MVP_RAT
ID MVP_RAT Reviewed; 861 AA.
AC Q62667;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Major vault protein;
DE Short=MVP;
GN Name=Mvp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7828886; DOI=10.1016/0378-1119(94)90667-x;
RA Kickhoefer V.A., Rome L.H.;
RT "The sequence of a cDNA encoding the major vault protein from Rattus
RT norvegicus.";
RL Gene 151:257-260(1994).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Kickhoefer V.A.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP ASSOCIATION WITH TEP1.
RX PubMed=10551828; DOI=10.1074/jbc.274.46.32712;
RA Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O., Rome L.H.;
RT "Vaults and telomerase share a common subunit, TEP1.";
RL J. Biol. Chem. 274:32712-32717(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (9.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=18044992; DOI=10.1371/journal.pbio.0050318;
RA Anderson D.H., Kickhoefer V.A., Sievers S.A., Rome L.H., Eisenberg D.;
RT "Draft crystal structure of the vault shell at 9-A resolution.";
RL PLoS Biol. 5:E318-E318(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), SUBUNIT, AND MVP REPEATS.
RX PubMed=19150846; DOI=10.1126/science.1164975;
RA Tanaka H., Kato K., Yamashita E., Sumizawa T., Zhou Y., Yao M., Iwasaki K.,
RA Yoshimura M., Tsukihara T.;
RT "The structure of rat liver vault at 3.5 Angstrom resolution.";
RL Science 323:384-388(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 TEP1.
CC Interacts with PTEN and activated MAPK1. The phosphorylated protein
CC interacts with the SH2 domains of PTPN11 and SRC. Interacts with APEX1
CC (By similarity). May interact with ZNF540 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q62667; P06536: Nr3c1; NbExp=2; IntAct=EBI-918333, EBI-1187143;
CC Q62667; P04150: NR3C1; Xeno; NbExp=2; IntAct=EBI-918333, EBI-493507;
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; U09870; AAC52161.2; -; mRNA.
DR EMBL; BC071174; AAH71174.1; -; mRNA.
DR PIR; I53908; I53908.
DR RefSeq; NP_073206.2; NM_022715.2.
DR PDB; 2QZV; X-ray; 9.00 A; A/B=1-861.
DR PDB; 4HL8; X-ray; 3.50 A; A=1-861.
DR PDB; 4V60; X-ray; 3.50 A; A/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/m=1-861.
DR PDB; 6BP7; EM; 4.90 A; A=1-861.
DR PDB; 6BP8; EM; 4.90 A; A=1-861.
DR PDB; 7PKR; EM; 3.80 A; A/AA/AB/AC/B/BA/BB/C/CA/CB/D/DA/DB/E/EA/EB/F/FA/FB/G/GA/GB/H/HA/HB/I/IA/IB/J/JA=1-861.
DR PDB; 7PKY; EM; 7.90 A; A/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=1-861.
DR PDB; 7PKZ; EM; 9.80 A; A/AA/AB/AC/B/BA/BB/C/CA/CB/D/DA/DB/E/EA/EB/F/FA/FB/G/GA/GB/H/HA/HB/I/IA/IB/J/JA=1-861.
DR PDBsum; 2QZV; -.
DR PDBsum; 4HL8; -.
DR PDBsum; 4V60; -.
DR PDBsum; 6BP7; -.
DR PDBsum; 6BP8; -.
DR PDBsum; 7PKR; -.
DR PDBsum; 7PKY; -.
DR PDBsum; 7PKZ; -.
DR AlphaFoldDB; Q62667; -.
DR SMR; Q62667; -.
DR BioGRID; 249195; 1.
DR DIP; DIP-29532N; -.
DR IntAct; Q62667; 7.
DR STRING; 10116.ENSRNOP00000027360; -.
DR iPTMnet; Q62667; -.
DR PhosphoSitePlus; Q62667; -.
DR jPOST; Q62667; -.
