MVP_MOUSE
ID MVP_MOUSE Reviewed; 861 AA.
AC Q9EQK5; Q922X6;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Major vault protein;
DE Short=MVP;
GN Name=Mvp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Wiemer E.A.C., Mossink M.H., van Zon A., Schoester M., de Boevere M.,
RA Scheper R.J., Sonneveld P.;
RT "Isolation and characterization of the major vault protein and vault RNA
RT from Mus musculus.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ASSOCIATION WITH TEP1.
RX PubMed=11149928; DOI=10.1083/jcb.152.1.157;
RA Kickhoefer V.A., Liu Y., Kong L.B., Snow B.E., Stewart P.L., Harrington L.,
RA Rome L.H.;
RT "The telomerase/vault-associated protein TEP1 is required for vault RNA
RT stability and its association with the vault particle.";
RL J. Cell Biol. 152:157-164(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-383, AND SUBUNIT.
RX PubMed=19779459; DOI=10.1038/emboj.2009.274;
RA Querol-Audi J., Casanas A., Uson I., Luque D., Caston J.R., Fita I.,
RA Verdaguer N.;
RT "The mechanism of vault opening from the high resolution structure of the
RT N-terminal repeats of MVP.";
RL EMBO J. 28:3450-3457(2009).
CC -!- FUNCTION: Required for normal vault structure. Vaults are multi-subunit
CC structures that may act as scaffolds for proteins involved in signal
CC transduction. Vaults may also play a role in nucleo-cytoplasmic
CC transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent
CC activation of JAK. Down-regulates SRC activity and signaling through
CC MAP kinases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The vault ribonucleoprotein particle is a huge (400 A x 670 A)
CC cage structure of 12.9 MDa. It consists of a dimer of half-vaults, with
CC each half-vault comprising 39 identical major vault protein (MVP)
CC chains, PARP4 and one or more vault RNAs (vRNAs). Interacts with PTEN
CC and activated MAPK1. The phosphorylated protein interacts with the SH2
CC domains of PTPN11 and SRC. Interacts with APEX1 (By similarity). May
CC interact with ZNF540 (By similarity). Interacts with TEP1.
CC {ECO:0000250, ECO:0000269|PubMed:19779459}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14764}. Nucleus
CC {ECO:0000250|UniProtKB:Q14764}.
CC -!- DOMAIN: MVP 3 mediates interaction with PTEN. {ECO:0000250}.
CC -!- DOMAIN: MVP 4 mediates interaction with PARP4. {ECO:0000250}.
CC -!- PTM: Phosphorylated on Tyr residues after EGF stimulation.
CC {ECO:0000250}.
CC -!- PTM: Dephosphorylated by PTPN11. {ECO:0000250}.
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DR EMBL; AF210456; AAG43520.1; -; mRNA.
DR EMBL; AY046318; AAL02325.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL17488.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL17489.1; -; Genomic_DNA.
DR EMBL; BC006709; AAH06709.1; -; mRNA.
DR RefSeq; XP_011240254.1; XM_011241952.2.
DR PDB; 3GF5; X-ray; 2.50 A; A/B=1-383.
DR PDB; 3GNF; X-ray; 2.10 A; B=1-383.
DR PDB; 3GNG; X-ray; 3.00 A; A=1-383.
DR PDBsum; 3GF5; -.
DR PDBsum; 3GNF; -.
DR PDBsum; 3GNG; -.
DR AlphaFoldDB; Q9EQK5; -.
DR SMR; Q9EQK5; -.
DR STRING; 10090.ENSMUSP00000127250; -.
DR iPTMnet; Q9EQK5; -.
DR PhosphoSitePlus; Q9EQK5; -.
DR SwissPalm; Q9EQK5; -.
DR REPRODUCTION-2DPAGE; Q9EQK5; -.
DR EPD; Q9EQK5; -.
DR jPOST; Q9EQK5; -.
DR MaxQB; Q9EQK5; -.
DR PaxDb; Q9EQK5; -.
DR PeptideAtlas; Q9EQK5; -.
DR PRIDE; Q9EQK5; -.
DR ProteomicsDB; 287334; -.
DR ABCD; Q9EQK5; 1 sequenced antibody.
DR DNASU; 78388; -.
