| Primary Identifier | IPR031968 | Type | Domain |
| Short Name | VASt |
| description | 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 bindingdomains 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 [, ].The predicted structure of the VASt domain is a two-layer sandwich α/β fold, also called "helix grip fold", containing three α-helices (α1 to3), six β-sheets (β1 to 6) and two loops (ω1 and 2) numbered from N to C terminus [].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. |
