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FLASH GENE
Symbol VTA1 contributors: mct/npt - updated : 22-01-2020
HGNC name Vps20-associated 1 homolog (S. cerevisiae)
HGNC id 20954
EXPRESSION
Type
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Nervousbrain   highly
Reproductivemale systemtestis  highly
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Muscularstriatum  highly
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • an ATP and actin domain at the N terminus
  • a nec with n copies of the IQ motif
  • a tandem MIT domain, that can bind MIM elements within both CHMP1A and IST1, implying that the complexes probably interact directly in cells
  • a calmodulin calcium-binding region at the C terminus, mediating dimerization and both subunits are required for its function as a VPS4A regulator
  • HOMOLOGY
    Homologene
    FAMILY
  • myosin superfamily
  • VTA1 family
  • CATEGORY motor/contractile
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,cytosolic
    text predominantly a cytosolic protein (Ward 2005)
    basic FUNCTION
  • may contribute to the dopamine-induced cell growth, which is negatively regulated by NGFRAP1 (Yu 2007)
  • role for direct binding between VTA1 and ESCRT-III proteins (CHMP1B, CHMP2A, VPS24) that is likely to complement VTA1 previously described ability to regulate VPS4 activity
  • helps regulate the membrane fission and recycling activities of the ESCRT pathway
  • presumably VTA1 promotes VPS4A assembly and activates the enzyme to remodel the ESCRT-III polymer and release ESCRT factors back into the cytoplasm
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • VTA1-CHMP5 complex (Bajorek 2009)
  • INTERACTION
    DNA
    RNA
    small molecule nucleotide,
  • ATP binding
  • protein
  • actin
  • interact with NGFRAP1, and the interaction occurred in cytoplasm (through N-terminus of VTA1 and the C-terminus of NGFRAP1 (Yu 2007)
  • interacting with CHMP5 (with CHMP5 function in multivesicular body sorting, whereas only VTA1 is required for HIV release) (Ward 2005)
  • VPS4A regulator (Xiao 2008)
  • binds to a different region within CHMP5 than within the other ESCRT-III proteins (Shim 2008)
  • interactions with ESCRT-III proteins may be regulated by ESCRT-III conformation (possible role for direct binding between VTA1 and ESCRT-III proteins that is likely to complement its previously described ability to regulate VPS4A and VPS4B activity) (Shim 2008)
  • interacts with other players of the ESCRT machinery as well as with two known cargo proteins, AQP2 and EGFR, whose degradation is affected upon reduction of VTA1 expression
  • tandem MIT domain of VTA1 binds different types of ESCRT-III proteins, promoting assembly of active VPS4 enzymes on the polymeric ESCRT-III substrate
  • CHMP5(139–195) binds the tandem MIT domain of VTA1
  • N-terminal domain of VTA1 (LIP5NTD) is required for VTA1-mediated stimulation of VPS4A, and the ESCRT-III protein CHMP5 strongly inhibits the stimulation
  • efficient abscission during cytokinesis requires proper function of the ESCRT-III protein IST1, which binds to the microtubule interacting and trafficking (MIT) domains of VPS4A, VTA1, and SPART via its C-terminal MIT-interacting motif (MIM)
  • interaction between the renal water channel aquaporin-2 (AQP2) and the lysosomal trafficking regulator-interacting protein VTA1 targets AQP2 to multivesicular bodies and facilitates lysosomal degradation
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS