VP35_EBOZM
ID VP35_EBOZM Reviewed; 340 AA.
AC Q05127; Q77LU7; Q8JS63;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Polymerase cofactor VP35;
DE AltName: Full=Ebola VP35 {ECO:0000303|PubMed:26962215};
DE Short=eVP35 {ECO:0000303|PubMed:26962215};
GN Name=VP35;
OS Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128952;
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=8482365; DOI=10.1016/0014-5793(93)81107-b;
RA Bukreyev A.A., Volchkov V.E., Blinov V.M., Netesov S.V.;
RT "The VP35 and VP40 proteins of filoviruses. Homology between Marburg and
RT Ebola viruses.";
RL FEBS Lett. 322:41-46(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8237108; DOI=10.1016/0168-1702(93)90063-s;
RA Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
RT "Sequence analysis of the Ebola virus genome: organization, genetic
RT elements, and comparison with the genome of Marburg virus.";
RL Virus Res. 29:215-240(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10073695; DOI=10.1099/0022-1317-80-2-355;
RA Volchkov V.E., Volchkova V.A., Chepurnov A.A., Blinov V.M., Netesov S.V.,
RA Feldmann H.;
RT "Characterization of the L gene and 5' trailer region of Ebola virus.";
RL J. Gen. Virol. 80:355-362(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate guinea pig-adapted;
RX PubMed=11062045; DOI=10.1006/viro.2000.0572;
RA Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A., Klenk H.D.;
RT "Molecular characterization of guinea pig-adapted variants of Ebola
RT virus.";
RL Virology 277:147-155(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate mouse-adapted;
RA Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION IN VIRAL REPLICATION.
RX PubMed=9971816; DOI=10.1128/jvi.73.3.2333-2342.1999;
RA Muhlberger E., Weik M., Volchkov V.E., Klenk H.D., Becker S.;
RT "Comparison of the transcription and replication strategies of marburg
RT virus and Ebola virus by using artificial replication systems.";
RL J. Virol. 73:2333-2342(1999).
RN [7]
RP FUNCTION.
RX PubMed=11027311; DOI=10.1073/pnas.220398297;
RA Basler C.F., Wang X., Muhlberger E., Volchkov V.E., Paragas J., Klenk H.D.,
RA Garcia-Sastre A., Palese P.;
RT "The Ebola virus VP35 protein functions as a type I IFN antagonist.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12289-12294(2000).
RN [8]
RP INTERACTION WITH THE NUCLEOPROTEIN.
RX PubMed=12191476; DOI=10.1016/s1097-2765(02)00588-9;
RA Huang Y., Xu L., Sun Y., Nabel G.J.;
RT "The assembly of Ebola virus nucleocapsid requires virion-associated
RT proteins 35 and 24 and posttranslational modification of nucleoprotein.";
RL Mol. Cell 10:307-316(2002).
RN [9]
RP FUNCTION.
RX PubMed=12829834; DOI=10.1128/jvi.77.14.7945-7956.2003;
RA Basler C.F., Mikulasova A., Martinez-Sobrido L., Paragas J., Muhlberger E.,
RA Bray M., Klenk H.D., Palese P., Garcia-Sastre A.;
RT "The Ebola virus VP35 protein inhibits activation of interferon regulatory
RT factor 3.";
RL J. Virol. 77:7945-7956(2003).
RN [10]
RP MUTAGENESIS OF ARG-305; LYS-309 AND ARG-312.
RX PubMed=15464838; DOI=10.1016/j.virol.2004.07.006;
RA Hartman A.L., Towner J.S., Nichol S.T.;
RT "A C-terminal basic amino acid motif of Zaire ebolavirus VP35 is essential
RT for type I interferon antagonism and displays high identity with the RNA-
RT binding domain of another interferon antagonist, the NS1 protein of
RT influenza A virus.";
RL Virology 328:177-184(2004).
RN [11]
RP SUBUNIT, AND MUTAGENESIS OF 90-LEU--LEU-93 AND LEU-107.
RX PubMed=16095644; DOI=10.1016/j.virol.2005.06.044;
RA Reid S.P., Cardenas W.B., Basler C.F.;
RT "Homo-oligomerization facilitates the interferon-antagonist activity of the
RT ebolavirus VP35 protein.";
RL Virology 341:179-189(2005).
