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Protein

Major vault protein

Gene

Mvp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 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 IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity).By similarity

GO - Biological processi

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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi70932. Mvp.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001589822 – 861Major vault proteinAdd BLAST860

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei421PhosphoserineCombined sources1
Cross-linki444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ62667.
PRIDEiQ62667.

PTM databases

iPTMnetiQ62667.
PhosphoSitePlusiQ62667.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020182.
GenevisibleiQ62667. RN.

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 interactors.
MINTiMINT-1775954.
STRINGi10116.ENSRNOP00000027360.

Structurei

Secondary structure

1861
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 20Combined sources7
Turni21 – 24Combined sources4
Beta strandi25 – 33Combined sources9
Beta strandi51 – 53Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi61 – 63Combined sources3
Beta strandi79 – 81Combined sources3
Beta strandi93 – 97Combined sources5
Beta strandi109 – 111Combined sources3
Beta strandi119 – 127Combined sources9
Beta strandi144 – 146Combined sources3
Beta strandi155 – 164Combined sources10
Beta strandi172 – 183Combined sources12
Beta strandi200 – 202Combined sources3
Beta strandi210 – 217Combined sources8
Beta strandi223 – 236Combined sources14
Beta strandi248 – 251Combined sources4
Turni253 – 255Combined sources3
Beta strandi257 – 259Combined sources3
Beta strandi265 – 275Combined sources11
Beta strandi280 – 286Combined sources7
Beta strandi292 – 294Combined sources3
Beta strandi299 – 305Combined sources7
Beta strandi307 – 309Combined sources3
Beta strandi315 – 322Combined sources8
Beta strandi324 – 326Combined sources3
Beta strandi331 – 336Combined sources6
Beta strandi342 – 347Combined sources6
Beta strandi356 – 359Combined sources4
Beta strandi361 – 365Combined sources5
Beta strandi369 – 377Combined sources9
Beta strandi387 – 392Combined sources6
Turni393 – 396Combined sources4
Beta strandi397 – 404Combined sources8
Beta strandi412 – 414Combined sources3
Helixi423 – 426Combined sources4
Beta strandi459 – 461Combined sources3
Beta strandi466 – 472Combined sources7
Turni473 – 476Combined sources4
Beta strandi477 – 484Combined sources8
Beta strandi486 – 488Combined sources3
Beta strandi493 – 495Combined sources3
Beta strandi498 – 502Combined sources5
Turni503 – 506Combined sources4
Beta strandi507 – 517Combined sources11
Beta strandi519 – 521Combined sources3
Beta strandi525 – 530Combined sources6
Beta strandi536 – 541Combined sources6
Beta strandi544 – 547Combined sources4
Helixi555 – 559Combined sources5
Helixi560 – 563Combined sources4
Helixi567 – 583Combined sources17
Helixi588 – 603Combined sources16
Turni629 – 631Combined sources3
Beta strandi633 – 637Combined sources5
Beta strandi644 – 647Combined sources4
Helixi648 – 757Combined sources110
Helixi759 – 802Combined sources44
Helixi806 – 811Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62667.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati2 – 56MVP 1PROSITE-ProRule annotation1 PublicationAdd BLAST55
Repeati57 – 111MVP 2PROSITE-ProRule annotation1 PublicationAdd BLAST55
Repeati112 – 164MVP 3PROSITE-ProRule annotation1 PublicationAdd BLAST53
Repeati165 – 217MVP 4PROSITE-ProRule annotation1 PublicationAdd BLAST53
Repeati218 – 272MVP 5PROSITE-ProRule annotation1 PublicationAdd BLAST55
Repeati273 – 323MVP 6PROSITE-ProRule annotation1 PublicationAdd BLAST51
Repeati324 – 379MVP 7PROSITE-ProRule annotation1 PublicationAdd BLAST56
Repeati380 – 457MVP 8PROSITE-ProRule annotation1 PublicationAdd BLAST78
Repeati458 – 520MVP 9PROSITE-ProRule annotation1 PublicationAdd BLAST63

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

eggNOGiENOG410IF6T. Eukaryota.
ENOG410ZCU8. LUCA.
HOGENOMiHOG000255109.
HOVERGENiHBG003499.
InParanoidiQ62667.
KOiK17266.
OrthoDBiEOG091G032A.
PhylomeDBiQ62667.

Family and domain databases

CDDicd08825. MVP_shoulder. 1 hit.
InterProiIPR021870. MVP_shoulder.
IPR002499. Vault_N.
[Graphical view]
PfamiPF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 4 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

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ62667.
PhosphoSitePlusiQ62667.

Proteomic databases

PaxDbiQ62667.
PRIDEiQ62667.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64681.
KEGGirno:64681.
UCSCiRGD:70932. rat.

Organism-specific databases

CTDi9961.
RGDi70932. Mvp.

Phylogenomic databases

eggNOGiENOG410IF6T. Eukaryota.
ENOG410ZCU8. LUCA.
HOGENOMiHOG000255109.
HOVERGENiHBG003499.
InParanoidiQ62667.
KOiK17266.
OrthoDBiEOG091G032A.
PhylomeDBiQ62667.

Miscellaneous databases

EvolutionaryTraceiQ62667.
PROiQ62667.

Gene expression databases

BgeeiENSRNOG00000020182.
GenevisibleiQ62667. RN.

Family and domain databases

CDDicd08825. MVP_shoulder. 1 hit.
InterProiIPR021870. MVP_shoulder.
IPR002499. Vault_N.
[Graphical view]
PfamiPF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 4 hits.
[Graphical view]
PROSITEiPS51224. MVP. 8 hits.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 115 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

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 one 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.