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Q9CQ10 (CHMP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Charged multivesicular body protein 3
Alternative name(s):
Chromatin-modifying protein 3
Vacuolar protein sorting-associated protein 24
Gene names
Name:Chmp3
Synonyms:Vps24
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cytoplasmcytosol By similarity. Membrane; Lipid-anchor By similarity. Endosome By similarity. Late endosome membrane By similarity. Note: Localizes to the midbody of dividing cells By similarity.

Tissue specificity

Expressed in lung, testis, heart, spleen, skeletal muscle, kidney, liver and brain. Ref.4

Domain

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 similarities

Belongs to the SNF7 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 224223Charged multivesicular body protein 3
PRO_0000211481

Regions

Region2 – 113112Intramolecular interaction with C-terminus By similarity
Region59 – 646Important for autoinhibitory function By similarity
Region151 – 22474Interaction with VPS4A By similarity
Region151 – 22272Intramolecular interaction with N-terminus By similarity
Region168 – 1692Important for autoinhibitory function By similarity
Region196 – 22429Interaction with STAMBP By similarity
Region205 – 2095Interaction with STAMBP By similarity
Region223 – 2242Interaction with STAMBP By similarity
Coiled coil22 – 5433 Potential
Coiled coil149 – 22476 Potential
Motif201 – 21313MIT-interacting motif By similarity

Sites

Binding site2181STAMBP By similarity
Site481Important for autoinhibitory function By similarity

Amino acid modifications

Modified residue2001Phosphoserine Ref.3
Lipidation21N-myristoyl glycine Potential
Cross-link179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict71T → S in BAB26273. Ref.1
Sequence conflict1611A → V in BAB31306. Ref.1
Sequence conflict1701F → L in BAB31306. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CQ10 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DC1A566E86D82A07

FASTA22425,219
        10         20         30         40         50         60 
MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKEVC 

        70         80         90        100        110        120 
VVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI 

       130        140        150        160        170        180 
PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEA AEMEIDRILF EITAGALGKA 

       190        200        210        220 
PSKVTDALPE PEPAGAMAAS EEGEEEEDEE DLEAMQSRLA TLRS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS20232.1.
RefSeqNP_080059.2. NM_025783.3.
UniGeneMm.181278.

3D structure databases

ProteinModelPortalQ9CQ10.
SMRQ9CQ10. Positions 5-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211654. 3 interactions.
IntActQ9CQ10. 2 interactions.

PTM databases

PhosphoSiteQ9CQ10.

Proteomic databases

MaxQBQ9CQ10.
PaxDbQ9CQ10.
PRIDEQ9CQ10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059462; ENSMUSP00000109815; ENSMUSG00000053119.
ENSMUST00000065364; ENSMUSP00000068410; ENSMUSG00000053119.
GeneID66700.
KEGGmmu:66700.
UCSCuc009cgw.1. mouse.

Organism-specific databases

CTD51652.
MGIMGI:1913950. Chmp3.

Phylogenomic databases

eggNOGCOG5491.
GeneTreeENSGT00550000074896.
HOGENOMHOG000177219.
HOVERGENHBG107031.
InParanoidQ9CQ10.
KOK12193.
OMAMLDETMD.
OrthoDBEOG7D59Q2.
PhylomeDBQ9CQ10.
TreeFamTF105848.

Gene expression databases

BgeeQ9CQ10.
CleanExMM_VPS24.
GenevestigatorQ9CQ10.

Family and domain databases

InterProIPR005024. Snf7.
[Graphical view]
PfamPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio322405.
PROQ9CQ10.
SOURCESearch...

Entry information

Entry nameCHMP3_MOUSE
AccessionPrimary (citable) accession number: Q9CQ10
Secondary accession number(s): Q9D2Z2, Q9D7A5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot