Family Report for: Duf_676

This family is made up of a group of uncharacterised eukaryotic proteins that are distantly related to the abhydrolase. It contains IPR016445 Rog1 is a yeast monoacylglycerol (MAG) lipase Lipase and the paralogue YDL109c phospholipase Lpl1. PIRSF005412 UCP005412_abhydr. Selvaraju et al. identified a phospholipase B encoded by the LPL1 gene in Saccharomyces cerevisiae which belongs to this family. In animals the protein is very long. Only c-term is Duf_676 In human the protein is called family with sequence similarity 135 member A F135A

Title: Identification of a phospholipase B encoded by the LPL1 gene in Saccharomyces cerevisiae
Selvaraju K, Rajakumar S, Nachiappan V
Ref: Biochimica & Biophysica Acta, 1841:1383, 2014 : PubMed
Abstract


ESTHER: Selvaraju_2014_Biochim.Biophys.Acta_1841_1383
PubMedSearch: Selvaraju 2014 Biochim.Biophys.Acta 1841 1383
PubMedID: 25014274
Gene_locus related to this paper: yeast-yo059

Abstract

Phospholipids also play a major role in maintaining the lipid droplet (LD) morphology. In our current study, deletion of LPL1 resulted in altered morphology of LDs and was confirmed by microscopic analysis. LPL1/YOR059c contains lipase specific motif GXSXG and acetate labeling in the LPL1 overexpressed strains depicted a decrease in glycerophospholipids and an increase in free fatty acids. The purified Lpl1p showed phospholipase activity with broader substrate specificity, acting on all glycerophospholipids primarily at sn-2 position and later at sn-1 position. Localization studies precisely revealed that Lpl1 is exclusively localized in the LD at the stationary phase. Site directed mutagenesis experiments clearly demonstrated that the lipase motif is vital for the phospholipase activity. In summary, our results demonstrate that yeast Lpl1 exerts phospholipase activity, plays a vital role in LD morphology, and its absence results in altered LD size. Based on the localization and enzyme activity we renamed YOR059c as LPL1 (LD phospholipase 1).