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Literature summary extracted from

  • Uemura, S.; Kihara, A.; Iwaki, S.; Inokuchi, J.; Igarashi, Y.
    Regulation of the transport and protein levels of the inositol phosphorylceramide mannosyltransferases Csg1 and Csh1 by the Ca2+-binding protein Csg2 (2007), J. Biol. Chem., 282, 8613-8621 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.370 recombinant expression of FLAG3-tagged enzyme in Saccharomyces cerevisiae KA31-1A (CSG1 CSH1) cells resulting in SUY69 cells, coexpression of Cgs2 Ca2+-binding protein, quantitative real-time PCR enzyme expression analysis. Csg2 has an effect on the protein level of Csg1 Saccharomyces cerevisiae
2.4.1.370 recombinant FLAG3-tagged wild-type and mutant enzymes in Saccharomyces cerevisiae KA31-1A (CSG1 CSH1) cells resulting in SUY73 cells, coexpression of Cgs2 Ca2+-binding protein, quantitative real-time PCR enzyme expression analysis. Csg2 has an effect on the protein level of Csh1 Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.370 N247Q site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme Saccharomyces cerevisiae
2.4.1.370 N51Q site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme Saccharomyces cerevisiae
2.4.1.370 N51Q/N247Q site-directed mutagenesis, N-glycosylation of the mutant is reduced compared to the wild-type enzyme Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.370 Golgi membrane integral membrane protein Csg1 exhibits a membrane topology with its C-terminus in the cytosol and its mannosyltransferase domain in the lumen Saccharomyces cerevisiae 139
-
2.4.1.370 Golgi membrane integral membrane protein Csh1 exhibits a membrane topology with its C-terminus in the cytosol and its mannosyltransferase domain in the lumen Saccharomyces cerevisiae 139
-
2.4.1.370 additional information complexed Csg1 functions in the Golgi and is then delivered to the vacuole for degradation Saccharomyces cerevisiae
-
-
2.4.1.370 additional information uncomplexed Csh1 cannot exit from the endoplasmic reticulum. Complexed Csh1 functions in the Golgi and is then delivered to the vacuole for degradation Saccharomyces cerevisiae
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-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.370 Ca2+ Ca2+ stimulates inositol phosphorylceramide (IPC) to mannosylinositol phosphorylceramide (MIPC) conversion, because of a Csg2-dependent increase in Csg1 levels Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.370 Saccharomyces cerevisiae P33300
-
-
2.4.1.370 Saccharomyces cerevisiae P38287
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-
2.4.1.370 Saccharomyces cerevisiae ATCC 204508 P33300
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2.4.1.370 Saccharomyces cerevisiae ATCC 204508 P38287
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-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.370 glycoprotein Csg1 is N-glycosylated with core-type structures. Deglycosylation by peptide N-glycosidase (PNGase) F. Csg2 has an effect on the glycosylation status of Csg1. Csg1 is predicted to be N-glycosylated at N224, N295, N298, N370, N379, and N380 Saccharomyces cerevisiae
2.4.1.370 glycoprotein Csh1 is N-glycosylated with mannan-type structures. Deglycosylation by peptide N-glycosidase (PNGase) F. Csg2 has an effect on the glycosylation status of Csh1. Csh1 is N-glycosylated at N51 and N247 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.370 GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
-
 Saccharomyces cerevisiae a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
-
 ?
2.4.1.370 GDP-alpha-D-mannose + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
-
 Saccharomyces cerevisiae ATCC 204508 a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide + GDP
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.370 ? x * 47000, about, recombinant FLAG3-tagged enzyme, sequence calculation, x * 48000, glycosylated recombinant FLAG3-tagged enzyme, SDS-PAGE Saccharomyces cerevisiae
2.4.1.370 ? x * 47500, about, recombinant FLAG3-tagged enzyme, sequence calculation, x * 55000-70000, glycosylated recombinant FLAG3-tagged enzyme, SDS-PAGE Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.4.1.370 Csg1
-
 Saccharomyces cerevisiae
2.4.1.370 CSH1
-
 Saccharomyces cerevisiae
2.4.1.370 SUR1
-
 Saccharomyces cerevisiae

Expression

EC Number Organism Comment Expression
2.4.1.370 Saccharomyces cerevisiae Ca2+ stimulates a Csg2-dependent increase in Csg1 levels up

General Information

EC Number General Information Comment Organism
2.4.1.370 physiological function complex sphingolipids in yeast are known to function in cellular adaptation to environmental changes. One of the yeast complex sphingolipids, mannosylinositol phosphorylceramide (MIPC), is produced by the redundant inositol phosphorylceramide (IPC) mannosyltransferases Csg1 and Csh1. The Ca2+-binding protein Csg2 can form a complex with either Csg1 or Csh1 and is considered to act as a regulatory subunit. After complexing with Csg2, both Csg1 and Csh1 function in the Golgi, and then are delivered to the vacuole for degradation. Csg2 has several regulatory functions for Csg1 and Csh1, including stability, transport, and gene expression. Differing effects of Csg2 on the degradation of isozymes Csg1 and Csh1 in the vacuole Saccharomyces cerevisiae