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Membrane-associated protein VP24 (Ebola VP24) (eVP24)

 VP24_EBOZM              Reviewed;         251 AA.
Q05322; Q773N1; Q8JS60; Q9DQD2;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
02-JUN-2021, entry version 93.
RecName: Full=Membrane-associated protein VP24;
AltName: Full=Ebola VP24 {ECO:0000303|PubMed:27974555};
Short=eVP24 {ECO:0000303|PubMed:27974555};
Name=VP24;
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
NCBI_TaxID=128952;
NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8237108; DOI=10.1016/0168-1702(93)90063-s;
Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
"Sequence analysis of the Ebola virus genome: organization, genetic
elements, and comparison with the genome of Marburg virus.";
Virus Res. 29:215-240(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=10073695; DOI=10.1099/0022-1317-80-2-355;
Volchkov V.E., Volchkova V.A., Chepurnov A.A., Blinov V.M., Netesov S.V.,
Feldmann H.;
"Characterization of the L gene and 5' trailer region of Ebola virus.";
J. Gen. Virol. 80:355-362(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate guinea pig-adapted;
PubMed=11062045; DOI=10.1006/viro.2000.0572;
Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A., Klenk H.D.;
"Molecular characterization of guinea pig-adapted variants of Ebola
virus.";
Virology 277:147-155(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate mouse-adapted;
Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=12191476; DOI=10.1016/s1097-2765(02)00588-9;
Huang Y., Xu L., Sun Y., Nabel G.J.;
"The assembly of Ebola virus nucleocapsid requires virion-associated
proteins 35 and 24 and posttranslational modification of nucleoprotein.";
Mol. Cell 10:307-316(2002).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12525613; DOI=10.1128/jvi.77.3.1793-1800.2003;
Han Z., Boshra H., Sunyer J.O., Zwiers S.H., Paragas J., Harty R.N.;
"Biochemical and functional characterization of the Ebola virus VP24
protein: implications for a role in virus assembly and budding.";
J. Virol. 77:1793-1800(2003).
[7]
FUNCTION.
PubMed=15220407; DOI=10.1128/jvi.78.14.7344-7351.2004;
Licata J.M., Johnson R.F., Han Z., Harty R.N.;
"Contribution of ebola virus glycoprotein, nucleoprotein, and VP24 to
budding of VP40 virus-like particles.";
J. Virol. 78:7344-7351(2004).
[8]
INTERACTION WITH HOST KPNA1.
PubMed=16698996; DOI=10.1128/jvi.02349-05;
Reid S.P., Leung L.W., Hartman A.L., Martinez O., Shaw M.L.,
Carbonnelle C., Volchkov V.E., Nichol S.T., Basler C.F.;
"Ebola virus VP24 binds karyopherin alpha-1 and blocks STAT1 nuclear
accumulation.";
J. Virol. 80:5156-5167(2006).
[9]
FUNCTION, AND INTERACTION WITH HOST KPNA1; KPNA5 AND KPNA6.
PubMed=17928350; DOI=10.1128/jvi.01097-07;
Reid S.P., Valmas C., Martinez O., Sanchez F.M., Basler C.F.;
"Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily
karyopherin alpha proteins with activated STAT1.";
J. Virol. 81:13469-13477(2007).
[10]
FUNCTION, AND INTERACTION WITH HOST STAT1.
PubMed=22383882; DOI=10.1371/journal.ppat.1002550;
Zhang A.P., Bornholdt Z.A., Liu T., Abelson D.M., Lee D.E., Li S.,
Woods V.L. Jr., Saphire E.O.;
"The ebola virus interferon antagonist VP24 directly binds STAT1 and has a
novel, pyramidal fold.";
PLoS Pathog. 8:E1002550-E1002550(2012).
[11]
FUNCTION, INTERACTION WITH NUCLEOPROTEIN NP AND VP35, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF VAL-170 AND ASN-171.
PubMed=28794491; DOI=10.1038/s41598-017-08167-8;
Banadyga L., Hoenen T., Ambroggio X., Dunham E., Groseth A., Ebihara H.;
"Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and
genome packaging.";
Sci. Rep. 7:7698-7698(2017).
[12]
STRUCTURE BY ELECTRON MICROSCOPY (7.30 ANGSTROMS).
PubMed=29144446; DOI=10.1038/nature24490;
Wan W., Kolesnikova L., Clarke M., Koehler A., Noda T., Becker S.,
Briggs J.A.G.;
"Structure and assembly of the Ebola virus nucleocapsid.";
Nature 551:394-397(2017).
[13]
X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 16-231, INTERACTION WITH HOST
KPNA5, MUTAGENESIS OF ARG-137, AND FUNCTION.
PubMed=25121748; DOI=10.1016/j.chom.2014.07.008;
Xu W., Edwards M.R., Borek D.M., Feagins A.R., Mittal A., Alinger J.B.,
Berry K.N., Yen B., Hamilton J., Brett T.J., Pappu R.V., Leung D.W.,
Basler C.F., Amarasinghe G.K.;
"Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5
to selectively compete with nuclear import of phosphorylated STAT1.";
Cell Host Microbe 16:187-200(2014).
[14]
INTERACTION WITH HOST KPNA1; KPNA5 AND KPNA6, AND NOMENCLATURE.
PubMed=27974555; DOI=10.1128/jvi.01715-16;
Schwarz T.M., Edwards M.R., Diederichs A., Alinger J.B., Leung D.W.,
Amarasinghe G.K., Basler C.F.;
"VP24-Karyopherin Alpha Binding Affinities Differ between Ebolavirus
Species, Influencing Interferon Inhibition and VP24 Stability.";
J. Virol. 91:0-0(2017).
[15]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 11-237, AND INTERACTION WITH HOST
KEAP1.
PubMed=24630991; DOI=10.1016/j.celrep.2014.01.043;
Edwards M.R., Johnson B., Mire C.E., Xu W., Shabman R.S., Speller L.N.,
Leung D.W., Geisbert T.W., Amarasinghe G.K., Basler C.F.;
"The Marburg virus VP24 protein interacts with Keap1 to activate the
cytoprotective antioxidant response pathway.";
Cell Rep. 6:1017-1025(2014).
-!- FUNCTION: Prevents the establishment of cellular antiviral state by
blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma
signaling pathways. Blocks the IFN-induced nuclear accumulation of host
phosphorylated STAT1 by interacting with the STAT1-binding region of
host importins. Alternatively interacts also directly with host STAT1
and may additionally inhibit its non-phosphorylated form. Plays a role
in assembly of viral nucleocapsid and virion budding. May act as a
minor matrix protein that plays a role in assembly of viral
nucleocapsid and virion budding. {ECO:0000269|PubMed:12191476,
ECO:0000269|PubMed:12525613, ECO:0000269|PubMed:15220407,
ECO:0000269|PubMed:17928350, ECO:0000269|PubMed:25121748}.
-!- SUBUNIT: Interacts with host importins KPNA1, KPNA5 and KPNA6
(PubMed:17928350, PubMed:25121748,PubMed:27974555). Interacts with host
STAT1 (PubMed:22383882). Interacts with host KEAP1; this interaction
activates host transcription factor NRF2 by blocking its interaction
with KEAP1 (PubMed:24630991). {ECO:0000269|PubMed:17928350,
ECO:0000269|PubMed:22383882, ECO:0000269|PubMed:24630991,
ECO:0000269|PubMed:25121748}.
-!- INTERACTION:
Q05322; O60684: KPNA6; Xeno; NbExp=7; IntAct=EBI-6153153, EBI-359923;
Q05322; P20700: LMNB1; Xeno; NbExp=6; IntAct=EBI-6153153, EBI-968218;
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:12525613};
Peripheral membrane protein {ECO:0000269|PubMed:12525613}. Host cell
membrane {ECO:0000269|PubMed:12525613}; Peripheral membrane protein
{ECO:0000269|PubMed:12525613}; Cytoplasmic side
{ECO:0000269|PubMed:12525613}. Host endomembrane system
{ECO:0000269|PubMed:12525613}; Peripheral membrane protein
{ECO:0000269|PubMed:12525613}. Note=In virion, localizes on the
intravirional side of the membrane. In the host cell, it is found
associated with virus-induced membrane proliferation foci and to the
plasma membrane where budding takes place (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the filoviridae membrane-associated protein VP24
family. {ECO:0000305}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; L11365; AAB81006.1; -; Genomic_RNA.
