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Protein

Charged multivesicular body protein 3

Gene

Chmp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei48 – 481Important for autoinhibitory functionBy similarity
Binding sitei218 – 2181STAMBPBy similarity

GO - Molecular functioni

  1. phosphatidylcholine binding Source: MGI
  2. phosphatidylinositol-4,5-bisphosphate binding Source: Ensembl
  3. protein homodimerization activity Source: MGI
  4. ubiquitin-specific protease binding Source: MGI

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell separation after cytokinesis Source: MGI
  3. endosome to lysosome transport Source: Ensembl
  4. negative regulation of viral release from host cell Source: MGI
  5. positive regulation of cytokinesis Source: Ensembl
  6. positive regulation of viral release from host cell Source: MGI
  7. protein heterooligomerization Source: MGI
  8. protein polymerization Source: MGI
  9. protein transport Source: UniProtKB-KW
  10. regulation of centrosome duplication Source: MGI
  11. regulation of endosome size Source: Ensembl
  12. regulation of viral process Source: MGI
  13. viral budding via host ESCRT complex Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_334712. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 3
Alternative name(s):
Chromatin-modifying protein 3
Vacuolar protein sorting-associated protein 24
Gene namesi
Name:Chmp3
Synonyms:Vps24
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1913950. Chmp3.

Subcellular locationi

  1. Cytoplasmcytosol By similarity
  2. Membrane By similarity; Lipid-anchor By similarity
  3. Endosome By similarity
  4. Late endosome membrane By similarity

  5. Note: Localizes to the midbody of dividing cells.By similarity

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle Source: MGI
  2. cytosol Source: UniProtKB-SubCell
  3. early endosome Source: Ensembl
  4. ESCRT III complex Source: MGI
  5. extracellular vesicular exosome Source: MGI
  6. late endosome membrane Source: UniProtKB-SubCell
  7. midbody Source: Ensembl
  8. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedSequence Analysis
Chaini2 – 224223Charged multivesicular body protein 3PRO_0000211481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence Analysis
Cross-linki179 – 179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei200 – 2001Phosphoserine1 Publication

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9CQ10.
PaxDbiQ9CQ10.
PRIDEiQ9CQ10.

PTM databases

PhosphoSiteiQ9CQ10.

Expressioni

Tissue specificityi

Expressed in lung, testis, heart, spleen, skeletal muscle, kidney, liver and brain.1 Publication

Gene expression databases

BgeeiQ9CQ10.
CleanExiMM_VPS24.
GenevestigatoriQ9CQ10.

Interactioni

Subunit structurei

Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentally. Forms a metastable monomer in solution; its core structure (without part of the putative autoinhibitory C-terminal acidic region) oligomerizes into a flat lattice via two different dimerization interfaces. In vitro, heteromerizes with CHMP2A (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. May interact with IGFBP7; the relevance of such interaction however remains unclear. Interacts with CHMP2A. Interacts with CHMP4A; the interaction requires the release of CHMP4A autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the interaction appears to relieve the autoinhibition of CHMP3 (By similarity). Interacts with VTA1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi211654. 3 interactions.
IntActiQ9CQ10. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ10.
SMRiQ9CQ10. Positions 5-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 113112Intramolecular interaction with C-terminusBy similarityAdd
BLAST
Regioni59 – 646Important for autoinhibitory functionBy similarity
Regioni151 – 22474Interaction with VPS4ABy similarityAdd
BLAST
Regioni151 – 22272Intramolecular interaction with N-terminusBy similarityAdd
BLAST
Regioni168 – 1692Important for autoinhibitory functionBy similarity
Regioni196 – 22429Interaction with STAMBPBy similarityAdd
BLAST
Regioni205 – 2095Interaction with STAMBPBy similarity
Regioni223 – 2242Interaction with STAMBPBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili22 – 5433Sequence AnalysisAdd
BLAST
Coiled coili149 – 22476Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 21313MIT-interacting motifBy similarityAdd
BLAST

Domaini

The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components.