RN [12]
RP CHARACTERIZATION OF RNA-BINDING ACTIVITY, AND MUTAGENESIS OF LYS-309 AND
RP ARG-312.
RX PubMed=16698997; DOI=10.1128/jvi.02199-05;
RA Cardenas W.B., Loo Y.M., Gale M. Jr., Hartman A.L., Kimberlin C.R.,
RA Martinez-Sobrido L., Saphire E.O., Basler C.F.;
RT "Ebola virus VP35 Protein binds double-Stranded RNA and inhibits alpha/beta
RT interferon production induced by RIG-I signaling.";
RL J. Virol. 80:5168-5178(2006).
RN [13]
RP INTERACTION WITH VP40.
RX PubMed=16698994; DOI=10.1128/jvi.01857-05;
RA Johnson R.F., McCarthy S.E., Godlewski P.J., Harty R.N.;
RT "Ebola virus VP35-VP40 interaction is sufficient for packaging 3E-5E
RT minigenome RNA into virus-like particles.";
RL J. Virol. 80:5135-5144(2006).
RN [14]
RP FUNCTION.
RX PubMed=16495261; DOI=10.1128/aac.50.3.984-993.2006;
RA Enterlein S., Warfield K.L., Swenson D.L., Stein D.A., Smith J.L.,
RA Gamble C.S., Kroeker A.D., Iversen P.L., Bavari S., Muhlberger E.;
RT "VP35 knockdown inhibits Ebola virus amplification and protects against
RT lethal infection in mice.";
RL Antimicrob. Agents Chemother. 50:984-993(2006).
RN [15]
RP FUNCTION.
RX PubMed=17065211; DOI=10.1128/jvi.01006-06;
RA Feng Z., Cerveny M., Yan Z., He B.;
RT "The VP35 protein of Ebola virus inhibits the antiviral effect mediated by
RT double-stranded RNA-dependent protein kinase PKR.";
RL J. Virol. 81:182-192(2007).
RN [16]
RP FUNCTION, INTERACTION WITH HOST IKBKE AND TBK1, AND PHOSPHORYLATION BY HOST
RP IKBKE.
RX PubMed=19153231; DOI=10.1128/jvi.01875-08;
RA Prins K.C., Cardenas W.B., Basler C.F.;
RT "Ebola virus protein VP35 impairs the function of interferon regulatory
RT factor-activating kinases IKKepsilon and TBK-1.";
RL J. Virol. 83:3069-3077(2009).
RN [17]
RP FUNCTION, AND INTERACTION WITH HOST IRF7; PIAS1 AND UBE2I.
RX PubMed=19557165; DOI=10.1371/journal.ppat.1000493;
RA Chang T.H., Kubota T., Matsuoka M., Jones S., Bradfute S.B., Bray M.,
RA Ozato K.;
RT "Ebola Zaire virus blocks type I interferon production by exploiting the
RT host SUMO modification machinery.";
RL PLoS Pathog. 5:e1000493-e1000493(2009).
RN [18]
RP FUNCTION, AND NOMENCLATURE.
RX PubMed=26962215; DOI=10.1128/jvi.00191-16;
RA Yen B.C., Basler C.F.;
RT "Effects of Filovirus Interferon Antagonists on Responses of Human
RT Monocyte-Derived Dendritic Cells to RNA Virus Infection.";
RL J. Virol. 90:5108-5118(2016).
RN [19]
RP INTERACTION WITH HOST DYNLL1, AND MOTIF.
RX PubMed=19403681; DOI=10.1128/jvi.00480-09;
RA Kubota T., Matsuoka M., Chang T.H., Bray M., Jones S., Tashiro M., Kato A.,
RA Ozato K.;
RT "Ebolavirus VP35 interacts with the cytoplasmic dynein light chain 8.";
RL J. Virol. 83:6952-6956(2009).
RN [20]
RP FUNCTION, INTERACTION WITH HOST PRKRA; DSRNA AND POLYMERASE L, AND
RP MUTAGENESIS OF PHE-239 AND ARG-312.