EMBL; AF086833; AAD14588.1; -; Genomic_RNA.
EMBL; AF272001; AAG40170.1; -; Genomic_RNA.
EMBL; AY142960; AAN37510.1; -; Genomic_RNA.
EMBL; AF499101; AAM76037.1; -; Genomic_RNA.
RefSeq; NP_066250.1; NC_002549.1.
PDB; 4M0Q; X-ray; 1.92 A; A/B=11-237.
PDB; 4U2X; X-ray; 3.15 A; A/B/C=16-231.
PDB; 6EHM; EM; 7.30 A; C/D=1-251.
PDBsum; 4M0Q; -.
PDBsum; 4U2X; -.
PDBsum; 6EHM; -.
SMR; Q05322; -.
IntAct; Q05322; 91.
DNASU; 911828; -.
GeneID; 911828; -.
KEGG; vg:911828; -.
Proteomes; UP000007209; Genome.
Proteomes; UP000109874; Genome.
Proteomes; UP000149419; Genome.
Proteomes; UP000150973; Genome.
GO; GO:0033645; C:host cell endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IDA:CACAO.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0046774; P:suppression by virus of host intracellular interferon activity; IDA:CACAO.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0046761; P:viral budding from plasma membrane; IDA:CACAO.
InterPro; IPR009433; Filo_VP24.
Pfam; PF06389; Filo_VP24; 1.
PIRSF; PIRSF011355; VP24; 1.
1: Evidence at protein level;
3D-structure; Host cell membrane; Host membrane; Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host STAT1 by virus; Interferon antiviral system evasion;
Membrane; Reference proteome; Viral immunoevasion; Virion.
CHAIN 1..251
/note="Membrane-associated protein VP24"
/id="PRO_0000222154"
VARIANT 50
/note="T -> I (in strain: Isolate mouse-adapted)"
VARIANT 71
/note="M -> I (in strain: Isolate guinea pig-adapted)"
VARIANT 147
/note="L -> P (in strain: Isolate guinea pig-adapted)"
VARIANT 187
/note="T -> I (in strain: Isolate guinea pig-adapted)"
MUTAGEN 137
/note="R->A: More than 90% loss of interaction with host
KPNA5."
/evidence="ECO:0000269|PubMed:25121748"
MUTAGEN 170
/note="V->A: Complete loss of interaction with NP."
/evidence="ECO:0000269|PubMed:28794491"
MUTAGEN 171
/note="N->A: Complete loss of interaction with NP."
/evidence="ECO:0000269|PubMed:28794491"
HELIX 16..26
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 30..33
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 35..42
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 45..50
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 54..60
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 62..65
/evidence="ECO:0007829|PDB:4M0Q"
TURN 67..69
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 70..74
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 77..80
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 85..87
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 90..105
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 108..110
/evidence="ECO:0007829|PDB:4M0Q"
TURN 113..115
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 116..128
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 139..142
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 147..165
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 172..174
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 178..182
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 187..193
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 196..202
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 207..209
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 211..213
/evidence="ECO:0007829|PDB:4M0Q"
STRAND 217..222
/evidence="ECO:0007829|PDB:4M0Q"
HELIX 224..228
/evidence="ECO:0007829|PDB:4M0Q"
SEQUENCE 251 AA; 28219 MW; 5A8F356AF2CC5A5C CRC64;
MAKATGRYNL ISPKKDLEKG VVLSDLCNFL VSQTIQGWKV YWAGIEFDVT HKGMALLHRL
KTNDFAPAWS MTRNLFPHLF QNPNSTIESP LWALRVILAA GIQDQLIDQS LIEPLAGALG
LISDWLLTTN TNHFNMRTQR VKEQLSLKML SLIRSNILKF INKLDALHVV NYNGLLSSIE
IGTQNHTIII TRTNMGFLVE LQEPDKSAMN RMKPGPAKFS LLHESTLKAF TQGSSTRMQS
LILEFNSSLA I


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WP1678: Nucleotide excision repair
WP73: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways

Related Genes :
