ID VP24_EBORE Reviewed; 251 AA. AC Q91DD5; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 83. 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 Reston ebolavirus (strain Philippines-96) (REBOV) (Reston Ebola virus). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus; OC Orthoebolavirus restonense; Reston ebolavirus. OX NCBI_TaxID=129003; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OH NCBI_TaxID=77225; Pteropodinae. OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=11722021; DOI=10.1007/s007050170049; RA Ikegami T., Calaor A.B., Miranda M.E., Niikura M., Saijo M., Kurane I., RA Yoshikawa Y., Morikawa S.; RT "Genome structure of Ebola virus subtype Reston: differences among Ebola RT subtypes."; RL Arch. Virol. 146:2021-2027(2001). 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:4D9O} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 11-231, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB050936; BAB69009.1; -; Genomic_RNA. DR PDB; 4D9O; X-ray; 2.00 A; A/B=11-231. DR PDBsum; 4D9O; -. DR SMR; Q91DD5; -. DR Proteomes; UP000002322; 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:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW. 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 Inhibition of host innate immune response by virus; KW Interferon antiviral system evasion; Membrane; Viral immunoevasion; Virion. FT CHAIN 1..251 FT /note="Membrane-associated protein VP24" FT /id="PRO_0000245067" FT HELIX 14..27 FT /evidence="ECO:0007829|PDB:4D9O" FT STRAND 30..33 FT /evidence="ECO:0007829|PDB:4D9O" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:4D9O" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:4D9O" FT HELIX 54..60 FT /evidence="ECO:0007829|PDB:4D9O" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:4D9O" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:4D9O" FT HELIX 90..106 FT /evidence="ECO:0007829|PDB:4D9O" FT HELIX 114..128 FT /evidence="ECO:0007829|PDB:4D9O" FT HELIX 139..142 FT /evidence="ECO:0007829|PDB:4D9O" FT HELIX 147..165 FT /evidence="ECO:0007829|PDB:4D9O" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:4D9O" FT STRAND 187..193 FT /evidence="ECO:0007829|PDB:4D9O" FT STRAND 196..202 FT /evidence="ECO:0007829|PDB:4D9O" FT STRAND 218..222 FT /evidence="ECO:0007829|PDB:4D9O" FT HELIX 224..230 FT /evidence="ECO:0007829|PDB:4D9O" SQ SEQUENCE 251 AA; 28169 MW; DB8F144CA8FB2509 CRC64; MAKATGRYNL VPPKKDMEKG VIFSDLCNFL ITQTLQGWKV YWAGIEFDVS QKGMALLTRL KTNDFAPAWA MTRNLFPHLF QNPNSVIQSP IWALRVILAA GLQDQLLDHS LVEPLTGALG LISDWLLTTT STHFNLRTRS VKDQLSLRML SLIRSNILQF INKLDALHVV NYNGLLSSIE IGTSTHTIII TRTNMGFLVE VQEPDKSAMN SKRPGPVKFS LLHESAFKPF TRVPQSGMQS LIMEFNSLLA I //