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FLASH GENE
Symbol VAPA contributors: mct/npt - updated : 24-03-2016
HGNC name VAMP (vesicle-associated membrane protein)-associated protein A, 33kDa
HGNC id 12648
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N-terminal MSP (major sperm protein) domain, containing an FFAT-motif binding site (correct distribution of the proline residues would be critical for the correct fold of the MSP domain which is required for recognition of the FFAT motif of its partner), and a VAP consensus sequence (VCS) ( )
  • an intermediate domain
  • the central domain is amphipathic and predicted to form a coiled-coil structure
  • a transmembrane domain (TMD)
  • eight potential phosphorylation sites
  • the C-terminal 20 amino acids hydrophobic and acting as an intracellular membrane anchor
  • secondary structure an alpha-helical coiled-coil domain
    HOMOLOGY
    interspecies homolog to murine Vapa
    homolog to yeast VAP Scs2p
    intraspecies homolog to VAPB (60 p100)
    Homologene
    FAMILY
    CATEGORY secretory , transport
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,organelle,Golgi
    intracellular,cytoplasm,cytosolic,vesicle
    intracellular,cytoplasm,cytoskeleton,microtubule
    basic FUNCTION
  • playing a role in vesicle trafficking
  • may act as docking sites for cytoplasmic factors to interact with the ER
  • may have structural and regulatory functions based on interactions of the MSP domain
  • playing an important role in the replication of the hepatitis C virus genome
  • is an integral membrane protein that plays an important role in membrane trafficking, endoplasmic reticulum homeostasis, and the stress-signaling system
  • VAPA with an altered proline distribution can phenocopy amyotrophic lateral sclerosis-associated VAPB
  • VAPB and the related protein VAPA form homo- and heterodimers that are anchored in the endoplasmic reticulum membrane and can interact with protein partners carrying a FFAT motif
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS exocytosis transport , endocytosis transport
    text vesicle trafficking
    PATHWAY
    metabolism
    signaling
    a component
  • dimerizing with VAPB
  • chaperone complex comprising HSP90AA1 and TTC1 that is recruited to the membrane protein VAPA, and regulates intracellular vesicle transport
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • VAMP1, VAMP2
  • interacting with VAPB and ATF6
  • interact directly with components of ER homeostatic and stress signalling systems and may therefore be parts of a previously unidentified regulatory pathway (mis-function of such regulatory systems may contribute to the pathological mechanisms of degenerative motor neuron disease)
  • GLTP interacting with VAPA
  • SLC26A5 appears to modify the expression of VAPA protein in outer hair cells (OHC), and VAPA could be involved in SLC26A5 transportation inside OHCs and may facilitate the targeting of this abundant OHC protein to the plasma membrane
  • partners of CLN8 are VAPA, C14orf1/hERG28, STX8, GABARAPL2, BNIP3 and BNIP3L proteins and are associated with biologically relevant processes such as synthesis and transport of lipids, vesicular/membrane trafficking, autophagy/mitophagy and apoptosis
  • VAPA, VAPB are endoplasmic reticulum (ER)-resident integral membrane protein that controls a nonvesicular mode of ceramide and cholesterol transfer from the ER to the Golgi complex by interacting with COL4A3BP and oxysterol-binding protein (OSBP), respectively
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --low  
    reduced levels of VAP family proteins result in decreased ER anchoring of lipid-binding proteins and cause motor neuron degeneration (Teuling 2007)
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS