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Q8VEJ9 (VPS4A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. 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:
Vacuolar protein sorting-associated protein 4A

EC=3.6.4.6
Gene names
Name:Vps4a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. 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. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Involved in cytokinesis By similarity.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT-III substrates are translocated in an ATP-dependent manner. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP6. Interacts with VPS4B; the interaction suggests a heteromeric assembly with VPS4B. Interacts with SPAST. Interacts with IST1 By similarity. Ref.1

Subcellular location

Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane; Peripheral membrane protein By similarity. Note: Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body By similarity. Ref.1

Tissue specificity

Highly expressed in testis and moderately in heart and brain. Not detected in spleen, lung, liver, skeletal muscle or kidney. Ref.1

Domain

The MIT domain serves as an adapter for ESCRT-III proteins. It forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT interacting motif) helices along the groove between MIT helices 2 and 3 present in a subset of ESCRT-III proteins thus establishing the canonical MIM-MIT interaction. In an extended conformation along the groove between helices 1 and 3, also binds to a type-2 MIT interacting motif (MIM2) By similarity.

Sequence similarities

Belongs to the AAA ATPase family.

Contains 1 MIT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 437436Vacuolar protein sorting-associated protein 4A
PRO_0000084766

Regions

Domain2 – 8079MIT
Nucleotide binding167 – 1748ATP Potential
Coiled coil15 – 3723 Potential

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue81N6-acetyllysine By similarity

Experimental info

Mutagenesis2281E → Q: Perinuclear localization. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VEJ9 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B67CF13F7AFD9129

FASTA43748,907
        10         20         30         40         50         60 
MTTSTLQKAI DLVTKATEED KAKNYEEALR LYQHAVEYFL HAIKYEAHSD KAKESIRAKC 

        70         80         90        100        110        120 
MQYLDRAEKL KDYLRNKEKH GKKPVKENQS EGKGSDSDSE GDNPEKKKLQ EQLMGAVVME 

       130        140        150        160        170        180 
KPNIRWNDVA GLEGAKEALK EAVILPIKFP HLFTGKRTPW RGILLFGPPG TGKSYLAKAV 

       190        200        210        220        230        240 
ATEANNSTFF SVSSSDLMSK WLGESEKLVK NLFELARQHK PSIIFIDEVD SLCGSRNENE 

       250        260        270        280        290        300 
SEAARRIKTE FLVQMQGVGN NNDGTLVLGA TNIPWVLDSA IRRRFEKRIY IPLPEEAARA 

       310        320        330        340        350        360 
QMFRLHLGST PHNLTDANIH ELARKTEGYS GADISIIVRD SLMQPVRKVQ SATHFKKVCG 

       370        380        390        400        410        420 
PSRTNPSVMI DDLLTPCSPG DPGAIEMTWM DVPGDKLLEP VVCMSDMLRS LATTRPTVNA 

       430 
DDLLKVKKFS EDFGQES 

« Hide

References

« Hide 'large scale' references
[1]"Comparative sequence and expression analyses of four mammalian VPS4 genes."
Beyer A., Scheuring S., Mueller S., Mincheva A., Lichter P., Koehrer K.
Gene 305:47-59(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-228, INTERACTION WITH VPS4B.
Strain: 129/SvEvTacfBr.
Tissue: Spleen.
[2]"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: Head.
[3]"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: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF530161 Genomic DNA. Translation: AAM94861.1.
AK047821 mRNA. Translation: BAC33165.1.
AK159117 mRNA. Translation: BAE34833.1.
BC018368 mRNA. Translation: AAH18368.1.
RefSeqNP_569053.1. NM_126165.1.
UniGeneMm.236004.

3D structure databases

ProteinModelPortalQ8VEJ9.
SMRQ8VEJ9. Positions 3-101, 116-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8VEJ9. 1 interaction.
MINTMINT-4120125.

PTM databases

PhosphoSiteQ8VEJ9.

Proteomic databases

PaxDbQ8VEJ9.
PRIDEQ8VEJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034388; ENSMUSP00000034388; ENSMUSG00000031913.
GeneID116733.
KEGGmmu:116733.
UCSCuc009ngv.1. mouse.

Organism-specific databases

CTD27183.
MGIMGI:1890520. Vps4a.

Phylogenomic databases

eggNOGCOG0464.
GeneTreeENSGT00550000074466.
HOGENOMHOG000225146.
HOVERGENHBG057074.
InParanoidQ8VEJ9.
KOK12196.
OMAVRWNDVA.
OrthoDBEOG74BJS2.
PhylomeDBQ8VEJ9.
TreeFamTF105012.

Gene expression databases

ArrayExpressQ8VEJ9.
BgeeQ8VEJ9.
CleanExMM_VPS4A.
GenevestigatorQ8VEJ9.

Family and domain databases

Gene3D1.20.58.280. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
SUPFAMSSF116846. SSF116846. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio369058.
PROQ8VEJ9.
SOURCESearch...

Entry information

Entry nameVPS4A_MOUSE
AccessionPrimary (citable) accession number: Q8VEJ9
Secondary accession number(s): Q3TXT2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 100 of the entry and version 1 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