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IID00230
UniprotQ9Y3E7
ProteinCharged multivesicular body protein 3
GeneCHMP3
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
222
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-222 Monomer :
 Evidence X-RAY 3frt A Reference
       Region 3frt A 8-11 disorder
       Region 3frt A 12-98 order
       Region 3frt A 99-102 disorder
       Region 3frt A 103-140 order
       Region 3frt A 141-156 disorder
       Region 3frt A 157-172 order
       Region 3frt A 173-222 disorder
 Evidence X-RAY 3frt B Reference
       Region 3frt B 8-11 disorder
       Region 3frt B 12-98 order
       Region 3frt B 99-101 disorder
       Region 3frt B 102-140 order
       Region 3frt B 141-156 disorder
       Region 3frt B 157-172 order
       Region 3frt B 173-222 disorder
 Evidence X-RAY 3frv A Reference
       Region 3frv A 1-7 disorder
       Region 3frv A 8-140 order
       Region 3frv A 141-150 disorder
Seq 9-183 Homo dimer :
 Evidence X-RAY 2gd5 A Reference
       Region 2gd5 A 9-11 disorder
       Region 2gd5 A 12-141 order
       Region 2gd5 A 142-160 disorder
       Region 2gd5 A 161-172 order
       Region 2gd5 A 173-183 disorder
 Evidence X-RAY 2gd5 B Reference
       Region 2gd5 B 9-140 order
       Region 2gd5 B 141-160 disorder
       Region 2gd5 B 161-180 order
       Region 2gd5 B 181-183 disorder
 Evidence X-RAY 2gd5 C Reference
       Region 2gd5 C 9-11 disorder
       Region 2gd5 C 12-98 order
       Region 2gd5 C 99-101 disorder
       Region 2gd5 C 102-140 order
       Region 2gd5 C 141-160 disorder
       Region 2gd5 C 161-176 order
       Region 2gd5 C 177-183 disorder
 Evidence X-RAY 2gd5 D Reference
       Region 2gd5 D 9-141 order
       Region 2gd5 D 142-156 disorder
       Region 2gd5 D 157-181 order
       Region 2gd5 D 182-183 disorder
Seqdisorder 183-222
 Evidence CD Reference
       Region 183-222 disorder
Seq 183-222 Hetero tetramer : IID00261Complex
 Evidence X-RAY 2xze Q Reference
       Region 2xze Q 183-199 disorder
       Region 2xze Q 200-222 order
 Evidence X-RAY 2xze R Reference
       Region 2xze R 183-202 disorder
       Region 2xze R 203-222 order
SeqProS verified 200-222 This region contains the ESCRT-III MIT domain interacting motif. Hetero tetramer : IID00261Complex
       Region 2xze Q 200-222 order
       Region 2xze R 203-222 order
       Region 183-222 disorder
Seqphosphorylation
    200-200 Phosphoserine
 
Prediction
NeProc
Disorder 1-10,99-110,122-222
Order 11-98,111-121
ProS 1-10,99-110,122-143,162-177,210-222
AlphaFold
Disorder 1-9,144-160,178-178,180-205,222-222
Order 10-143,161-177,179-179,206-221
Pfam Hmmer
PF03357 18-188 2.5e-57
SEG 149-166 ,196-212
Function
Function in SwissProt
Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells.