MVP_PONAB
ID MVP_PONAB Reviewed; 893 AA.
AC Q5R9N2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Major vault protein;
DE Short=MVP;
GN Name=MVP;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859354; CAH91528.1; -; mRNA.
DR RefSeq; NP_001125896.1; NM_001132424.1.
DR AlphaFoldDB; Q5R9N2; -.
DR SMR; Q5R9N2; -.
DR STRING; 9601.ENSPPYP00000008203; -.
DR GeneID; 100172829; -.
DR KEGG; pon:100172829; -.
DR CTD; 9961; -.
DR eggNOG; ENOG502QPP0; Eukaryota.
DR InParanoid; Q5R9N2; -.
DR Proteomes; UP000001595; 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 Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14764"
FT CHAIN 2..893
FT /note="Major vault protein"
FT /id="PRO_0000246783"
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 856..893
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 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14764"
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"
SQ SEQUENCE 893 AA; 99234 MW; 7F7C68BC0AE68197 CRC64;
MATEEFIIRI PPYHYIHVLD QNSNVSHVEV GPKTYIRQDN ERVLFAPMRM VTVPPRHYCT
VANPVSRDAQ GLVLFDVTGQ VRLRHADLEI RLAQDPFPLY PGEVLEKDIT PLQVVLPNTA
LHLKALLDFE DKDGDKVVAG DEWLLEGPGT YIPRKEVEVV EIIQATIIRQ NQALRLRARK
ECWDRDGKER VTGEEWLVTT VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARRNFRDFRG
VSRRTGEEWL VTVQDTEAHV PDVHEEVLGV VPITTLGPHN YCVILDPVGP DGKNQLGQKR
VVKGEKSFFL QPGEQLEQGI QDVYVLSEQQ GLLLRALQPL EDGEDEEKVS HQAGDRWLIR
GPLEYVPSAK VEVVEERQAI PLDENEGIYV QDVKTGKVRA VIGSTYMLTQ DEVLWEKELP
PGVEELLNKG QDPLADRGEK DTAKSLQPLA PRNKTRVVSY RVPHNAAVQV YDYREKRARV
VFGPELVSLG PEEQFTVLSL SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ
LAYNWHFQVN DRKDPQETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
AAVFGFETSE AKDPDGMALP RPRDQAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL
AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARKELLELE ALSMAVESTG
TAKAEAESRA EAARIEGEGS VLQAKLKAQA LAIETEAELQ RVQKVRELEL VYARAQLELG
VSKAQQLAEV EVKKFKQMTE AIGPSTIRDL AVAGPEMQVK LLQSLGLKST LITDGSTPIN
LFNTAFGLLG MGPEGQPLGR RVASGPSPGE GISPQSAQAP QAPGDNHVVP VLR
