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Protein

Major vault protein

Gene

Mvp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity).By similarity

GO - Biological processi

  1. cell proliferation Source: Ensembl
  2. ERBB signaling pathway Source: Ensembl
  3. negative regulation of protein autophosphorylation Source: Ensembl
  4. negative regulation of protein tyrosine kinase activity Source: Ensembl
  5. negative regulation of signaling Source: Ensembl
  6. protein activation cascade Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Major vault protein
Short name:
MVP
Gene namesi
Name:Mvp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi70932. Mvp.

Subcellular locationi

Cytoplasm. Nucleus By similarity

GO - Cellular componenti

  1. cytoskeleton Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. membrane Source: Ensembl
  4. nucleus Source: UniProtKB-SubCell
  5. perinuclear region of cytoplasm Source: Ensembl
  6. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 861860Major vault proteinPRO_0000158982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Post-translational modificationi

Phosphorylated on Tyr residues after EGF stimulation.By similarity
Dephosphorylated by PTPN11.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ62667.
PRIDEiQ62667.

PTM databases

PhosphoSiteiQ62667.

Expressioni

Gene expression databases

GenevestigatoriQ62667.

Interactioni

Subunit structurei

The vault ribonucleoprotein particle is a huge (400 A x 670 A) cage structure of 12.9 MDa. It consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains, PARP4 and one or more vault RNAs (vRNAs). Interacts with TEP1. Interacts with PTEN and activated MAPK1. The phosphorylated protein interacts with the SH2 domains of PTPN11 and SRC. Interacts with APEX1 (By similarity). May interact with ZNF540 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NR3C1P041502EBI-918333,EBI-493507From a different organism.
Nr3c1P065362EBI-918333,EBI-1187143

Protein-protein interaction databases

DIPiDIP-29532N.
IntActiQ62667. 3 interactions.
MINTiMINT-1775954.
STRINGi10116.ENSRNOP00000027360.

Structurei

Secondary structure

1
861
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 213Combined sources
Beta strandi25 – 339Combined sources
Beta strandi38 – 414Combined sources
Beta strandi46 – 483Combined sources
Beta strandi51 – 533Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 633Combined sources
Beta strandi67 – 704Combined sources
Beta strandi79 – 813Combined sources
Beta strandi84 – 918Combined sources
Beta strandi93 – 975Combined sources
Beta strandi109 – 1113Combined sources
Helixi116 – 1183Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi158 – 1614Combined sources
Helixi169 – 1713Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi226 – 2305Combined sources
Beta strandi232 – 2365Combined sources
Beta strandi248 – 2514Combined sources
Turni253 – 2553Combined sources
Beta strandi257 – 2593Combined sources
Beta strandi265 – 2706Combined sources
Beta strandi273 – 2753Combined sources
Turni277 – 2793Combined sources
Beta strandi282 – 2865Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi299 – 3024Combined sources
Beta strandi304 – 3085Combined sources
Beta strandi315 – 3206Combined sources
Beta strandi324 – 3263Combined sources
Beta strandi328 – 33912Combined sources
Beta strandi341 – 3433Combined sources
Beta strandi357 – 3626Combined sources
Beta strandi371 – 3788Combined sources
Beta strandi387 – 3926Combined sources
Turni393 – 3953Combined sources
Beta strandi398 – 4047Combined sources
Beta strandi412 – 4143Combined sources
Helixi422 – 4265Combined sources
Beta strandi459 – 4613Combined sources
Beta strandi466 – 4716Combined sources
Beta strandi473 – 4753Combined sources
Beta strandi478 – 4814Combined sources
Beta strandi486 – 4883Combined sources
Beta strandi493 – 4953Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi503 – 5053Combined sources
Beta strandi510 – 5178Combined sources
Beta strandi519 – 5213Combined sources
Beta strandi522 – 5309Combined sources
Beta strandi536 – 54712Combined sources
Turni550 – 5534Combined sources
Helixi555 – 5595Combined sources
Helixi560 – 5623Combined sources
Beta strandi563 – 5664Combined sources
Helixi567 – 58317Combined sources
Helixi588 – 60215Combined sources
Turni603 – 6053Combined sources
Turni629 – 6313Combined sources
Beta strandi633 – 64715Combined sources
Helixi648 – 801154Combined sources
Helixi806 – 8094Combined sources
Helixi811 – 8133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZVX-ray9.00A/B1-861[»]
4HL8X-ray3.50A1-861[»]
4V60X-ray3.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m1-861[»]
ProteinModelPortaliQ62667.
SMRiQ62667. Positions 1-779.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62667.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 5655MVP 11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati57 – 11155MVP 21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati112 – 16453MVP 31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati165 – 21753MVP 41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati218 – 27255MVP 51 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati273 – 32351MVP 61 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati324 – 37956MVP 71 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati380 – 45778MVP 81 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati458 – 52063MVP 91 PublicationPROSITE-ProRule annotationAdd
BLAST

Domaini

MVP 3 mediates interaction with PTEN.By similarity
MVP 4 mediates interaction with PARP4.By similarity

Sequence similaritiesi

Contains 9 MVP (vault) repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG70525.
GeneTreeiENSGT00390000008969.
HOGENOMiHOG000255109.
HOVERGENiHBG003499.
InParanoidiQ62667.
KOiK17266.
OMAiQDPLADR.
OrthoDBiEOG773XFB.
PhylomeDBiQ62667.

