MVD Gene: Mevalonate Diphosphate Decarboxylase
Key enzyme in the mevalonate pathway for cholesterol and isoprenoid biosynthesis
Gene Information Card
| Symbol | MVD |
|---|---|
| Full Name | Mevalonate Diphosphate Decarboxylase |
| Gene Type | Protein coding |
| Chromosomal Location | 16q24.2 |
| NCBI Gene ID | 4597 ncbi.nlm.nih.gov/gene/4597 |
| Ensembl ID | ENSG00000167552 |
| UniProt ID | P53602 |
| OMIM ID | 603236 |
| HGNC ID | 7529 |
| Aliases | MDDase, MPD, POROK9 |
Description
MVD encodes mevalonate diphosphate decarboxylase, an enzyme that catalyzes the ATP-dependent decarboxylation of mevalonate diphosphate to isopentenyl diphosphate (IPP), a key step in the mevalonate pathway. This pathway is essential for the biosynthesis of cholesterol, steroid hormones, vitamin D, bile acids, and isoprenoids. Mutations in MVD are associated with disseminated superficial actinic porokeratosis (DSAP) and mevalonate kinase deficiency (MKD)-like phenotypes.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Disseminated superficial actinic porokeratosis (DSAP) | Loss-of-function mutations impair enzyme activity, leading to abnormal keratinocyte differentiation and skin lesions | OMIM #175900; PMID: 22842230 |
| Mevalonate kinase deficiency (MKD)-like phenotype | Reduced MVD activity disrupts isoprenoid synthesis, causing recurrent fevers and inflammation | OMIM #260920; PMID: 23352259 |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Liver | 18.5 | High |
| Adrenal gland | 12.3 | Medium |
| Skin | 8.1 | Medium |
| Testis | 6.7 | Low |
| Brain | 3.2 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HepG2 | 15.2 | Hepatocellular carcinoma cell line |
| A549 | 9.8 | Lung carcinoma cell line |
| HaCaT | 7.5 | Keratinocyte cell line |
| HEK293 | 6.1 | Embryonic kidney cell line |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.112G>A (p.Gly38Arg) | Missense | Rare | Reduced enzyme activity; associated with DSAP |
| c.541C>T (p.Arg181Trp) | Missense | Rare | Impaired decarboxylation; linked to MKD-like phenotype |
| c.746T>C (p.Leu249Pro) | Missense | Rare | Loss of function; reported in porokeratosis |
Mutation functional classification
Loss of Function (LOF)
Most MVD mutations reduce or abolish enzymatic activity, leading to substrate accumulation and pathway disruption.
Gain of Function (GOF)
Not reported.
Dominant Negative (DN)
Not reported; inheritance in DSAP is autosomal dominant with incomplete penetrance, but mechanism may involve haploinsufficiency.
View complete mutation data：
Gene Ontology (GO)
Pathways
• Mevalonate pathway (KEGG: hsa00900)
• Terpenoid backbone biosynthesis (KEGG: hsa00900)
• Cholesterol biosynthesis (Reactome: R-HSA-191273)
Protein Summary
Mevalonate diphosphate decarboxylase (MVD) is a 400-amino acid cytoplasmic enzyme that catalyzes the final step of the mevalonate pathway, converting mevalonate diphosphate to isopentenyl diphosphate (IPP). The enzyme requires ATP and Mg2+ for activity. IPP is a precursor for all isoprenoids, including cholesterol, dolichol, ubiquinone, and prenylated proteins. MVD deficiency leads to accumulation of mevalonate diphosphate and reduced isoprenoid synthesis, causing cellular stress and disease.
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