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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
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(139195) 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