RX PubMed=23870315; DOI=10.1016/j.chom.2013.06.010;
RA Luthra P., Ramanan P., Mire C.E., Weisend C., Tsuda Y., Yen B., Liu G.,
RA Leung D.W., Geisbert T.W., Ebihara H., Amarasinghe G.K., Basler C.F.;
RT "Mutual antagonism between the Ebola virus VP35 protein and the RIG-I
RT activator PACT determines infection outcome.";
RL Cell Host Microbe 14:74-84(2013).
RN [21]
RP INTERACTION WITH HOST DYNLL1, AND FUNCTION.
RX PubMed=25741013; DOI=10.1128/jvi.03652-14;
RA Luthra P., Jordan D.S., Leung D.W., Amarasinghe G.K., Basler C.F.;
RT "Ebola virus VP35 interaction with dynein LC8 regulates viral RNA
RT synthesis.";
RL J. Virol. 89:5148-5153(2015).
RN [22]
RP INTERACTION WITH VP24.
RX PubMed=28794491; DOI=10.1038/s41598-017-08167-8;
RA Banadyga L., Hoenen T., Ambroggio X., Dunham E., Groseth A., Ebihara H.;
RT "Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and
RT genome packaging.";
RL Sci. Rep. 7:7698-7698(2017).
RN [23]
RP INTERACTION WITH VP30, AND SUBCELLULAR LOCATION.
RX PubMed=23493393; DOI=10.1074/jbc.m113.461285;
RA Biedenkopf N., Hartlieb B., Hoenen T., Becker S.;
RT "Phosphorylation of Ebola virus VP30 influences the composition of the
RT viral nucleocapsid complex: impact on viral transcription and
RT replication.";
RL J. Biol. Chem. 288:11165-11174(2013).
RN [24]
RP INTERACTION WITH HOST TRIM6, SUBCELLULAR LOCATION, AND UBIQUITINATION AT
RP LYS-309.
RX PubMed=28679761; DOI=10.1128/jvi.00833-17;
RA Bharaj P., Atkins C., Luthra P., Giraldo M.I., Dawes B.E., Miorin L.,
RA Johnson J.R., Krogan N.J., Basler C.F., Freiberg A.N., Rajsbaum R.;
RT "The Host E3-Ubiquitin Ligase TRIM6 Ubiquitinates the Ebola Virus VP35
RT Protein and Promotes Virus Replication.";
RL J. Virol. 91:0-0(2017).
RN [25]
RP INTERACTION WITH HOST STAU1.
RX PubMed=30301857; DOI=10.1128/mbio.01771-18;
RA Fang J., Pietzsch C., Ramanathan P., Santos R.I., Ilinykh P.A.,
RA Garcia-Blanco M.A., Bukreyev A., Bradrick S.S.;
RT "Staufen1 Interacts with Multiple Components of the Ebola Virus
RT Ribonucleoprotein and Enhances Viral RNA Synthesis.";
RL MBio 9:0-0(2018).
RN [26]
RP PHOSPHORYLATION AT SER-187; SER-205; THR-206; SER-208 AND SER-317, AND
RP MUTAGENESIS OF SER-187 AND SER-317.
RX PubMed=31694758; DOI=10.1016/j.bbrc.2019.10.147;
RA Zhu L., Gao T., Yang W., Liu Y., Liu X., Hu Y., Jin Y., Li P., Xu K.,
RA Zou G., Zhao L., Cao R., Zhong W., Xia X., Cao C.;
RT "Ebola virus replication is regulated by the phosphorylation of viral
RT protein VP35.";
RL Biochem. Biophys. Res. Commun. 521:687-692(2020).
RN [27]
RP PHOSPHORYLATION AT SER-187; SER-205; THR-206; THR-207; SER-208; THR-210;
RP SER-310 AND SER-317, INTERACTION WITH THE NUCLEOPROTEIN, AND MUTAGENESIS OF
RP THR-210.
RX PubMed=31562565; DOI=10.1007/s00018-019-03303-1;
RA Ivanov A., Ramanathan P., Parry C., Ilinykh P.A., Lin X., Petukhov M.,
RA Obukhov Y., Ammosova T., Amarasinghe G.K., Bukreyev A., Nekhai S.;
RT "Global phosphoproteomic analysis of Ebola virions reveals a novel role for
RT VP35 phosphorylation-dependent regulation of genome transcription.";
RL Cell. Mol. Life Sci. 77:2579-2603(2020).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 215-340, MUTAGENESIS OF ARG-312,
RP RNA-BINDING, AND DOMAIN.
RX PubMed=19122151; DOI=10.1073/pnas.0807854106;
RA Leung D.W., Ginder N.D., Fulton D.B., Nix J., Basler C.F., Honzatko R.B.,
RA Amarasinghe G.K.;
RT "Structure of the Ebola VP35 interferon inhibitory domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:411-416(2009).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 215-340, INTERACTION WITH DSRNA,
RP AND MUTAGENESIS OF LYS-319 AND ARG-322.
RX PubMed=20071589; DOI=10.1128/jvi.02459-09;
RA Prins K.C., Delpeut S., Leung D.W., Reynard O., Volchkova V.A., Reid S.P.,
RA Ramanan P., Cardenas W.B., Amarasinghe G.K., Volchkov V.E., Basler C.F.;
RT "Mutations abrogating VP35 interaction with double-stranded RNA render
RT Ebola virus avirulent in guinea pigs.";
RL J. Virol. 84:3004-3015(2010).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 215-338.
RX PubMed=20081868; DOI=10.1038/nsmb.1765;
RA Leung D.W., Prins K.C., Borek D.M., Farahbakhsh M., Tufariello J.M.,
RA Ramanan P., Nix J.C., Helgeson L.A., Otwinowski Z., Honzatko R.B.,
RA Basler C.F., Amarasinghe G.K.;
RT "Structural basis for dsRNA recognition and interferon antagonism by Ebola
RT VP35.";
RL Nat. Struct. Mol. Biol. 17:165-172(2010).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 218-340.
RX PubMed=24067086; DOI=10.1021/bi400704d;
RA Binning J.M., Wang T., Luthra P., Shabman R.S., Borek D.M., Liu G., Xu W.,
RA Leung D.W., Basler C.F., Amarasinghe G.K.;
RT "Development of RNA aptamers targeting Ebola virus VP35.";
RL Biochemistry 52:8406-8419(2013).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 215-340, INTERACTION WITH
RP NUCLEOPROTEIN N, AND FUNCTION.
RX PubMed=24495995; DOI=10.1016/j.jmb.2014.01.010;
RA Brown C.S., Lee M.S., Leung D.W., Wang T., Xu W., Luthra P., Anantpadma M.,
RA Shabman R.S., Melito L.M., MacMillan K.S., Borek D.M., Otwinowski Z.,
RA Ramanan P., Stubbs A.J., Peterson D.S., Binning J.M., Tonelli M.,
RA Olson M.A., Davey R.A., Ready J.M., Basler C.F., Amarasinghe G.K.;
RT "In silico derived small molecules bind the filovirus VP35 protein and
RT inhibit its polymerase cofactor activity.";
RL J. Mol. Biol. 426:2045-2058(2014).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (3.71 ANGSTROMS) OF 20-47, INTERACTION WITH NP,
RP INTRINSICALLY DISORDERED REGION, AND FUNCTION.
RX PubMed=25865894; DOI=10.1016/j.celrep.2015.03.034;
RA Leung D.W., Borek D., Luthra P., Binning J.M., Anantpadma M., Liu G.,
RA Harvey I.B., Su Z., Endlich-Frazier A., Pan J., Shabman R.S., Chiu W.,
RA Davey R.A., Otwinowski Z., Basler C.F., Amarasinghe G.K.;
RT "An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral
RT RNA Synthesis by Modulating Nucleoprotein-RNA Interactions.";
RL Cell Rep. 11:376-389(2015).
