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PROSITE documentation PDOC51778

VASt domain profile





Description

The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains (see <PDOC00437>), including START lipid-binding domains (see <PDOC50848>). The ~190-amino acid VASt domain is predominantly associated with lipid binding domains such as GRAM, C2 (see <PDOC00380>) and PH (see <PDOC50003>) domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol [1,2].

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 to 3), six β-sheets (β1 to 6) and two loops (omega1 and 2) numbered from N to C terminus [1].

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.

The profile we developed covers the entire VASt domain.

Last update:

October 2015 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

VAST, PS51778; VASt domain profile  (MATRIX)


References

1AuthorsKhafif M. Cottret L. Balague C. Raffaele S.
TitleIdentification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes.
SourceBMC Bioinformatics 15:222-222(2014).
PubMed ID24965341
DOI10.1186/1471-2105-15-222

2AuthorsGatta A.T. Wong L.H. Sere Y.Y. Calderon-Norena D.M. Cockcroft S. Menon A.K. Levine T.P.
TitleA new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.
SourceElife 4:0-0(2015).
PubMed ID26001273
DOI10.7554/eLife.07253



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Miscellaneous

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