|PROSITE documentation PDOC51778|
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 .
Some proteins known to contain a VASt domain are listed below:
The profile we developed covers the entire VASt domain.Last update:
October 2015 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Khafif M. Cottret L. Balague C. Raffaele S.|
|Title||Identification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes.|
|Source||BMC Bioinformatics 15:222-222(2014).|
|2||Authors||Gatta A.T. Wong L.H. Sere Y.Y. Calderon-Norena D.M. Cockcroft S. Menon A.K. Levine T.P.|
|Title||A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.|