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Literature summary for 2.3.1.84 extracted from

  • Lin, J.L.; Wheeldon, I.
    Dual N- and C-terminal helices are required for endoplasmic reticulum and lipid droplet association of alcohol acetyltransferases in Saccharomyces cerevisiae (2014), PLoS ONE, 9, e104141.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
E509A/E512A/E513A mutation in isoform Atf1, mutated protein shows 84% localization to lipid droplets Saccharomyces cerevisiae
L511A/L514A/Y518A/L512A mutation in isoform Atf1, loss of membrane association Saccharomyces cerevisiae
additional information truncation of amphipathic helices within the N- and C-terminal domains of isoform Atf1 (residues 24-41 and 508-525) impair endoplasmic reticulum localization and membrane association. Mutations of the basic or hydrophobic residues in the N-terminal helix and hydrophobic residues in the C-terminal helix of Atf1 disrupt ER association and subsequent sorting from the ER to lipid droplets. Similar amphipathic helices are found at both ends of isoform Atf2, enabling ER and lipid droplet association. Mutations to the N- and C-terminal helices of Atf2 prevent membrane association Saccharomyces cerevisiae
R22A/R23A/R36A mutation in isoform Atf2, protein is localized in the cytoplasm Saccharomyces cerevisiae
W518A/F521/I529A/F532A R36A mutation in isoform Atf2, protein is localized in the cytoplasm Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum both isoforms Atf1 and Atf2 Saccharomyces cerevisiae 5783
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lipid droplet isoform Atf1 Saccharomyces cerevisiae 5811
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membrane
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 Saccharomyces cerevisiae 16020
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Saccharomyces cerevisiae BY4742
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