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 binding domains such as GRAM [pfam:PF02893], C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol [[cite:PUB00084279],[cite:PUB00084280]]. 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 [[cite:PUB00084279]]. Some proteins known to contain a VASt domain are : 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 and may be involved in sterol transfer between intracellular membranes.It is also found in human GramD1a-c.
","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"VAD1_analog_of_StAR-related_lipid_transfer","extract":"VAD1 analog of StAR-related lipid transfer (VASt) is a steroidogenic acute regulatory protein‐related lipid transfer (StART)-like lipid-binding domain first identified in the vad1 protein in Arabidopsis thaliana. Proteins containing these domains are found in eukaryotes and usually contain another lipid-binding domain, typically the GRAM domain and sometimes the C2 domain in plants and the integral peroxisomal membrane peroxin Pex24p domain in oomycetes.
","thumbnail":null}],"literature":{"PUB00084280":{"PMID":26001273,"ISBN":null,"volume":"4","issue":null,"year":2015,"title":"A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.","URL":null,"raw_pages":null,"medline_journal":"Elife","ISO_journal":"Elife","authors":["Gatta AT","Wong LH","Sere YY","Calderon-Norena DM","Cockcroft S","Menon AK","Levine TP."],"DOI_URL":"http://dx.doi.org/10.7554/eLife.07253"},"PUB00084279":{"PMID":24965341,"ISBN":null,"volume":"15","issue":null,"year":2014,"title":"Identification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes.","URL":null,"raw_pages":"222","medline_journal":"BMC Bioinformatics","ISO_journal":"BMC Bioinformatics","authors":["Khafif M","Cottret L","Balague C","Raffaele S."],"DOI_URL":"http://dx.doi.org/10.1186/1471-2105-15-222"}},"set_info":{"accession":"CL0209","name":"Bet_v_1_like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":194,"interactions":0,"matches":14430,"pathways":0,"proteins":12938,"proteomes":3299,"sets":1,"structural_models":{"alphafold":9903},"structures":12,"taxa":8680},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":300,"alignment:full":10731},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"6cay","name":"Crystal structure of the first StART-like domain of Ysp2p/Lam2p in its apo and ergosterol-bound state."}}}