VP24_EBOSU
ID VP24_EBOSU Reviewed; 251 AA.
AC Q5XX02;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Membrane-associated protein VP24;
DE AltName: Full=Reston VP24 {ECO:0000303|PubMed:27974555};
DE Short=rVP24 {ECO:0000303|PubMed:27974555};
GN Name=VP24;
OS Sudan ebolavirus (strain Human/Uganda/Gulu/2000) (SEBOV) (Sudan Ebola
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=386033;
OH NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16139097; DOI=10.1016/j.virusres.2005.03.028;
RA Sanchez A., Rollin P.E.;
RT "Complete genome sequence of an Ebola virus (Sudan species) responsible for
RT a 2000 outbreak of human disease in Uganda.";
RL Virus Res. 113:16-25(2005).
RN [2]
RP INTERACTION WITH HOST KPNA1; KPNA5 AND KPNA6, AND NOMENCLATURE.
RX PubMed=27974555; DOI=10.1128/jvi.01715-16;
RA Schwarz T.M., Edwards M.R., Diederichs A., Alinger J.B., Leung D.W.,
RA Amarasinghe G.K., Basler C.F.;
RT "VP24-Karyopherin Alpha Binding Affinities Differ between Ebolavirus
RT Species, Influencing Interferon Inhibition and VP24 Stability.";
RL J. Virol. 91:0-0(2017).
RN [3] {ECO:0007744|PDB:3VNE, ECO:0007744|PDB:3VNF}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 9-232, AND INTERACTION WITH HOST
RP STAT1.
RX PubMed=22383882; DOI=10.1371/journal.ppat.1002550;
RA Zhang A.P., Bornholdt Z.A., Liu T., Abelson D.M., Lee D.E., Li S.,
RA Woods V.L. Jr., Saphire E.O.;
RT "The ebola virus interferon antagonist VP24 directly binds STAT1 and has a
RT novel, pyramidal fold.";
RL PLoS Pathog. 8:E1002550-E1002550(2012).
CC -!- FUNCTION: Prevents the establishment of cellular antiviral state by
CC blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma
CC signaling pathways. Blocks the IFN-induced nuclear accumulation of host
CC phosphorylated STAT1, by interacting with the STAT1-binding region of
CC host importin alpha-1/KPNA1 protein, thereby inhibiting the latter.
CC Without the activity of this protein, activated STAT1 would not enter
CC the nucleus and be unable to activate IFN-induced genes. Plays a role
CC in assembly of viral nucleocapsid and virion budding. May act as a
CC minor matrix protein that plays a role in assembly of viral
CC nucleocapsid and virion budding.
CC -!- SUBUNIT: Interacts with host importins KPNA1, KPNA5 and KPNA6
CC (PubMed:27974555). Interacts with host STAT1 (PubMed:22383882).
CC {ECO:0000269|PubMed:22383882, ECO:0000269|PubMed:27974555}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Host endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=In virion, localizes on the
CC intravirional side of the membrane. In the host cell, it is found
CC associated with virus-induced membrane proliferation foci and to the
CC plasma membrane where budding takes place (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the filoviridae membrane-associated protein VP24
CC family. {ECO:0000305}.
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DR EMBL; AY729654; AAU43889.1; -; Genomic_RNA.
DR RefSeq; YP_138526.1; NC_006432.1.
DR PDB; 3VNE; X-ray; 2.00 A; A=9-232.
DR PDB; 3VNF; X-ray; 2.10 A; A=13-228.
DR PDBsum; 3VNE; -.
DR PDBsum; 3VNF; -.
DR SMR; Q5XX02; -.
DR DNASU; 3160772; -.
DR GeneID; 3160772; -.
DR KEGG; vg:3160772; -.
DR Proteomes; UP000000277; Genome.
DR GO; GO:0033645; C:host cell endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR InterPro; IPR009433; Filo_VP24.
DR Pfam; PF06389; Filo_VP24; 1.
DR PIRSF; PIRSF011355; VP24; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host membrane; Host-virus interaction;
KW Interferon antiviral system evasion; Membrane; Virion.
FT CHAIN 1..251
FT /note="Membrane-associated protein VP24"
FT /id="PRO_0000245069"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 147..165
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3VNF"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3VNE"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:3VNE"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:3VNE"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3VNE"
SQ SEQUENCE 251 AA; 28277 MW; 1378EDBB6829875A CRC64;
MAKATGRYNL VTPKRELEQG VVFSDLCNFL VTPTVQGWKV YWAGLEFDVN QKGITLLNRL
KVNDFAPAWA MTRNLFPHLF KNQQSEVQTP IWALRVILAA GILDQLMDHS LIEPLSGALN
LIADWLLTTS TNHFNMRTQR VKDQLSMRML SLIRSNIINF INKLETLHVV NYKGLLSSVE
IGTPSYAIII TRTNMGYLVE VQEPDKSAMD IRHPGPVKFS LLHESTLKPV ATPKPSSITS
LIMEFNSSLA I