[VP40] Matrix protein VP40 (Ebola VP40) (eVP40) (Membrane-associated protein VP40)
[MDV038] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) (Virion structural protein UL26) [Cleaved into: Assemblin (EC 3.4.21.97) (Capsid protein VP24) (Protease); Assembly protein (Capsid assembly protein) (Capsid protein VP22A)]
[UL26] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) (Virion structural protein UL26) [Cleaved into: Assemblin (EC 3.4.21.97) (Capsid protein VP24) (Protease); Assembly protein (Capsid assembly protein) (Capsid protein VP22A)]
[35] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) (Virion structural gene 35 protein) [Cleaved into: Assemblin (EC 3.4.21.97) (Capsid protein VP24) (Protease); Assembly protein (Capsid assembly protein) (Capsid protein VP22A)]
[BVRF2] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) (Protein EC-RF3/EC-RF3A) (Virion structural protein BVRF2) [Cleaved into: Assemblin (EC 3.4.21.97) (Capsid protein VP24) (Protease); Assembly protein (Capsid assembly protein) (Capsid protein VP22A)]
[] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Capsid protein VP24) (Protease); Assembly protein (Capsid assembly protein) (Capsid protein VP22A)]
[VP24] Membrane-associated protein VP24 (Marburg VP24) (mVP24)
[] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) (Virion structural protein UL26) [Cleaved into: Assemblin (EC 3.4.21.97) (Capsid protein VP24) (Protease); Assembly protein (Capsid assembly protein) (Capsid protein VP22A)]
[35] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Capsid protein VP24) (Protease); Assembly protein (Capsid assembly protein) (Capsid protein VP22A)]
[17] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Capsid protein VP24) (Protease); Assembly protein (Capsid assembly protein) (Capsid protein VP22A)]
[GP] Envelope glycoprotein (GP1,2) (GP) [Cleaved into: GP1; GP2; Shed GP (GP1,2-delta)]
[VP40] Matrix protein VP40 (Ebola VP40) (eVP40) (Membrane-associated protein VP40)
[KPNA1 RCH2] Importin subunit alpha-5 (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) [Cleaved into: Importin subunit alpha-5, N-terminally processed]
[VP24 vp24] Membrane-associated protein VP24
[KPNA6 IPOA7] Importin subunit alpha-7 (Karyopherin subunit alpha-6)
[STAT1] Signal transducer and activator of transcription 1-alpha/beta (Transcription factor ISGF-3 components p91/p84)
[KPNA5] Importin subunit alpha-6 (Karyopherin subunit alpha-5)
[VP24 DF49_50518gpVP24] Membrane-associated protein VP24
[VP40] Matrix protein VP40 (Marburg VP40) (mVP40) (Membrane-associated protein VP40)
[VP24] Membrane-associated protein VP24 (Marburg VP24) (mVP24)
[VP24] Membrane-associated protein VP24 (Marburg VP24) (mVP24)
[VP24] Membrane-associated protein VP24 (Marburg VP24) (mVP24)
[VP24] Membrane-associated protein VP24 (Marburg VP24) (mVP24)
[NP] Nucleoprotein (Ebola NP) (eNP) (Nucleocapsid protein) (Protein N)
[LMNB1 LMN2 LMNB] Lamin-B1
[UL26] Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) (Virion structural protein UL26) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease); Assembly protein (Capsid assembly protein)]
[NP] Nucleoprotein (Nucleocapsid protein) (Protein N)
[VP40] Matrix protein VP40 (Ebola VP40) (eVP40) (Membrane-associated protein VP40)
[GP] Envelope glycoprotein (GP1,2) (GP) [Cleaved into: Shed GP (GP1,2-delta); GP1; GP2]
[GP] Pre-small/secreted glycoprotein (pre-sGP) [Cleaved into: Small/secreted glycoprotein (sGP); Delta-peptide]

Bibliography :
[29850750] Development of oligonucleotide-based antagonists of Ebola virus protein 24 inhibiting its interaction with karyopherin alpha 1.
[28574091] Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5.
[27974555] VP24-Karyopherin Alpha Binding Affinities Differ between Ebolavirus Species, Influencing Interferon Inhibition and VP24 Stability.
[25121748] Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1.