PROSITE documentation PDOC51778VASt domain profile
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.
-------------------------------------------------------------------------------
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). | |
| PubMed ID | 24965341 | |
| DOI | 10.1186/1471-2105-15-222 |
| 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. | |
| Source | Elife 4:0-0(2015). | |
| PubMed ID | 26001273 | |
| DOI | 10.7554/eLife.07253 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)