MVP_BOVIN
ID MVP_BOVIN Reviewed; 890 AA.
AC Q3SYU9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Major vault protein;
DE Short=MVP;
GN Name=MVP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 May interact with ZNF540 (By similarity). {ECO:0000250}.
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; BC103371; AAI03372.1; -; mRNA.
DR RefSeq; NP_001030394.1; NM_001035317.2.
DR AlphaFoldDB; Q3SYU9; -.
DR SMR; Q3SYU9; -.
DR STRING; 9913.ENSBTAP00000010451; -.
DR PaxDb; Q3SYU9; -.
DR PeptideAtlas; Q3SYU9; -.
DR PRIDE; Q3SYU9; -.
DR GeneID; 516456; -.
DR KEGG; bta:516456; -.
DR CTD; 9961; -.
DR eggNOG; ENOG502QPP0; Eukaryota.
DR InParanoid; Q3SYU9; -.
DR OrthoDB; 256008at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; Ubl conjugation.
FT CHAIN 1..890
FT /note="Major vault protein"
FT /id="PRO_0000246782"
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 REGION 425..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14764"
SQ SEQUENCE 890 AA; 98924 MW; 3144AB6D61269BBF CRC64;
MSMEESIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERILFAPVRM LTVPPRHYCM
VANPVARDAQ GTVLFDVTGQ VRLRHADLEI RLAQDPFPLF PGEVLEKDIT PLQVVLPNTA
LHLKALLDFE DKNGQKVVAG DEWLFEGPGT YIPQKEVEVI EIIQATVIKQ NQALRLRARK
ECLDRDGKER VTGEEWLVRS VGAYLPAVFE EVLDVVDAVI LTEKTALHLR ARQNFRDVRG
VTRRTGEEWL VTVQDTEAHV PDVYEEVMGV VSVTTLGPHN YCVILDPVGP DGKNQLGQKL
VFKGEQSFFL QPGEKLERGI QNVYVLSEQQ GLLLRALQPL EEGEGKEKVS HQAGDHWLIR
GPLEYVPPAK VEVVEERQAI PLDENEGIYV QDVKTGRVRA VIGSTYMLTQ DEVLWEKELP
PGVEELLNKG QDPLADRGEK ETSKTPKLST PRNKTRVVSY RVPHNAAVQV YDYREKKARV
VFGPELVLLG PEEQFTVLSL SAGRPKRPHA RRTLCLLLGP DFFTDVITIE TADHARLQLQ
LAYNWHFELS DRKDPQETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
TAVFGFETQE TKGPDTMALP QPRDRAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL
AIEIATNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARRELLELE ALSTAVESTG
TAKAEAESRA EAARIEGEGA VLQAKLKAEA LAIETEAELE RVKKVRELEL LYARAQLELE
VSKAQQLAEV EVKKFKQMTE ALGPSTIRDM AVAGPEMQVK LLQSLGLKST LITDGSTPIN
LFNTALGLLG LGAEAQPPAK KPTGGPSVQE GLLPISTAAP LTLGNNQVVP
