Pathways & interactions
VASt domain (IPR031968)
Short name: VASt
Overlapping homologous superfamilies
The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains, including START lipid-binding domains. The ~190-amino acid VASt domain is predominantly associated with lipid binding domains such as GRAM, C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol [PMID: 24965341, PMID: 26001273].
The predicted structure of the VASt domain is a two-layer sandwich alpha beta fold, also called "helix grip fold", containing three alpha helices (alpha1 to 3), six beta-sheets (beta1 to 6) and two loops (omega1 and 2) numbered from N to C terminus [PMID: 24965341].
Some proteins known to contain a VASt domain are listed below:
- Plant vascular associated death1 (VAD1), a regulator of programmed cell death (PCD) harboring a GRAM putative lipid-binding domain.
- Yeast SNF1 Interacting Protein 3 (SIP3), may be involved in sterol transfer between intracellular membranes.
- Yeast Suicide Protein 1 (YSP1), a mitochondrial protein specifically required for the mitochondrial thread-grain transition, de-energization, and the cell death. May be involved in sterol transfer between intracellular membranes.
- Yeast Suicide Protein 2 (YSP2), a mitochondrial membrane protein involved in mitochondrial fragmentation. May be involved in sterol transfer between intracellular membranes.
- Human GramD1a-c.