CHMP3_PONAB
ID CHMP3_PONAB Reviewed; 222 AA.
AC Q5RAU5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Charged multivesicular body protein 3;
DE AltName: Full=Chromatin-modifying protein 3;
DE AltName: Full=Vacuolar protein sorting-associated protein 24;
GN Name=CHMP3; Synonyms=VPS24;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable core component of the endosomal sorting required for
CC transport complex III (ESCRT-III) which is involved in multivesicular
CC bodies (MVBs) formation and sorting of endosomal cargo proteins into
CC MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by
CC invagination and scission from the limiting membrane of the endosome
CC and mostly are delivered to lysosomes enabling degradation of membrane
CC proteins, such as stimulated growth factor receptors, lysosomal enzymes
CC and lipids. The MVB pathway appears to require the sequential function
CC of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC dissociate from the invaginating membrane before the ILV is released.
CC The ESCRT machinery also functions in topologically equivalent membrane
CC fission events, such as the terminal stages of cytokinesis and the
CC budding of enveloped viruses (lentiviruses). ESCRT-III proteins are
CC believed to mediate the necessary vesicle extrusion and/or membrane
CC fission activities, possibly in conjunction with the AAA ATPase VPS4.
CC Selectively binds to phosphatidylinositol 3,5-bisphosphate
CC PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other
CC phosphoinositides tested. Involved in late stages of cytokinesis. Plays
CC a role in endosomal sorting/trafficking of EGF receptor (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Probable core component of the endosomal sorting required for
CC transport complex III (ESCRT-III). ESCRT-III components are thought to
CC multimerize to form a flat lattice on the perimeter membrane of the
CC endosome. Several assembly forms of ESCRT-III may exist that interact
CC and act sequentially. Forms a metastable monomer in solution; its core
CC structure (without part of the putative autoinhibitory C-terminal
CC acidic region) oligomerizes into a flat lattice via two different
CC dimerization interfaces. In vitro, heteromerizes with CHMP2A (but not
CC CHMP4) to form helical tubular structures that expose membrane-
CC interacting sites on the outside whereas VPS4B can associate on the
CC inside of the tubule. May interact with IGFBP7; the relevance of such
CC interaction however remains unclear. Interacts with CHMP2A. Interacts
CC with CHMP4A; the interaction requires the release of CHMP4A
CC autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the
CC interaction appears to relieve the autoinhibition of CHMP3 (By
CC similarity). Interacts with VTA1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Endosome {ECO:0000250}. Late
CC endosome membrane {ECO:0000250}. Note=Localizes to the midbody of
CC dividing cells. {ECO:0000250}.
CC -!- DOMAIN: The acidic C-terminus and the basic N-termminus are thought to
CC render the protein in a closed, soluble and inactive conformation
CC through an autoinhibitory intramolecular interaction. The open and
CC active conformation, which enables membrane binding and
CC oligomerization, is achieved by interaction with other cellular binding
CC partners, probably including other ESCRT components.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858917; CAH91115.1; -; mRNA.
DR RefSeq; NP_001125653.1; NM_001132181.1.
DR AlphaFoldDB; Q5RAU5; -.
DR SMR; Q5RAU5; -.
DR STRING; 9601.ENSPPYP00000013615; -.
DR GeneID; 100172572; -.
DR KEGG; pon:100172572; -.
DR CTD; 51652; -.
DR eggNOG; KOG3229; Eukaryota.
DR HOGENOM; CLU_069208_0_1_1; -.
DR InParanoid; Q5RAU5; -.
DR OMA; INEMMDD; -.
DR OrthoDB; 1418709at2759; -.
DR TreeFam; TF105848; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:1904930; C:amphisome membrane; IEA:UniProt.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:UniProt.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProt.
DR GO; GO:0030496; C:midbody; IEA:UniProt.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProt.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProt.
DR GO; GO:0097352; P:autophagosome maturation; IEA:UniProt.
DR GO; GO:1902774; P:late endosome to lysosome transport; IEA:UniProt.
DR GO; GO:0061952; P:midbody abscission; IEA:UniProt.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IEA:UniProt.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:UniProt.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:UniProt.
DR GO; GO:0031468; P:nuclear membrane reassembly; IEA:UniProt.
DR GO; GO:0001778; P:plasma membrane repair; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:UniProt.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:UniProt.
DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProt.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProt.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Endosome;
KW Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..222
FT /note="Charged multivesicular body protein 3"
FT /id="PRO_0000211482"
FT REGION 2..113
FT /note="Intramolecular interaction with C-terminus"
FT /evidence="ECO:0000250"
FT REGION 59..64
FT /note="Important for autoinhibitory function"
FT /evidence="ECO:0000250"
FT REGION 151..222
FT /note="Interaction with VPS4A"
FT /evidence="ECO:0000250"
FT REGION 151..220
FT /note="Intramolecular interaction with N-terminus"
FT /evidence="ECO:0000250"
FT REGION 168..169
FT /note="Important for autoinhibitory function"
FT /evidence="ECO:0000250"
FT REGION 180..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..222
FT /note="Interaction with STAMBP"
FT /evidence="ECO:0000250"
FT REGION 203..207
FT /note="Interaction with STAMBP"
FT /evidence="ECO:0000250"
FT REGION 221..222
FT /note="Interaction with STAMBP"
FT /evidence="ECO:0000250"
FT COILED 22..54
FT /evidence="ECO:0000255"
FT COILED 141..222
FT /evidence="ECO:0000255"
FT MOTIF 201..211
FT /note="MIT-interacting motif"
FT /evidence="ECO:0000250"
FT SITE 48
FT /note="Important for autoinhibitory function"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Interaction with STAMBP"
FT /evidence="ECO:0000250"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E7"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E7"
SQ SEQUENCE 222 AA; 25049 MW; 83B2CDD41C584BD3 CRC64;
MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC
VVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI
PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEE AEMEIDRILF EITAGALGKA
PSKVTDALPE PEPSGAMAAS EDEEEEEEAL EAMQSRLATL RS
