GLRA1
entrez
2741
canonical
uniprot
P23415
canonical
ensembl
ENSG00000145888
resolver
ensp
ENSP00000274576
resolver
ensp
ENSP00000411593
resolver
genesymbol
GLRA1
resolver
hgnc
HGNC:4326
resolver
uniprot
B2R6T3
resolver
uniprot
Q14C71
resolver
uniprot
Q14C77
resolver
uniprot
Q6DJV9
resolver
uniprot_entry
GLRA1_HUMAN
resolver
uniprot_entry
Q14C71_HUMAN
resolver
uniprot_sec
B2R6T3
resolver
uniprot_sec
Q14C77
resolver
uniprot_sec
Q6DJV9
resolver
activity_regulation
ACTIVITY REGULATION: Channel opening is triggered by extracellular glycine (PubMed:16144831, PubMed:2155780, PubMed:22715885, PubMed:37821459). Channel characteristics depend on the subunit composition; heteropentameric channels are activated by lower glycine levels and display faster desensitization (PubMed:14551753). Channel opening is also triggered by taurine and beta-alanine (PubMed:16144831, PubMed:9009272). Channel activity is potentiated by nanomolar concentrations of Zn(2+); half-maximal activation is observed with 37 nM Zn(2+) (PubMed:16144831). Inhibited by higher Zn(2+) levels; haf-maximal inhibition occurs at 20 uM Zn(2+) (PubMed:16144831). Inhibited by strychnine (PubMed:16144831, PubMed:2155780, PubMed:25445488). Strychnine binding locks the channel in a closed conformation and prevents channel opening in response to extracellular glycine (By similarity). Inhibited by lindane (PubMed:25445488). Inhibited by picrotoxin (PubMed:22715885, PubMed:23994010, PubMed:25730860). {ECO:0000250|UniProtKB:O93430, ECO:0000269|PubMed:14551753, ECO:0000269|PubMed:16144831, ECO:0000269|PubMed:2155780, ECO:0000269|PubMed:22715885, ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25445488, ECO:0000269|PubMed:25730860, ECO:0000269|PubMed:37821459, ECO:0000269|PubMed:9009272}.
uniprot
proteins
amino_acid_sequence
MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ
uniprot
proteins
disease_involvement
DISEASE: Hyperekplexia 1 (HKPX1) [MIM:149400]: A neurologic disorder characterized by muscular rigidity of central nervous system origin, particularly in the neonatal period, and by an exaggerated startle response to unexpected acoustic or tactile stimuli. {ECO:0000269|PubMed:10514101, ECO:0000269|PubMed:24108130, ECO:0000269|PubMed:25730860, ECO:0000269|PubMed:7611730, ECO:0000269|PubMed:7881416, ECO:0000269|PubMed:7925268, ECO:0000269|PubMed:7981700, ECO:0000269|PubMed:8298642, ECO:0000269|PubMed:8571969, ECO:0000269|PubMed:8733061, ECO:0000269|PubMed:9009272, ECO:0000269|PubMed:9067762, ECO:0000269|PubMed:9920650, ECO:0000269|Ref.20}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Subunit of heteromeric glycine-gated chloride channels (PubMed:14551753, PubMed:23994010, PubMed:25730860, PubMed:37821459). Plays an important role in the down-regulation of neuronal excitability (PubMed:8298642, PubMed:9009272). Contributes to the generation of inhibitory postsynaptic currents (PubMed:25445488). Channel activity is potentiated by ethanol (PubMed:25973519). Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol (By similarity). {ECO:0000250|UniProtKB:Q64018, ECO:0000269|PubMed:14551753, ECO:0000269|PubMed:16144831, ECO:0000269|PubMed:2155780, ECO:0000269|PubMed:22715885, ECO:0000269|PubMed:22973015, ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25445488, ECO:0000269|PubMed:25730860, ECO:0000269|PubMed:25973519, ECO:0000269|PubMed:7920629, ECO:0000269|PubMed:7925268, ECO:0000269|PubMed:9009272, ECO:0000305|PubMed:8298642}.