DR GeneID; 78388; -.
DR CTD; 9961; -.
DR MGI; MGI:1925638; Mvp.
DR eggNOG; ENOG502QPP0; Eukaryota.
DR InParanoid; Q9EQK5; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 78388; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Mvp; mouse.
DR EvolutionaryTrace; Q9EQK5; -.
DR PRO; PR:Q9EQK5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9EQK5; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0038127; P:ERBB signaling pathway; ISO:MGI.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0072376; P:protein activation cascade; IMP:UniProtKB.
DR CDD; cd08825; MVP_shoulder; 1.
DR Gene3D; 2.30.30.550; -; 4.
DR Gene3D; 2.30.30.560; -; 2.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR039059; MVP.
DR InterPro; IPR041139; MVP_rep_dom.
DR InterPro; IPR043023; MVP_rep_sf.
DR InterPro; IPR021870; MVP_shoulder.
DR InterPro; IPR041134; Vault_2.
DR InterPro; IPR043179; Vault_2_sf.
DR InterPro; IPR040989; Vault_3.
DR InterPro; IPR041136; Vault_4.
DR InterPro; IPR002499; Vault_N.
DR PANTHER; PTHR14165; PTHR14165; 1.
DR Pfam; PF11978; MVP_shoulder; 1.
DR Pfam; PF01505; Vault; 4.
DR Pfam; PF17794; Vault_2; 2.
DR Pfam; PF17795; Vault_3; 1.
DR Pfam; PF17796; Vault_4; 1.
DR PROSITE; PS51224; MVP; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14764"
FT CHAIN 2..861
FT /note="Major vault protein"
FT /id="PRO_0000158981"
FT REPEAT 2..56
FT /note="MVP 1"
FT REPEAT 57..111
FT /note="MVP 2"
FT REPEAT 112..164
FT /note="MVP 3"
FT REPEAT 165..217
FT /note="MVP 4"
FT REPEAT 218..272
FT /note="MVP 5"
FT REPEAT 273..323
FT /note="MVP 6"
FT REPEAT 324..379
FT /note="MVP 7"
FT REPEAT 380..457
FT /note="MVP 8"
FT REPEAT 458..520
FT /note="MVP 9"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14764"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62667"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14764"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14764"
FT CONFLICT 348
FT /note="K -> R (in Ref. 1; AAG43520)"
FT /evidence="ECO:0000305"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:3GNF"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 26..36
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3GNG"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 172..183
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3GF5"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3GNG"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:3GNF"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3GF5"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:3GNF"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:3GNF"
SQ SEQUENCE 861 AA; 95924 MW; B722F4FA747CA378 CRC64;
MATEEAIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPVRM VTVPPRHYCI
VANPVSRDAQ SSVLFDVTGQ VRLRHADQEI RLAQDPFPLY PGELLEKDIT PLQVVLPNTA
LHLKALLDFE DKNGDKVMAG DEWLFEGPGT YIPQKEVEVV EIIQATVIKQ NQALRLRARK
ECFDRDGKER VTGEEWLVRS VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARQNFKDLRG
VAHRTGEEWL VTVQDTEAHV PDVYEEVLGV VPITTLGPRH YCVILDPMGP DGKNQLGQKR
VVKGEKSFFL QPGERLERGI QDVYVLSEQQ GLLLKALQPL EEGEGEEKVA HQAGDRWLIR
GPLEYVPSAK VEVVEERQAI PLDQNEGIYV QDVKTGKVRA VIGSTYMLTQ DEVLWEKELP
SGVEELLNLG HDPLADRGQK GTAKVLQPSA ARNKTRVVSY RVPHNAAVQV YDYRAKRARV
VFGPELVSLD PEEQFTVLSL SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ
LAYNWHFELK NRNDPEETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
MAVFGFEMSE DAGPDGALLP RARDRAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL
AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARKELLELE AMSMAVESTG
NAKAEAESRA EAARIEGEGS VLQAKLKAQA LAIETEAELE RVKKVREMEL IYSRAQLELE
VSKAQQLADV EAKKFKEMTE ALGPGTIRDL AVAGPEMQVK LLQSLGLKST LITDGSSPIN
LFNTAFGLLG LGSDGQPPVQ K
