MVD
Function
Catalyzes the ATP dependent decarboxylation of (R)-5-diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and sterol synthesis.
Involvement in disease
Porokeratosis 7, multiple types
POROK7
A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported.
None
The disease is caused by variants affecting the gene represented in this entry.
Pathway
Steroid biosynthesis; cholesterol biosynthesis.
Sequence Similarities
Belongs to the diphosphomevalonate decarboxylase family.
Tissue Specificity
Expressed in heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta.
Cellular localization
- Cytoplasm
Alternative names
MPD, MVD, Diphosphomevalonate decarboxylase, Mevalonate (diphospho)decarboxylase, Mevalonate pyrophosphate decarboxylase, MDDase