{PDOC51778}
{PS51778; VAST}
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* VASt domain profile *
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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 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 [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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2015 / First entry.

[ 1] Khafif M., Cottret L., Balague C., Raffaele S.
     "Identification and phylogenetic analyses of VASt, an uncharacterized
     protein domain associated with lipid-binding domains in Eukaryotes."
     BMC Bioinformatics 15:222-222(2014).
     PubMed=24965341; DOI=10.1186/1471-2105-15-222
[ 2] Gatta A.T., Wong L.H., Sere Y.Y., Calderon-Norena D.M., Cockcroft S.,
     Menon A.K., Levine T.P.
     "A new family of StART domain proteins at membrane contact sites has a
     role in ER-PM sterol transport."
     Elife 4:0-0(2015).
     PubMed=26001273; DOI=10.7554/eLife.07253

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