{"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}}