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IID00887
UniprotQ9NZZ3
ProteinCharged multivesicular body protein 5
GeneCHMP5
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
219
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 139-195 Hetero trimer : IID00881Complex
 Evidence X-RAY 4txr C Reference
       Region 4txr C 139-150 disorder
       Region 4txr C 151-190 order
       Region 4txr C 191-195 disorder
Seq 139-195 Hetero dimer : IID00881Complex
 Evidence NMR 2lxm B Reference
       Region 2lxm B 139-153 disorder
       Region 2lxm B 154-189 order
       Region 2lxm B 190-195 disorder
Seq 151-219 Hetero dimer : Q5VW32
 Evidence X-RAY 3uly B Reference
       Region 3uly B 151-199 disorder
       Region 3uly B 200-216 order
       Region 3uly B 217-219 disorder
 Evidence X-RAY 3um0 B Reference
       Region 3um0 B 200-217 order
       Region 3um0 B 218-219 disorder
Seq 151-219 Hetero tetramer : Q5VW32
 Evidence X-RAY 3um1 E Reference
       Region 3um1 E 151-199 disorder
       Region 3um1 E 200-216 order
       Region 3um1 E 217-219 disorder
 Evidence X-RAY 3um1 B Reference
       Region 3um1 B 151-199 disorder
       Region 3um1 B 200-216 order
       Region 3um1 B 217-219 disorder
 Evidence X-RAY 3um2 E Reference
       Region 3um2 E 200-216 order
       Region 3um2 E 217-219 disorder
 Evidence X-RAY 3um2 B Reference
       Region 3um2 B 200-216 order
       Region 3um2 B 217-219 disorder
SeqProS verified 151-190 Hetero trimer : IID00881Complex
       Region 4txr C 151-190 order
       Region 3uly B 151-199 disorder
SeqProS verified 151-190 Hetero dimer : IID00881Complex
       Region 2lxm B 154-189 order
       Region 3uly B 151-199 disorder
SeqProS possible 200-217 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950). Hetero tetramer : Q5VW32
       Region 3um2 B 200-216 order
       Region 3um2 E 200-216 order
       Region 3um1 B 200-216 order
       Region 3um1 E 200-216 order
SeqProS possible 200-217 Same region of the homolog (Q9Y3E7, CHMP3) is disordered in the free state (PubMed=21827950). Hetero dimer : Q5VW32
       Region 3um0 B 200-217 order
       Region 3uly B 200-216 order
Seqphosphorylation
    86-86 Phosphoserine
 
Prediction
NeProc
Disorder 1-27,56-57,156-219
Order 28-55,58-155
ProS 1-8,16-27,56-57,156-172,180-194,208-219
AlphaFold
Disorder 1-11,123-126,148-158,170-200,217-219
Order 12-122,127-147,159-169,201-216
Pfam Hmmer
PF03357 12-197 3.2e-84
SEG 125-137 ,157-179
Function
Function in SwissProt
Probable peripherally associated 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) (PubMed:14519844). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release (PubMed:14519844).