P24524
uniprot
P24524
canonical
activity_regulation
ACTIVITY REGULATION: Low levels of Zn(2+) ions (1 uM) increase glycine sensitivity and decrease the glycine concentration required for half-maximal channel activity (PubMed:23895467). Channel activity is strongly enhanced by ethanol (PubMed:23895467). Inhibited by picrotoxin (PubMed:23834509). Inhibited by prostaglandin E2, probably via PKA-mediated phosphorylation at Ser-379 (PubMed:15131310). {ECO:0000269|PubMed:15131310, ECO:0000269|PubMed:23834509, ECO:0000269|PubMed:23895467}.
uniprot
proteins
amino_acid_sequence
MAHVRHFRTLLSGFYFWEAALLLSLVATKETNSARSRSAPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFINSFGSIAETTMDYRVNIFLRQKWNDPRLAYSEYPDDSLDLDPSMLDSIWKPDLFFANEKGANFHEVTTDNKLLRIFKNGNVLYSIRLTLTLSCPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQDEAPVQVAEGLTLPQFLLKEEKDLRYCTKHYNTGKFTCIEVRFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRKNKTEAFALEKFYRFSDTDDEVRESRLSFTAYGMGPCLQAKDGVVPKGPNHAVQVMPKSADEMRKVFIDRAKKIDTISRACFPLAFLIFNIFYWVIYKILRHEDIHHQQD
uniprot
proteins
function
FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:15131310, PubMed:23613537, PubMed:23834509, PubMed:23895467). Channel characteristics depend on the subunit composition; heteropentameric channels display faster channel closure (PubMed:25445488). Plays an important role in the down-regulation of neuronal excitability (By similarity). Contributes to the generation of inhibitory postsynaptic currents (PubMed:25445488). Contributes to increased pain perception in response to increased prostaglandin E2 levels (By similarity). Plays a role in cellular responses to ethanol (PubMed:23895467). {ECO:0000250|UniProtKB:Q91XP5, ECO:0000269|PubMed:15131310, ECO:0000269|PubMed:23834509, ECO:0000269|PubMed:23895467, ECO:0000269|PubMed:25445488}.
uniprot
proteins
mass_dalton
53672
uniprot
proteins
mutagenesis
MUTAGEN 218; /note="P->L: Strongly enhances glycine sensitivity so that the channel starts to be activated at 0.001 mM glycine."; /evidence="ECO:0000269|PubMed:23895467"; MUTAGEN 379; /note="S->A: Loss of a predicted PKA phosphorylation site. Nearly abolishes down-regulation of inhibitory postsynaptic currents by prostaglandin E2."; /evidence="ECO:0000269|PubMed:15131310"; MUTAGEN 379; /note="S->E: Phosphomimetic mutant that triggers a local conformation change."; /evidence="ECO:0000269|PubMed:23834509"; MUTAGEN 379; /note="S->G: Loss of a predicted PKA phosphorylation site. Abolishes the conformation change observed after treatment with forskolin."; /evidence="ECO:0000269|PubMed:23834509
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PKA; this causes down-regulation of channel activity (Probable). {ECO:0000305|PubMed:15131310, ECO:0000305|PubMed:23834509}.
uniprot
proteins
protein_family
GLRA3 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
15131310
uniprot
proteins
pubmed
19723286
uniprot
proteins
pubmed
2176214
uniprot
proteins
pubmed
23613537
uniprot
proteins
pubmed
23834509
uniprot
proteins
pubmed
23895467
uniprot
proteins
pubmed
25445488
uniprot
proteins
sequence_length
464
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305|PubMed:19723286}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75311}. Perikaryon {ECO:0000269|PubMed:19723286}. Cell projection, dendrite {ECO:0000269|PubMed:19723286}. Synapse {ECO:0000269|PubMed:19723286}. Cell membrane {ECO:0000269|PubMed:15131310, ECO:0000269|PubMed:19723286, ECO:0000269|PubMed:23613537, ECO:0000269|PubMed:23834509, ECO:0000269|PubMed:23895467, ECO:0000269|PubMed:25445488}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75311}. Note=Partially colocalizes with GPHN that is known to mediate receptor clustering at postsynaptic membranes. {ECO:0000269|PubMed:19723286}.
uniprot
proteins
transmembrane_region
TRANSMEM 256..277; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:O75311"; TRANSMEM 283..303; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:O75311"; TRANSMEM 315..335; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:O75311"; TRANSMEM 431..451; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:O75311
uniprot
proteins