DR PaxDb; Q62667; -.
DR PRIDE; Q62667; -.
DR GeneID; 64681; -.
DR KEGG; rno:64681; -.
DR UCSC; RGD:70932; rat.
DR CTD; 9961; -.
DR RGD; 70932; Mvp.
DR eggNOG; ENOG502QPP0; Eukaryota.
DR HOGENOM; CLU_016171_0_0_1; -.
DR InParanoid; Q62667; -.
DR PhylomeDB; Q62667; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; Q62667; -.
DR PRO; PR:Q62667; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q62667; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0038127; P:ERBB signaling pathway; ISO:RGD.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:RGD.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0072376; P:protein activation cascade; ISO:RGD.
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_0000158982"
FT REPEAT 2..56
FT /note="MVP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REPEAT 57..111
FT /note="MVP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REPEAT 112..164
FT /note="MVP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REPEAT 165..217
FT /note="MVP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REPEAT 218..272
FT /note="MVP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REPEAT 273..323
FT /note="MVP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REPEAT 324..379
FT /note="MVP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REPEAT 380..457
FT /note="MVP 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REPEAT 458..520
FT /note="MVP 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00571,
FT ECO:0000269|PubMed:19150846"
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14764"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 STRAND 14..20
FT /evidence="ECO:0007829|PDB:4HL8"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 172..183
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 223..236
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:4HL8"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:4HL8"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 397..404
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:4HL8"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:4HL8"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 477..484
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:4HL8"
FT TURN 503..506
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 507..517
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 544..547
FT /evidence="ECO:0007829|PDB:4HL8"
FT HELIX 555..559
FT /evidence="ECO:0007829|PDB:4HL8"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:4HL8"
FT HELIX 567..583
FT /evidence="ECO:0007829|PDB:4HL8"
FT HELIX 588..603
FT /evidence="ECO:0007829|PDB:4HL8"
FT TURN 629..631
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:4HL8"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:4HL8"
FT HELIX 648..757
FT /evidence="ECO:0007829|PDB:4HL8"
FT HELIX 759..802
FT /evidence="ECO:0007829|PDB:4HL8"
FT HELIX 806..811
FT /evidence="ECO:0007829|PDB:4HL8"
SQ SEQUENCE 861 AA; 95798 MW; E51604F295D49A93 CRC64;
MATEEAIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPVRM VTVPPRHYCI
VANPVSRDTQ SSVLFDITGQ VRLRHADQEI RLAQDPFPLY PGEVLEKDIT PLQVVLPNTA
LHLKALLDFE DKNGDKVMAG DEWLFEGPGT YIPQKEVEVV EIIQATVIKQ NQALRLRARK
ECFDREGKGR VTGEEWLVRS VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ALQNFRDLRG
VLHRTGEEWL VTVQDTEAHV PDVYEEVLGV VPITTLGPRH YCVILDPMGP DGKNQLGQKR
VVKGEKSFFL QPGERLERGI QDVYVLSEQQ GLLLKALQPL EEGESEEKVS HQAGDCWLIR
GPLEYVPSAK VEVVEERQAI PLDQNEGIYV QDVKTGKVRA VIGSTYMLTQ DEVLWEKELP
SGVEELLNLG HDPLADRGQK GTAKPLQPSA PRNKTRVVSY RVPHNAAVQV YDYRAKRARV
VFGPELVTLD PEEQFTVLSL SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ
LAYNWHFELK NRNDPAEAAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
MAVFGFEMSE DTGPDGTLLP KARDQAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL
AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARKELLELE AMSMAVESTG
NAKAEAESRA EAARIEGEGS VLQAKLKAQA LAIETEAELE RVKKVREMEL IYARAQLELE
VSKAQQLANV EAKKFKEMTE ALGPGTIRDL AVAGPEMQVK LLQSLGLKST LITDGSSPIN
LFSTAFGLLG LGSDGQPPAQ K
