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{
"metadata": {
"accession": "cd19004",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "cdd",
"member_databases": null,
"integrated": null,
"hierarchy": null,
"name": {
"name": "extracellular domain of gamma-aminobutyric acid receptor subunit pi (GABRP)",
"short": "LGIC_ECD_GABAAR_pi"
},
"description": [
{
"text": "<p>This family contains extracellular domain of pi subunit of type-A gamma-aminobutyric acid receptor (GABAAR). GABAAR is an anionic channel, mediating fast inhibitory synaptic transmission. Upon gamma-aminobutyric acid (GABA) binding to the ligand binding site on ECD, Cl- ions are selectively conducted through the GABAAR pore, resulting in hyperpolarization of the neuron. GABAAR is the principal mediator of rapid inhibitory synaptic transmission in the human brain. A decline in GABAAR signaling triggers hyperactive neurological disorders such as insomnia, anxiety, and epilepsy. GABRP is expressed mainly in non-neuronal tissues such as the mammary gland, prostate gland, lung, thymus, and uterus. It is also highly expressed in certain types of cancer such as basal-like breast cancer and pancreatic ductal adenocarcinoma. GABRP is involved in inhibitory synaptic transmission in the central nervous system. Its assembly with other GABAAR subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone. Studies suggest that polymorphisms in the GABRP gene may be associated with the susceptibility to systematic lupus erythematosus (SLE). [[cite:PUB00019920]]</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00019920": {
"PMID": 11357122,
"ISBN": null,
"volume": "411",
"issue": "6835",
"year": 2001,
"title": "Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors.",
"URL": null,
"raw_pages": "269-76",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Brejc K",
"van Dijk WJ",
"Klaassen RV",
"Schuurmans M",
"van Der Oost J",
"Smit AB",
"Sixma TK."
],
"DOI_URL": "http://dx.doi.org/10.1038/35077011"
}
},
"set_info": {
"accession": "cl28912",
"name": "LGIC_ECD"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 582,
"pathways": 0,
"proteins": 582,
"proteomes": 286,
"sets": 1,
"structural_models": {
"alphafold": 544,
"bfvd": 0
},
"structures": 1,
"taxa": 1056
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
