"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PF21222"	"{'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}"	"{}"	"[{'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}]"	""	""	""	"IPR048524"	False	False	False	"{'PUB00151730': {'PMID': 25342746, 'ISBN': None, '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': None, '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': None}}"	""	"{'name': 'Lysosome-associated membrane glycoprotein 2, transmembrane segment', 'short': 'Lamp2_2nd'}"	""	""	""	"pfam"	"domain"	""