Major vault protein (MVP)
The protein contains 893 amino acids for an estimated molecular weight of 99327 Da.
Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases. (updated: Jan. 31, 2018)
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.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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:rs35916172 | |
| dbSNP:rs3764944 | |
| empty |
Biological Process
Cell population proliferation
ERBB signaling pathway
MRNA transport
Negative regulation of epidermal growth factor receptor signaling pathway
Negative regulation of protein autophosphorylation
Negative regulation of protein tyrosine kinase activity
Negative regulation of signaling
Neutrophil degranulation
Protein activation cascade
Protein transport
Regulation of signaling
The reference OMIM entry for this protein is 605088
Major vault protein, rat, homolog of; mvp
Lung resistance-related protein; lrp
DESCRIPTION
Vaults are hollow intracellular organelles with dimensions of about 57 by 32 nm and a nuclear mass of about 13 MD, 3 times the size of a ribosome. They are composed of a small RNA (VTRNA1-1; 612695), the 100-kD major vault protein (MVP), and minor vault proteins of 193 kD (PARP4; 607519) and 240 kD (TEP1; 601686). MVP accounts for over 70% of the particle mass (Izquierdo et al., 1996; Kickhoefer et al., 1999).CLONING
Multidrug-resistant (MDR) cancer cells frequently overexpress the 110-kD lung resistance-related protein (LRP). Overexpression of LRP often predicts a poor response to chemotherapy. By screening a multidrug-resistant non-P-glycoprotein (see ABCB1; 171050) fibrosarcoma cell line with an LRP-specific monoclonal antibody, Scheffer et al. (1995) isolated a cDNA encoding LRP. The deduced 896-amino acid LRP protein shares 88% amino acid identity with the rat major vault protein (Mvp). RNase protection assays showed that LRP expression was enhanced 4- to 8-fold in non-P-glycoprotein MDR cell lines. Using immunohistochemical analysis, Izquierdo et al. (1996) found that LRP was widely expressed in normal and tumor tissues and showed a characteristic cytoplasmic granular pattern. High LRP expression was detected in the epithelial lining of bronchioles and upper and lower digestive tract, renal proximal tubules, epidermal keratinocytes and melanocytes, macrophages, and adrenal cortex. Lower and variable expression of LRP was detected in other tissues. LRP was expressed in all tumor types tested, and its level of expression fairly reflected the chemosensitivity of the tumors, with lower expression in highly chemosensitive tumors. Immunoprecipitated LRP had an apparent molecular mass of 110 kD by SDS-PAGE. By EST database analysis, Holzmann et al. (2001) identified a long MVP splice variant, L-MVP, that contains a 41-bp stretch in the 5-prime region that is intronic in the shorter S-MVP splice variant. This 41-bp stretch introduces an upstream ORF encoding a deduced 18-amino acid peptide. RT-PCR detected ubiquitous expression of both variants, and S-MVP was always the major variant. Van Zon et al. (2002) identified a central calcium-binding EF-hand motif and a C-terminal coiled-coil domain in MVP. Using confocal immunocytochemistry with anti-MVP antibody, Slesina et al. (2005) found a dense distribution of vault particles in the cytoplasm of human U373 astroglioma cell line. A punctate staining pattern was also detected in the nucleus. Cryoimmunoelectron microscopy revealed clusters of immunogold particles at nuclear pores and in the nucleoplasm, suggesting that nuclear MVP was also associated with vaults. Quantification of fluorescent MVP in the cytosol and nucleus of U373 cells revealed about 5% of MVP in the nucleus.GENE FUNCTION
Kickhoefer et al. (1998) found that expression of MVP and VTRNA1-1 and assembly of vaults increased up to 15-fold in several drug-resistant cell lines compared with the parental cell lines. They hypothesized that the absolute vault level in cell lines may dictate the extent of drug resistance. Abbondanza et al. (1998) found that MVP coprecipitated with estrogen receptor (ER, or ESR1; 133430) from nuclear extracts of MCF-7 human breast cancer cells and that ER associated with intact vaults. Mutation analysis showed that a central region of ER containing nuclear localization signals was involved in the interaction. A limited amount of ER molecules in the nuclear e ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Feb. 10, 2018: 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
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605088 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed