Diphosphomevalonate decarboxylase (MVD)
The protein contains 400 amino acids for an estimated molecular weight of 43405 Da.
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. (updated: June 17, 2020)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs34519538 | |
| POROK7 | |
| POROK7 | |
| POROK7; unknown pathological significance | |
| POROK7 | |
| POROK7 | |
| POROK7 | |
| POROK7 | |
| POROK7 | |
| POROK7 |
Biological Process
Cellular protein metabolic process
Cholesterol biosynthetic process
Dolichol-linked oligosaccharide biosynthetic process
Dolichyl diphosphate biosynthetic process
Isopentenyl diphosphate biosynthetic process, mevalonate pathway
Isoprenoid biosynthetic process
Positive regulation of cell population proliferation
Post-translational protein modification
Protein N-linked glycosylation via asparagine
Regulation of cholesterol biosynthetic process
Regulation of lipid metabolic process
Small molecule metabolic process
The reference OMIM entry for this protein is 603236
Mevalonate pyrophosphate decarboxylase; mvd
Mpd
DESCRIPTION
The enzyme mevalonate pyrophosphate decarboxylase (MVD; EC 4.1.1.33) catalyzes the conversion of mevalonate pyrophosphate into isopentenyl pyrophosphate. This unusual enzyme decarboxylates and dehydrates its substrate while hydrolyzing ATP. As a unique enzyme in one of the early steps in cholesterol biosynthesis, MVD may be a useful target for drugs aimed at lowering serum cholesterol levels (summary by Toth and Huwyler, 1996).CLONING
Toth and Huwyler (1996) cloned the human MVD gene from a liver cDNA library. The cDNA encoded a 400-amino acid polypeptide. Northern blot analysis revealed a 2-kb mRNA present at similar levels in various human tissues. Expression studies indicated that the recombinant human enzyme is active as a 43-kD homodimer.MAPPING
Gross (2012) mapped the MVD gene to chromosome 16q24.3 based on an alignment of the MVD sequence (GenBank GENBANK BC000011) with the genomic sequence (GRCh37). ... More on the omim web site
June 29, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603236 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed