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Q62667 (MVP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major vault protein

Short name=MVP
Gene names
Name:Mvp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length861 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.5 Ref.6

Subcellular location

Cytoplasm. Nucleus By similarity.

Domain

MVP 3 mediates interaction with PTEN By similarity.

MVP 4 mediates interaction with PARP4 By similarity.

Post-translational modification

Phosphorylated on Tyr residues after EGF stimulation By similarity.

Dephosphorylated by PTPN11 By similarity.

Sequence similarities

Contains 9 MVP (vault) repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NR3C1P041502EBI-918333,EBI-493507From a different organism.
Nr3c1P065362EBI-918333,EBI-1187143

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 861860Major vault protein
PRO_0000158982

Regions

Repeat2 – 5655MVP 1
Repeat57 – 11155MVP 2
Repeat112 – 16453MVP 3
Repeat165 – 21753MVP 4
Repeat218 – 27255MVP 5
Repeat273 – 32351MVP 6
Repeat324 – 37956MVP 7
Repeat380 – 45778MVP 8
Repeat458 – 52063MVP 9

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Secondary structure

.................................................................................................................................... 861
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q62667 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: E51604F295D49A93

FASTA86195,798
        10         20         30         40         50         60 
MATEEAIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPVRM VTVPPRHYCI 

        70         80         90        100        110        120 
VANPVSRDTQ SSVLFDITGQ VRLRHADQEI RLAQDPFPLY PGEVLEKDIT PLQVVLPNTA 

       130        140        150        160        170        180 
LHLKALLDFE DKNGDKVMAG DEWLFEGPGT YIPQKEVEVV EIIQATVIKQ NQALRLRARK 

       190        200        210        220        230        240 
ECFDREGKGR VTGEEWLVRS VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ALQNFRDLRG 

       250        260        270        280        290        300 
VLHRTGEEWL VTVQDTEAHV PDVYEEVLGV VPITTLGPRH YCVILDPMGP DGKNQLGQKR 

       310        320        330        340        350        360 
VVKGEKSFFL QPGERLERGI QDVYVLSEQQ GLLLKALQPL EEGESEEKVS HQAGDCWLIR 

       370        380        390        400        410        420 
GPLEYVPSAK VEVVEERQAI PLDQNEGIYV QDVKTGKVRA VIGSTYMLTQ DEVLWEKELP 

       430        440        450        460        470        480 
SGVEELLNLG HDPLADRGQK GTAKPLQPSA PRNKTRVVSY RVPHNAAVQV YDYRAKRARV 

       490        500        510        520        530        540 
VFGPELVTLD PEEQFTVLSL SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ 

       550        560        570        580        590        600 
LAYNWHFELK NRNDPAEAAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR 

       610        620        630        640        650        660 
MAVFGFEMSE DTGPDGTLLP KARDQAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL 

       670        680        690        700        710        720 
AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARKELLELE AMSMAVESTG 

       730        740        750        760        770        780 
NAKAEAESRA EAARIEGEGS VLQAKLKAQA LAIETEAELE RVKKVREMEL IYARAQLELE 

       790        800        810        820        830        840 
VSKAQQLANV EAKKFKEMTE ALGPGTIRDL AVAGPEMQVK LLQSLGLKST LITDGSSPIN 

       850        860 
LFSTAFGLLG LGSDGQPPAQ K 

« Hide

References

« Hide 'large scale' references
[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]"Vaults and telomerase share a common subunit, TEP1."
Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O., Rome L.H.
J. Biol. Chem. 274:32712-32717(1999) [PubMed] [Europe PMC] [Abstract]
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]"The structure of rat liver vault at 3.5 Angstrom resolution."
Tanaka H., Kato K., Yamashita E., Sumizawa T., Zhou Y., Yao M., Iwasaki K., Yoshimura M., Tsukihara T.
Science 323:384-388(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), SUBUNIT, MVP REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09870 mRNA. Translation: AAC52161.2.
BC071174 mRNA. Translation: AAH71174.1.
PIRI53908.
RefSeqNP_073206.2. NM_022715.2.
UniGeneRn.10028.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZVX-ray9.00A/B1-861[»]
2ZUOX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L/M1-861[»]
2ZV4X-ray3.50N/O/P/Q/R/S/T/U/V/W/X/Y/Z1-861[»]
2ZV5X-ray3.50a/b/c/d/e/f/g/h/i/j/k/l/m1-861[»]
4HL8X-ray3.50A1-861[»]
ProteinModelPortalQ62667.
SMRQ62667. Positions 1-779.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29532N.
IntActQ62667. 3 interactions.
MINTMINT-1775954.
STRING10116.ENSRNOP00000027360.

PTM databases

PhosphoSiteQ62667.

Proteomic databases

PaxDbQ62667.
PRIDEQ62667.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027360; ENSRNOP00000027360; ENSRNOG00000020182.
GeneID64681.
KEGGrno:64681.
UCSCRGD:70932. rat.

Organism-specific databases

CTD9961.
RGD70932. Mvp.

Phylogenomic databases

eggNOGNOG70525.
GeneTreeENSGT00390000008969.
HOGENOMHOG000255109.
HOVERGENHBG003499.
InParanoidQ62667.
KOK17266.
OMAQDPLADR.
OrthoDBEOG773XFB.
PhylomeDBQ62667.

Gene expression databases

ArrayExpressQ62667.
GenevestigatorQ62667.

Family and domain databases

InterProIPR021870. MVP_shoulder.
IPR002499. Vault_N.
[Graphical view]
PfamPF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 5 hits.
[Graphical view]
PROSITEPS51224. MVP. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ62667.
NextBio613698.
PROQ62667.

Entry information

Entry nameMVP_RAT
AccessionPrimary (citable) accession number: Q62667
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 96 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references