteins
pubmed
7507926
uniprot
proteins
pubmed
7874121
uniprot
proteins
pubmed
7920629
uniprot
proteins
pubmed
9145798
uniprot
proteins
sequence_length
457
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305|PubMed:12975813, ECO:0000305|PubMed:17114051, ECO:0000305|PubMed:24801766}; Multi-pass membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:17114051, ECO:0000269|PubMed:24801766}. Perikaryon {ECO:0000269|PubMed:24801766}. Cell projection, dendrite {ECO:0000269|PubMed:24801766}. Cell membrane {ECO:0000269|PubMed:16672662, ECO:0000305|PubMed:9145798}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415, ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 251..272; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:O93430"; TRANSMEM 278..298; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:O93430"; TRANSMEM 310..330; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:O93430"; TRANSMEM 426..446; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:O93430
uniprot
proteins