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Literature summary for 1.14.18.6 extracted from

  • Dunn, T.M.; Haak, D.; Monaghan, E.; Beeler, T.J.
    Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain (1998), Yeast, 14, 311-321.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q03529
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Cofactor

Cofactor Comment Organism Structure
cytochrome b5 protein contains a cytochrome b5-like domain and a domain that resembles the family of cytochrome b5-dependent enzymes that use iron and oxygen to catalyse desaturation or hydroxylation of fatty acids Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function mutants lacking Scs7 fail to accumulate the inositolphosphorylceramide species, IPC-C, which is the predominant form found in wild-type cells. Instead scs7 mutants accumulate an IPC-B species believed to be unhydroxylated on the amide-linked C26-fatty acid. Elimination of the gene suppresses the Ca2+-sensitive phenotype of csg1 and csg2 mutants. The CSG1 and CSG2 genes are required for mannosylation of IPC-C Saccharomyces cerevisiae