{"metadata":{"accession":"PF10240","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR023341","hierarchy":null,"name":{"name":"MABP domain","short":"MABP"},"description":[{"text":"<p>This domain is found in the N-terminal region of MVB12 proteins, which are subunits of the ESCRT-I complex involved in multivesicular body formation. The MABP domain adopts a type-I beta-prism fold with internal three-fold symmetry, consisting of three homologous segments  each forming a three-stranded beta-sheet. It is found in diverse proteins including vertebrate DENND4A/B/C, Drosophila Crag, and bacterial MACPF-like proteins. The domain is believed to function as a membrane-associated adaptor that links other domains to vesicular membranes during intracellular trafficking. Most eukaryotic versions contain conserved cysteine residues in the first and third subdomains [[cite:PUB00045017],[cite:PUB00054220]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00054220":{"PMID":20448139,"ISBN":null,"volume":"26","issue":"12","year":2010,"title":"UMA and MABP domains throw light on receptor endocytosis and selection of endosomal cargoes.","URL":null,"raw_pages":"1477-80","medline_journal":"Bioinformatics","ISO_journal":"Bioinformatics","authors":["de Souza RF","Aravind L."],"DOI_URL":"http://dx.doi.org/10.1093/bioinformatics/btq235"},"PUB00078904":{"PMID":24284069,"ISBN":null,"volume":"127","issue":"Pt 3","year":2014,"title":"The molecular basis for selective assembly of the UBAP1-containing endosome-specific ESCRT-I complex.","URL":null,"raw_pages":"663-72","medline_journal":"J Cell Sci","ISO_journal":"J. Cell. Sci.","authors":["Wunderley L","Brownhill K","Stefani F","Tabernero L","Woodman P."],"DOI_URL":"http://dx.doi.org/10.1242/jcs.140673"},"PUB00044885":{"PMID":16895919,"ISBN":null,"volume":"281","issue":"39","year":2006,"title":"CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP.","URL":null,"raw_pages":"28919-31","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Konishi H","Tashiro K","Murata Y","Nabeshi H","Yamauchi E","Taniguchi H."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M605693200"},"PUB00078903":{"PMID":20654576,"ISBN":null,"volume":"399","issue":"2","year":2010,"title":"Distinct functions of human MVB12A and MVB12B in the ESCRT-I dependent on their posttranslational modifications.","URL":null,"raw_pages":"232-7","medline_journal":"Biochem Biophys Res Commun","ISO_journal":"Biochem. Biophys. Res. Commun.","authors":["Tsunematsu T","Yamauchi E","Shibata H","Maki M","Ohta T","Konishi H."],"DOI_URL":"http://dx.doi.org/10.1016/j.bbrc.2010.07.060"},"PUB00045017":{"PMID":17717151,"ISBN":null,"volume":"317","issue":"5844","year":2007,"title":"A common fold mediates vertebrate defense and bacterial attack.","URL":null,"raw_pages":"1548-51","medline_journal":"Science","ISO_journal":"Science","authors":["Rosado CJ","Buckle AM","Law RH","Butcher RE","Kan WT","Bird CH","Ung K","Browne KA","Baran K","Bashtannyk-Puhalovich TA","Faux NG","Wong W","Porter CJ","Pike RN","Ellisdon AM","Pearce MC","Bottomley SP","Emsley J","Smith AI","Rossjohn J","Hartland EL","Voskoboinik I","Trapani JA","Bird PI","Dunstone MA","Whisstock JC."],"DOI_URL":"http://dx.doi.org/10.1126/science.1144706"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":65,"interactions":0,"matches":5672,"pathways":0,"proteins":5658,"proteomes":1228,"sets":0,"structural_models":{"alphafold":1252},"structures":2,"taxa":4000},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":3,"alignment:full":4466},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3tow","name":"Crystal Structure of the MABP Domain of MVB12B of Human ESCRT-I Complex"}}}