| Description | This entry represents the N-terminal domain of the stress survival proteins, such as survival factor 1 (Svf1). The protein Svf1 is required for yeast survival under conditions of oxidative stress, including cold stress [ ]. Cells deficient in Svf1 have increased levels of reactive oxygen species (ROS) under certain conditions. Svf1 affects cellular survival in part via modulation of the sphingolipid metabolic pathway []. Two Svf1 family proteins have been identified in the genome of Schizosaccharomyces pombe (Svf1 and Svf2).Svf1 is a ceramide binding protein that contributes to sphingolipid metabolism at Golgi compartments and its membrane-targeting is important to maintain flux of ceramides into complex sphingolipids. Svf1 consists of two lipocalin-like domains and binds ceramide via a hydrophobic pocket that is located at the interface between these two domains [ ]. Two histidine residues located in a small predicted α-helical cap covering the hydrophobic pocket, are essential for the ceramide binding. Their mutation results in loss of ceramide binding as well as cis-Golgi targeting of the protein. The arrangement of two tandem lipocalin-like domains is reminiscent to AttH-like proteins (). | Name | Svf1-like, N-terminal |
| Short Name | Svf1-like_N | Type | Domain |
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