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IID50365
UniprotP36108
ProteinDOA4-independent degradation protein 4
GeneDID4
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
232
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 183-232 Hetero dimer : IID50372Complex
 Evidence X-RAY 2v6x B Reference
       Region 2v6x B 183-206 order
       Region 2v6x B 207-216 disorder
       Region 2v6x B 217-231 order
       Region 2v6x B 232-232 disorder
SeqProS predicted 183-206,217-231 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950). Hetero dimer : IID50372Complex
       Region 2v6x B 183-206 order
       Region 2v6x B 217-231 order
 
Prediction
NeProc
Disorder 1-10,91-168,174-232
Order 11-90,169-173
ProS 1-10,91-152,165-168,174-187,218-232
AlphaFold
Disorder 1-11,117-121,146-146,150-159,188-217,231-232
Order 12-116,122-145,147-149,160-187,218-230
Pfam Hmmer
PF03357 20-191 1.3e-35
SEG 22-46 ,156-166
Function
Function in SwissProt
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.
Biological Process
See also
Diagram with PDB data
VPS4/VTA1/DID4Vps4p-Vta1p complex with peptide binding to the central pore of Vps4p