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{
"metadata": {
"accession": "PF21222",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "pfam",
"member_databases": null,
"integrated": "IPR048524",
"hierarchy": null,
"name": {
"name": "Lysosome-associated membrane glycoprotein 2, transmembrane segment",
"short": "Lamp2_2nd"
},
"description": [
{
"text": "<p>This domain is found in Lysosome-associated membrane glycoprotein 2 from humans (Lamp2) and similar proteins from vertebrates. Lamp2 is an integral membrane protein that plays an important role in chaperone-mediated autophagy (CMA), targeting pertinent proteins for lysosomal degradation. This protein is organised into two conserved luminal domains, a single transmembrane domain (this entry) and a short C-terminal cytosolic tail. It adopts a trimeric configuration, and the transmembrane domains of the three monomers form a three-helix bundle structure [[cite:PUB00151730]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00151730": {
"PMID": 25342746,
"ISBN": null,
"volume": "289",
"issue": "51",
"year": 2014,
"title": "Structure of transmembrane domain of lysosome-associated membrane protein type 2a (LAMP-2A) reveals key features for substrate specificity in chaperone-mediated autophagy.",
"URL": null,
"raw_pages": "35111-23",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Rout AK",
"Strub MP",
"Piszczek G",
"Tjandra N."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 37,
"interactions": 0,
"matches": 3025,
"pathways": 0,
"proteins": 3008,
"proteomes": 1121,
"sets": 0,
"structural_models": {
"alphafold": 2770,
"bfvd": 0
},
"structures": 4,
"taxa": 3883
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 2,
"alignment:full": 2077
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}