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{
"metadata": {
"accession": "PR01920",
"entry_id": null,
"type": "family",
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"source_database": "prints",
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"integrated": "IPR017349",
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"name": {
"name": "Tumour necrosis factor receptor 3",
"short": "TNFACTORR3"
},
"description": [
{
"text": "<p> The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain - a region that contains many cysteine residues arranged in a specific repetitive pattern [7917108]. The cysteines allow formation of an extended rod-like structure, responsible for ligand binding [8387891]. </p> <p> Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences [15500863]. Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved [11239407,9826575]. </p> <p> TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis [15500863]. Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease [9826574]. </p> <p> TNF receptor 3 (also known as lymphotoxin-beta receptor) acts as a receptor for the heterotrimer of lymphotoxin-alpha and beta, and also for the TNF ligand LIGHT. Activation of the receptor promotes apoptosis via recruitment of TNFR-associated factor 3 (TRAF3) [9122217]. </p>",
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}
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"domain_architectures": 0,
"interactions": 0,
"matches": 1359,
"pathways": 0,
"proteins": 300,
"proteomes": 145,
"sets": 0,
"structural_models": {
"alphafold": 269,
"bfvd": 0
},
"structures": 0,
"taxa": 470
},
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"is_llm": false,
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}
}
