Descriptions

CHMP3 is a 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. The autoinhibition of CHMP3 is regulated through the intramolecular interactions between N-terminal basic domain and C-terminal acidic domain. The binding of the endosome-associated ubiquitin isopeptidase (AMSH) to the acidic half relieves the autoinhibition of CHMP3. CHMP3 can be induced to block HIV-1 release (Anti-HIV-1 budding activity) by coexpressing AMSH or by truncating the acidic domain.

Autoinhibitory domains (AIDs)

Target domain

1-150 (N-terminal domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6NY88

Entry ID Method Resolution Chain Position Source
AF-Q6NY88-F1 Predicted AlphaFoldDB

No variants for Q6NY88

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6NY88

No associated diseases with Q6NY88

No regional properties for Q6NY88

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q6NY88

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytosol
  • Membrane ; Lipid-anchor
  • Endosome
  • Late endosome membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
ESCRT III complex A complex with membrane scission activity that plays a major role in many processes where membranes are remodelled - including endosomal transport (vesicle budding), nuclear envelope organisation (membrane closure, mitotic bridge cleavage), and cytokinesis (abscission).
late endosome membrane The lipid bilayer surrounding a late endosome.
multivesicular body A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

3 GO annotations of biological process

Name Definition
endosome transport via multivesicular body sorting pathway The directed movement of substances from endosomes to lysosomes or vacuoles by a pathway in which molecules are sorted into multivesicular bodies, which then fuse with the target compartment.
late endosome to vacuole transport The directed movement of substances from late endosomes to the vacuole. In yeast, after transport to the prevacuolar compartment, endocytic content is delivered to the late endosome and on to the vacuole. This pathway is analogous to endosome to lysosome transport.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q58CS7 CHMP3 Charged multivesicular body protein 3 Bos taurus (Bovine) SS
Q9Y3E7 CHMP3 Charged multivesicular body protein 3 Homo sapiens (Human) EV
Q9CQ10 Chmp3 Charged multivesicular body protein 3 Mus musculus (Mouse) SS
Q8CGS4 Chmp3 Charged multivesicular body protein 3 Rattus norvegicus (Rat) SS
Q5BKM3 chmp3 Charged multivesicular body protein 3 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
Q7ZVB1 chmp1b Charged multivesicular body protein 1b Danio rerio (Zebrafish) (Brachydanio rerio) PR
Q7ZW25 chmp2a Charged multivesicular body protein 2a Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MGLFGKTQEK PPKDLINEWS LKIRKEMRVI DRQIRDIQRE EEKVKRSIKD AAKKGQKDVC
70 80 90 100 110 120
IILAKEMIQS KRAINKLYAS KAQMNSVLLS MKNQLSVLRV AGALQKSTEV MKAMQSLVKI
130 140 150 160 170 180
PEIQATMRDL SKEMMKAGII EEMLEDTLEG MDDEEEMEEA AEAEVDKILF EITAGALGKA
190 200 210 220
PSKVTDLPDP VAIGATAAPE EESEEEEEIE EMQSRLAALR S