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Q8VEJ9

- VPS4A_MOUSE

UniProt

Q8VEJ9 - VPS4A_MOUSE

Protein

Vacuolar protein sorting-associated protein 4A

Gene

Vps4a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    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: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission By similarity.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi167 – 1748ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nucleoside-triphosphatase activity Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. abscission Source: UniProtKB
    2. cell division Source: UniProtKB-KW
    3. cytokinesis checkpoint Source: UniProtKB
    4. negative regulation of cytokinesis Source: UniProtKB
    5. protein transport Source: UniProtKB-KW
    6. vesicle-mediated transport Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, Protein transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vacuolar protein sorting-associated protein 4A (EC:3.6.4.6)
    Gene namesi
    Name:Vps4aImported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1890520. Vps4a.

    Subcellular locationi

    Prevacuolar compartment membrane 1 Publication; Peripheral membrane protein 1 Publication. Late endosome membrane By similarity; Peripheral membrane protein By similarity. Midbody By similarity
    Note: Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells. Localizes to the midbody of dividing cells, interaction with ZFYVE19/ANCHR mediates retention at midbody. Localized in two distinct rings on either side of the Fleming body By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. late endosome membrane Source: UniProtKB-SubCell
    3. midbody Source: UniProtKB
    4. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi228 – 2281E → Q: Perinuclear localization. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 437436Vacuolar protein sorting-associated protein 4APRO_0000084766Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity
    Modified residuei8 – 81N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8VEJ9.
    PaxDbiQ8VEJ9.
    PRIDEiQ8VEJ9.

    PTM databases

    PhosphoSiteiQ8VEJ9.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ8VEJ9.
    BgeeiQ8VEJ9.
    CleanExiMM_VPS4A.
    GenevestigatoriQ8VEJ9.

    Interactioni

    Subunit structurei

    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. Interacts with ZFYVE19/ANCHR; leading to retain it at midbody By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8VEJ9. 1 interaction.
    MINTiMINT-4120125.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VEJ9.
    SMRiQ8VEJ9. Positions 3-101, 116-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8079MITAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili15 – 3723Sequence AnalysisAdd
    BLAST

    Domaini

    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.By similarity

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Sequence Analysis
    Contains 1 MIT domain.Sequence Analysis

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0464.
    GeneTreeiENSGT00550000074466.
    HOGENOMiHOG000225146.
    HOVERGENiHBG057074.
    InParanoidiQ8VEJ9.
    KOiK12196.
    OMAiRPTVNTE.
    OrthoDBiEOG74BJS2.
    PhylomeDBiQ8VEJ9.
    TreeFamiTF105012.

    Family and domain databases

    Gene3Di1.20.58.280. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR007330. MIT.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF04212. MIT. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00745. MIT. 1 hit.
    [Graphical view]
    SUPFAMiSSF116846. SSF116846. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00674. AAA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8VEJ9-1 [UniParc]FASTAAdd to Basket

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    MTTSTLQKAI DLVTKATEED KAKNYEEALR LYQHAVEYFL HAIKYEAHSD    50
    KAKESIRAKC MQYLDRAEKL KDYLRNKEKH GKKPVKENQS EGKGSDSDSE 100
    GDNPEKKKLQ EQLMGAVVME KPNIRWNDVA GLEGAKEALK EAVILPIKFP 150
    HLFTGKRTPW RGILLFGPPG TGKSYLAKAV ATEANNSTFF SVSSSDLMSK 200
    WLGESEKLVK NLFELARQHK PSIIFIDEVD SLCGSRNENE SEAARRIKTE 250
    FLVQMQGVGN NNDGTLVLGA TNIPWVLDSA IRRRFEKRIY IPLPEEAARA 300
    QMFRLHLGST PHNLTDANIH ELARKTEGYS GADISIIVRD SLMQPVRKVQ 350
    SATHFKKVCG PSRTNPSVMI DDLLTPCSPG DPGAIEMTWM DVPGDKLLEP 400
    VVCMSDMLRS LATTRPTVNA DDLLKVKKFS EDFGQES 437
    Length:437
    Mass (Da):48,907
    Last modified:March 1, 2002 - v1
    Checksum:iB67CF13F7AFD9129
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF530161 Genomic DNA. Translation: AAM94861.1.
    AK047821 mRNA. Translation: BAC33165.1.
    AK159117 mRNA. Translation: BAE34833.1.
    BC018368 mRNA. Translation: AAH18368.1.
    CCDSiCCDS40463.1.
    RefSeqiNP_569053.1. NM_126165.1.
    UniGeneiMm.236004.

    Genome annotation databases

    EnsembliENSMUST00000034388; ENSMUSP00000034388; ENSMUSG00000031913.
    GeneIDi116733.
    KEGGimmu:116733.
    UCSCiuc009ngv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF530161 Genomic DNA. Translation: AAM94861.1 .
    AK047821 mRNA. Translation: BAC33165.1 .
    AK159117 mRNA. Translation: BAE34833.1 .
    BC018368 mRNA. Translation: AAH18368.1 .
    CCDSi CCDS40463.1.
    RefSeqi NP_569053.1. NM_126165.1.
    UniGenei Mm.236004.

    3D structure databases

    ProteinModelPortali Q8VEJ9.
    SMRi Q8VEJ9. Positions 3-101, 116-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8VEJ9. 1 interaction.
    MINTi MINT-4120125.

    PTM databases

    PhosphoSitei Q8VEJ9.

    Proteomic databases

    MaxQBi Q8VEJ9.
    PaxDbi Q8VEJ9.
    PRIDEi Q8VEJ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034388 ; ENSMUSP00000034388 ; ENSMUSG00000031913 .
    GeneIDi 116733.
    KEGGi mmu:116733.
    UCSCi uc009ngv.1. mouse.

    Organism-specific databases

    CTDi 27183.
    MGIi MGI:1890520. Vps4a.

    Phylogenomic databases

    eggNOGi COG0464.
    GeneTreei ENSGT00550000074466.
    HOGENOMi HOG000225146.
    HOVERGENi HBG057074.
    InParanoidi Q8VEJ9.
    KOi K12196.
    OMAi RPTVNTE.
    OrthoDBi EOG74BJS2.
    PhylomeDBi Q8VEJ9.
    TreeFami TF105012.

    Enzyme and pathway databases

    Reactomei REACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).

    Miscellaneous databases

    NextBioi 369058.
    PROi Q8VEJ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VEJ9.
    Bgeei Q8VEJ9.
    CleanExi MM_VPS4A.
    Genevestigatori Q8VEJ9.

    Family and domain databases

    Gene3Di 1.20.58.280. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR007330. MIT.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF04212. MIT. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00745. MIT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF116846. SSF116846. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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/SvEvTacfBrImported.
      Tissue: SpleenImported.
    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.
      , 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/NImported.
      Tissue: Mammary glandImported.

    Entry informationi

    Entry nameiVPS4A_MOUSE
    AccessioniPrimary (citable) accession number: Q8VEJ9
    Secondary accession number(s): Q3TXT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 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