20250201 IID50365 DOA4-independent degradation protein 4 ESCRT-III complex subunit VPS2 Vacuolar protein-sorting-associated protein 2 Vacuolar protein-targeting protein 14 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 232 P36108 D6VXT5 Required 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 motif 219 229 0 0 DID4 DOA4-independent degradation pro MSLFEWVFGKNVTPQERLKKNQRALERTQRELEREKRKLELQDKKLVSEIKKSAKNGQVAAAKVQAKDLVRTRNYIQKFDNMKAQLQAISLRIQAVRSSDQMTRSMSEATGLLAGMNRTMNLPQLQRISMEFEKQSDLMGQRQEFMDEAIDNVMGDEVDEDEEADEIVNKVLDEIGVDLNSQLQSTPQNLVSNAPIAETAMGIPEPIGAGSEFHGNPDDDLQARLNTLKKQT 1 2v6xB 183 206 order 1 2 2v6xB 207 216 disorder 1 3 2v6xB 217 231 order 1 4 2v6xB 232 232 disorder 1 1 2v6x X-RAY 17928861 T.OBITA,S.SAKSENA,S.GHAZI-TABATABAI,D.J.GILL,O.PERISIC,S.D.EMR,R.L.WILLIAMS STRUCTURAL BASIS FOR SELECTIVE RECOGNITION OF ESCRT-III BY THE AAA ATPASE VPS4 2007 NATURE 449 735 x-ray 2v6x B 183 232 98 2 207 216 232 232 1 2v6x_1 4064 Hetero dimer 2v6xB P36108 IID50365 2v6xA P52917 IID50372 2v6xB-2v6xA ProS 1 predicted 1 183 206 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). ProS 2 possible 3 217 231 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950).
P52917-1 VPS4/VTA1/DID4 Vps4p-Vta1p complex with peptide binding to the central pore of Vps4p
12-116,122-145,147-149,160-187,218-230 1-11,117-121,146-146,150-159,188-217,231-232 11-90,169-173 1-10,91-168,174-232 1-10,91-152,165-168,174-187,218-232 22-46,156-166