uniprot
proteins
mass_dalton
52624
uniprot
proteins
mutagenesis
MUTAGEN 80; /note="A->S: The mutant channel requires much higher glycine concentrations for activation."; /evidence="ECO:0000269|PubMed:7920629"; MUTAGEN 137; /note="H->F: Abolishes sensitivity of channel activity to potentiation or inhibition by Zn(2+); when associated with K-222."; /evidence="ECO:0000269|PubMed:16144831"; MUTAGEN 137; /note="H->N: Strongly decreases sensitivity to inhibition by Zn(2+)."; /evidence="ECO:0000269|PubMed:16144831"; MUTAGEN 220; /note="E->A: Abolishes potentiation of channel activity by Zn(2+)."; /evidence="ECO:0000269|PubMed:16144831"; MUTAGEN 222; /note="D->A: Abolishes potentiation of channel activity by Zn(2+)."; /evidence="ECO:0000269|PubMed:16144831"; MUTAGEN 222; /note="D->K: Abolishes sensitivity of channel activity to potentiation or inhibition by Zn(2+); when associated with F-137."; /evidence="ECO:0000269|PubMed:16144831"; MUTAGEN 243; /note="H->A: Strongly decreases potentiation of channel activity by Zn(2+)."; /evidence="ECO:0000269|PubMed:16144831"; MUTAGEN 282; /note="G->A: Increased single-channel conductance. No effect on glycine sensitivity, but decreased rate of activation."; /evidence="ECO:0000269|PubMed:25730860"; MUTAGEN 304; /note="K->C: Decreases channel conductance; the mutant channel requires much higher glycine concentrations for activation."; /evidence="ECO:0000269|PubMed:25730860
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
10514101
uniprot
proteins
pubmed
12667090
uniprot
proteins
pubmed
14551753
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15952785
uniprot
proteins
pubmed
16144831
uniprot
proteins
pubmed
19861413
uniprot
proteins
pubmed
2155780
uniprot
proteins
pubmed
22715885
uniprot
proteins
pubmed
22973015
uniprot
proteins
pubmed
23994010
uniprot
proteins
pubmed
24108130
uniprot
proteins
pubmed
25445488
uniprot
proteins
pubmed
25730860
uniprot
proteins
pubmed
25973519
uniprot
proteins
pubmed
35526563
uniprot
proteins
pubmed
37821459
uniprot
proteins
pubmed
7611730
uniprot
proteins
pubmed
7881416
uniprot
proteins
pubmed
7920629
uniprot
proteins
pubmed
7925268
uniprot
proteins
pubmed
7981700
uniprot
proteins
pubmed
8298642
uniprot
proteins
pubmed
8571969
uniprot
proteins
pubmed
8733061
uniprot
proteins
pubmed
9009272
uniprot
proteins
pubmed
9067762
uniprot
proteins
pubmed
9920650
uniprot
proteins
sequence_length
457
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q64018}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q64018}. Synapse {ECO:0000250|UniProtKB:Q64018}. Perikaryon {ECO:0000250|UniProtKB:Q64018}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q64018}. Cell membrane {ECO:0000269|PubMed:14551753, ECO:0000269|PubMed:16144831, ECO:0000269|PubMed:2155780, ECO:0000269|PubMed:22715885, ECO:0000269|PubMed:22973015, ECO:0000269|PubMed:24108130, ECO:0000269|PubMed:25445488, ECO:0000269|PubMed:25730860, ECO:0000269|PubMed:25973519, ECO:0000269|PubMed:7920629, ECO:0000269|PubMed:7925268, ECO:0000269|PubMed:9009272}; Multi-pass membrane protein {ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25730860, ECO:0000305|PubMed:2155780}.
uniprot
proteins
transmembrane_region
TRANSMEM 251..272; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25730860"; TRANSMEM 278..298; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25730860"; TRANSMEM 310..330; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25730860"; TRANSMEM 426..446; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:23994010
uniprot
proteins