CC -!- FUNCTION: Plays an essential role in viral RNA synthesis and also a
CC role in suppressing innate immune signaling (PubMed:11027311). Acts as
CC a polymerase cofactor in the RNA polymerase transcription and
CC replication complexes (PubMed:9971816, PubMed:16495261,
CC PubMed:24495995). Serves as nucleoprotein/NP monomer chaperone prior to
CC the formation of the large oligomeric RNA-bound complexes (By
CC similarity). Regulates RNA synthesis by modulating NP-RNA interactions
CC and interacting with DYNLL1 (PubMed:25741013). VP35-NP interaction
CC controls the switch between RNA-bound NP and free NP and thus the
CC switch between genome replication and genome packaging into the
CC nucleocapsid (PubMed:25865894). Prevents establishment of cellular
CC antiviral state, thereby suppressing host DC maturation
CC (PubMed:26962215). Acts by inhibiting host DDX58/RIG-I activation both
CC by shielding dsRNA from detection and by preventing PRKRA binding to
CC DDX58 (PubMed:23870315). Blocks virus-induced phosphorylation and
CC activation of interferon regulatory factor 3/IRF3, a transcription
CC factor critical for the induction of interferons alpha and beta
CC (PubMed:12829834). This blockage is produced through the interaction
CC with and inhibition of host IKBKE and TBK1, producing a strong
CC inhibition of the phosphorylation and activation of IRF3
CC (PubMed:12829834). Also inhibits the antiviral effect mediated by the
CC host interferon-induced, double-stranded RNA-activated protein kinase
CC EIF2AK2/PKR (PubMed:17065211). Increases PIAS1-mediated SUMOylation of
CC IRF7, thereby repressing interferon transcription (PubMed:19557165).
CC Also acts as a suppressor of RNA silencing by interacting with host
CC DICER1, TARBP2/TRBP and PRKRA/PACT (By similarity). As a dimer, binds
CC and sequesters dsRNA contributing to the inhibition of interferon
CC production (By similarity). {ECO:0000250|UniProtKB:Q5XX07,
CC ECO:0000250|UniProtKB:Q6V1Q9, ECO:0000250|UniProtKB:Q8JPY0,
CC ECO:0000269|PubMed:11027311, ECO:0000269|PubMed:12829834,
CC ECO:0000269|PubMed:16495261, ECO:0000269|PubMed:17065211,
CC ECO:0000269|PubMed:19557165, ECO:0000269|PubMed:23870315,
CC ECO:0000269|PubMed:24495995, ECO:0000269|PubMed:25741013,
CC ECO:0000269|PubMed:25865894, ECO:0000269|PubMed:26962215,
CC ECO:0000269|PubMed:9971816}.
CC -!- SUBUNIT: Homodimer (By similarity). Homooligomer; via the coiled coil
CC domain (PubMed:16095644). Interacts with nucleoprotein NP and
CC polymerase L; VP35 bridges L and NP and allows the formation of the
CC polymerase complex (PubMed:25865894) (Probable). Also interacts with
CC VP30; this interaction is regulated by VP30 phosphorylation
CC (PubMed:23493393). Interacts with host IKBKE and TBK1; the interactions
CC lead to inhibition of cellular antiviral response by blocking necessary
CC interactions of IKBKE and TBK1 with their substrate IRF3. Interacts
CC with host DYNLL1; this interaction stabilizes VP35 N-terminal
CC oligomerization domain, enhances viral RNA synthesis but does not
CC participate in suppressing the host innate immune response
CC (PubMed:19403681, PubMed:25741013). Interacts with host PRKRA; this
CC interaction inhibits the interaction between DDX58 and PRKRA. Interacts
CC with dsRNA (PubMed:19122151, PubMed:20071589, PubMed:23870315).
CC Interacts with host TRIM6; this interaction plays an important role in
CC promoting efficient viral replication (PubMed:28679761). Interacts with
CC host STAU1 (PubMed:30301857). Interacts with host IRF7, PIAS1 and
CC UBE2I/UBC9; these interactions mediate the sumoylation of IRF7 and
CC contribute to the inhibition of IFN-type I production
CC (PubMed:19557165). Interacts with host DICER1; this interaction
CC prevents TARBP2/TRBP binding to DICER1 and thus allows the virus to
CC counteract host RNA silencing (By similarity). Interacts with host
CC TARBP2/TRBP and PRKRA/PACT; these interactions prevent TARBP2 and PRKRA
CC binding to DICER1 and thus allows the virus to counteract host RNA
CC silencing (By similarity). {ECO:0000250|UniProtKB:Q6V1Q9,
CC ECO:0000250|UniProtKB:Q8JPY0, ECO:0000269|PubMed:16095644,
CC ECO:0000269|PubMed:19122151, ECO:0000269|PubMed:19403681,
CC ECO:0000269|PubMed:19557165, ECO:0000269|PubMed:20071589,
CC ECO:0000269|PubMed:23493393, ECO:0000269|PubMed:23870315,
CC ECO:0000269|PubMed:25741013, ECO:0000269|PubMed:25865894,
CC ECO:0000269|PubMed:28679761, ECO:0000269|PubMed:30301857,
CC ECO:0000305|PubMed:31562565}.