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5491.
GeneTreeiENSGT00550000074896.
HOGENOMiHOG000177219.
HOVERGENiHBG107031.
InParanoidiQ9CQ10.
KOiK12193.
OMAiQKDVCVI.
OrthoDBiEOG7D59Q2.
PhylomeDBiQ9CQ10.
TreeFamiTF105848.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQ10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD
60 70 80 90 100
AAKKGQKEVC VVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV
110 120 130 140 150
AGSLQKSTEV MKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES
160 170 180 190 200
MDDQEEMEEA AEMEIDRILF EITAGALGKA PSKVTDALPE PEPAGAMAAS
210 220
EEGEEEEDEE DLEAMQSRLA TLRS
Length:224
Mass (Da):25,219
Last modified:January 23, 2007 - v3
Checksum:iDC1A566E86D82A07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71T → S in BAB26273 (PubMed:16141072).Curated
Sequence conflicti161 – 1611A → V in BAB31306 (PubMed:16141072).Curated
Sequence conflicti170 – 1701F → L in BAB31306 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009414 mRNA. Translation: BAB26273.1.
AK014818 mRNA. Translation: BAB29566.1.
AK016677 mRNA. Translation: BAB30375.1.
AK018611 mRNA. Translation: BAB31306.1.
AK083562 mRNA. Translation: BAC38951.1.
BC049964 mRNA. Translation: AAH49964.1.
CCDSiCCDS20232.1.
RefSeqiNP_080059.2. NM_025783.3.
UniGeneiMm.181278.

Genome annotation databases

EnsembliENSMUST00000059462; ENSMUSP00000109815; ENSMUSG00000053119.
ENSMUST00000065364; ENSMUSP00000068410; ENSMUSG00000053119.
GeneIDi66700.
KEGGimmu:66700.
UCSCiuc009cgw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009414 mRNA. Translation: BAB26273.1.
AK014818 mRNA. Translation: BAB29566.1.
AK016677 mRNA. Translation: BAB30375.1.
AK018611 mRNA. Translation: BAB31306.1.
AK083562 mRNA. Translation: BAC38951.1.
BC049964 mRNA. Translation: AAH49964.1.
CCDSiCCDS20232.1.
RefSeqiNP_080059.2. NM_025783.3.
UniGeneiMm.181278.

3D structure databases

ProteinModelPortaliQ9CQ10.
SMRiQ9CQ10. Positions 5-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211654. 3 interactions.
IntActiQ9CQ10. 2 interactions.

PTM databases

PhosphoSiteiQ9CQ10.

Proteomic databases

MaxQBiQ9CQ10.
PaxDbiQ9CQ10.
PRIDEiQ9CQ10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059462; ENSMUSP00000109815; ENSMUSG00000053119.
ENSMUST00000065364; ENSMUSP00000068410; ENSMUSG00000053119.
GeneIDi66700.
KEGGimmu:66700.
UCSCiuc009cgw.1. mouse.

Organism-specific databases

CTDi51652.
MGIiMGI:1913950. Chmp3.

Phylogenomic databases

eggNOGiCOG5491.
GeneTreeiENSGT00550000074896.
HOGENOMiHOG000177219.
HOVERGENiHBG107031.
InParanoidiQ9CQ10.
KOiK12193.
OMAiQKDVCVI.
OrthoDBiEOG7D59Q2.
PhylomeDBiQ9CQ10.
TreeFamiTF105848.

Enzyme and pathway databases

ReactomeiREACT_334712. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

NextBioi322405.
PROiQ9CQ10.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ10.
CleanExiMM_VPS24.
GenevestigatoriQ9CQ10.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum, Testis and Tongue.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: 129.
    Tissue: Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. "Characterization of a novel alternatively spliced human transcript encoding an N-terminally truncated Vps24 protein that suppresses the effects of Bax in an ESCRT independent manner in yeast."
    Khoury C.M., Yang Z., Ismail S., Greenwood M.T.
    Gene 391:233-241(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiCHMP3_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ10
Secondary accession number(s): Q9D2Z2, Q9D7A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.