20250201IID50365DOA4-independent degradation protein 4ESCRT-III complex subunit VPS2Vacuolar protein-sorting-associated protein 2Vacuolar protein-targeting protein 14Saccharomyces cerevisiae (strain ATCC 204508 / S288c)232P36108D6VXT5Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Can directly stimulate VPS4 ATPase activity. The DID4/VPS2-VPS24 subcomplex is required for the VPS4-dependent dissociation of ESCRT-III.MIT-interacting motif21922900DID4DOA4-independent degradation proMSLFEWVFGKNVTPQERLKKNQRALERTQRELEREKRKLELQDKKLVSEIKKSAKNGQVAAAKVQAKDLVRTRNYIQKFDNMKAQLQAISLRIQAVRSSDQMTRSMSEATGLLAGMNRTMNLPQLQRISMEFEKQSDLMGQRQEFMDEAIDNVMGDEVDEDEEADEIVNKVLDEIGVDLNSQLQSTPQNLVSNAPIAETAMGIPEPIGAGSEFHGNPDDDLQARLNTLKKQT12v6xB183206order122v6xB207216disorder132v6xB217231order142v6xB232232disorder112v6xX-RAY17928861T.OBITA,S.SAKSENA,S.GHAZI-TABATABAI,D.J.GILL,O.PERISIC,S.D.EMR,R.L.WILLIAMSSTRUCTURAL BASIS FOR SELECTIVE RECOGNITION OF ESCRT-III BY THE AAA ATPASE VPS42007NATURE449735x-ray2v6xB18323298220721623223212v6x_14064Hetero dimer2v6xBP36108IID503652v6xAP52917IID503722v6xB-2v6xAProS1predicted1183206This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5).ProS2possible3217231Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950).P52917-1VPS4/VTA1/DID4Vps4p-Vta1p complex with peptide binding to the central pore of Vps4p12-116,122-145,147-149,160-187,218-2301-11,117-121,146-146,150-159,188-217,231-23211-90,169-1731-10,91-168,174-2321-10,91-152,165-168,174-187,218-23222-46,156-166