|Gene:||SEC59||Accession Number: G-5521 (MetaCyc)|
Synonyms: dolichol phosphokinase
Species: Saccharomyces cerevisiae
The product of gene SEC59 was computationally predicted to be highly hydrophobic and to contain two potential N-glycosylation sites [Bernstein89]. The product of gene SEC59 contains a 13-amino acid consensus sequence thought to be involved in dolichol recognition. This sequence is also found in the glycosyltransferase products of genes ALG1, ALG7, and DPM1 [Albright89].
Human dolichol kinase has been cloned and expressed in Escherichia coli and its topological arrangement as a membrane protein characterized [Shridas06]. In humans, mutations in the gene encoding dolichol kinase can cause a lethal metabolic disorder [Kranz07].
Gene Citations: [Heller92]
Locations: endoplasmic reticulum
|Map Position: [295,178 <- 296,737]|
Molecular Weight of Polypeptide: 58.916 kD (from nucleotide sequence)
|Cellular Component:||GO:0005783 - endoplasmic reticulum [Bernstein89]|
Enzymatic reaction of: dolichol kinase
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
In Pathways: dolichol and dolichyl phosphate biosynthesis
Saccharomyces cerevisiae cells carrying the SEC59 mutation are deficient in dolichol kinase activity [Heller92].
Albright89: Albright CF, Orlean P, Robbins PW (1989). "A 13-amino acid peptide in three yeast glycosyltransferases may be involved in dolichol recognition." Proc Natl Acad Sci U S A 86(19);7366-9. PMID: 2678101
Kranz07: Kranz C, Jungeblut C, Denecke J, Erlekotte A, Sohlbach C, Debus V, Kehl HG, Harms E, Reith A, Reichel S, Grobe H, Hammersen G, Schwarzer U, Marquardt T (2007). "A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy." Am J Hum Genet 80(3);433-40. PMID: 17273964
Shridas06: Shridas P, Waechter CJ (2006). "Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein with a cytoplasmically oriented CTP-binding site." J Biol Chem 281(42);31696-704. PMID: 16923818
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