Family and domain databases

InterProiIPR021870. MVP_shoulder.
IPR002499. Vault_N.
[Graphical view]
PfamiPF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 5 hits.
[Graphical view]
PROSITEiPS51224. MVP. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62667-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATEEAIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPVRM
60 70 80 90 100
VTVPPRHYCI VANPVSRDTQ SSVLFDITGQ VRLRHADQEI RLAQDPFPLY
110 120 130 140 150
PGEVLEKDIT PLQVVLPNTA LHLKALLDFE DKNGDKVMAG DEWLFEGPGT
160 170 180 190 200
YIPQKEVEVV EIIQATVIKQ NQALRLRARK ECFDREGKGR VTGEEWLVRS
210 220 230 240 250
VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ALQNFRDLRG VLHRTGEEWL
260 270 280 290 300
VTVQDTEAHV PDVYEEVLGV VPITTLGPRH YCVILDPMGP DGKNQLGQKR
310 320 330 340 350
VVKGEKSFFL QPGERLERGI QDVYVLSEQQ GLLLKALQPL EEGESEEKVS
360 370 380 390 400
HQAGDCWLIR GPLEYVPSAK VEVVEERQAI PLDQNEGIYV QDVKTGKVRA
410 420 430 440 450
VIGSTYMLTQ DEVLWEKELP SGVEELLNLG HDPLADRGQK GTAKPLQPSA
460 470 480 490 500
PRNKTRVVSY RVPHNAAVQV YDYRAKRARV VFGPELVTLD PEEQFTVLSL
510 520 530 540 550
SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ LAYNWHFELK
560 570 580 590 600
NRNDPAEAAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
610 620 630 640 650
MAVFGFEMSE DTGPDGTLLP KARDQAVFPQ NGLVVSSVDV QSVEPVDQRT
660 670 680 690 700
RDALQRSVQL AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE
710 720 730 740 750
KARKELLELE AMSMAVESTG NAKAEAESRA EAARIEGEGS VLQAKLKAQA
760 770 780 790 800
LAIETEAELE RVKKVREMEL IYARAQLELE VSKAQQLANV EAKKFKEMTE
810 820 830 840 850
ALGPGTIRDL AVAGPEMQVK LLQSLGLKST LITDGSSPIN LFSTAFGLLG
860
LGSDGQPPAQ K
Length:861
Mass (Da):95,798
Last modified:January 23, 2007 - v4
Checksum:iE51604F295D49A93
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09870 mRNA. Translation: AAC52161.2.
BC071174 mRNA. Translation: AAH71174.1.
PIRiI53908.
RefSeqiNP_073206.2. NM_022715.2.
UniGeneiRn.10028.

Genome annotation databases

EnsembliENSRNOT00000027360; ENSRNOP00000027360; ENSRNOG00000020182.
GeneIDi64681.
KEGGirno:64681.
UCSCiRGD:70932. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09870 mRNA. Translation: AAC52161.2.
BC071174 mRNA. Translation: AAH71174.1.
PIRiI53908.
RefSeqiNP_073206.2. NM_022715.2.
UniGeneiRn.10028.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZVX-ray9.00A/B1-861[»]
4HL8X-ray3.50A1-861[»]
4V60X-ray3.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m1-861[»]
ProteinModelPortaliQ62667.
SMRiQ62667. Positions 1-779.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29532N.
IntActiQ62667. 3 interactions.
MINTiMINT-1775954.
STRINGi10116.ENSRNOP00000027360.

PTM databases

PhosphoSiteiQ62667.

Proteomic databases

PaxDbiQ62667.
PRIDEiQ62667.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027360; ENSRNOP00000027360; ENSRNOG00000020182.
GeneIDi64681.
KEGGirno:64681.
UCSCiRGD:70932. rat.

Organism-specific databases

CTDi9961.
RGDi70932. Mvp.

Phylogenomic databases

eggNOGiNOG70525.
GeneTreeiENSGT00390000008969.
HOGENOMiHOG000255109.
HOVERGENiHBG003499.
InParanoidiQ62667.
KOiK17266.
OMAiQDPLADR.
OrthoDBiEOG773XFB.
PhylomeDBiQ62667.

Miscellaneous databases

EvolutionaryTraceiQ62667.
NextBioi613698.
PROiQ62667.

Gene expression databases

GenevestigatoriQ62667.

Family and domain databases

InterProiIPR021870. MVP_shoulder.
IPR002499. Vault_N.
[Graphical view]
PfamiPF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 5 hits.
[Graphical view]
PROSITEiPS51224. MVP. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a cDNA encoding the major vault protein from Rattus norvegicus."
    Kickhoefer V.A., Rome L.H.
    Gene 151:257-260(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Kickhoefer V.A.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. Cited for: ASSOCIATION WITH TEP1.
  5. "Draft crystal structure of the vault shell at 9-A resolution."
    Anderson D.H., Kickhoefer V.A., Sievers S.A., Rome L.H., Eisenberg D.
    PLoS Biol. 5:E318-E318(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (9.0 ANGSTROMS), SUBUNIT.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), SUBUNIT, MVP REPEATS.

Entry informationi

Entry nameiMVP_RAT
AccessioniPrimary (citable) accession number: Q62667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 101 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.