CC -!- INTERACTION:
CC Q05127; P18272: NP; NbExp=2; IntAct=EBI-6148294, EBI-9820219;
CC Q05127; Q14164: IKBKE; Xeno; NbExp=3; IntAct=EBI-6148294, EBI-307369;
CC Q05127; Q12906: ILF3; Xeno; NbExp=6; IntAct=EBI-6148294, EBI-78756;
CC Q05127; O75569: PRKRA; Xeno; NbExp=2; IntAct=EBI-6148294, EBI-713955;
CC Q05127; Q9UHD2: TBK1; Xeno; NbExp=2; IntAct=EBI-6148294, EBI-356402;
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm
CC {ECO:0000269|PubMed:23493393, ECO:0000269|PubMed:28679761}.
CC -!- DOMAIN: The interferon inhibitory domain (IID) binds dsRNA.
CC {ECO:0000269|PubMed:19122151}.
CC -!- PTM: Phosphorylated by host IKBKE (PubMed:19153231). Phosphorylation
CC contributes to efficient viral replication and transcription
CC (PubMed:31694758, PubMed:31562565). {ECO:0000269|PubMed:19153231,
CC ECO:0000269|PubMed:31562565, ECO:0000269|PubMed:31694758}.
CC -!- SIMILARITY: Belongs to the filoviridae polymerase cofactor VP35 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01071}.
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DR EMBL; X61274; CAA43578.1; -; Genomic_RNA.
DR EMBL; L11365; AAB81002.1; -; Genomic_RNA.
DR EMBL; AF086833; AAD14582.1; -; Genomic_RNA.
DR EMBL; AF272001; AAG40165.1; -; Genomic_RNA.
DR EMBL; AY142960; AAN37505.1; -; Genomic_RNA.
DR EMBL; AF499101; AAM76032.1; -; Genomic_RNA.
DR RefSeq; NP_066244.1; NC_002549.1.
DR PDB; 3FKE; X-ray; 1.40 A; A/B=215-340.
DR PDB; 3L25; X-ray; 2.00 A; A/B/D/E=215-340.
DR PDB; 3L26; X-ray; 2.40 A; A/B=215-340.
DR PDB; 3L27; X-ray; 1.95 A; A/B/C/D=215-340.
DR PDB; 3L28; X-ray; 2.40 A; A/B/C/D/E/F=215-338.
DR PDB; 3L29; X-ray; 1.70 A; A/B=215-340.
DR PDB; 4IBB; X-ray; 1.75 A; A/B=215-340.
DR PDB; 4IBC; X-ray; 1.74 A; A/B=215-340.
DR PDB; 4IBD; X-ray; 1.84 A; A/B=215-340.
DR PDB; 4IBE; X-ray; 1.95 A; A/B=215-340.
DR PDB; 4IBF; X-ray; 2.29 A; A/B=215-340.
DR PDB; 4IBG; X-ray; 1.41 A; A/B=215-340.
DR PDB; 4IBI; X-ray; 1.47 A; A/B=215-340.
DR PDB; 4IBJ; X-ray; 1.54 A; A/B=215-340.
DR PDB; 4IBK; X-ray; 1.85 A; A/B=215-340.
DR PDB; 4IJE; X-ray; 1.90 A; A/B/C/D=218-340.
DR PDB; 4IJF; X-ray; 2.51 A; A=218-340.
DR PDB; 4YPI; X-ray; 3.71 A; E/F/G/H=20-47.
DR PDB; 4ZTA; X-ray; 2.40 A; A=15-59.
DR PDB; 4ZTG; X-ray; 2.80 A; A=15-59.
DR PDB; 4ZTI; X-ray; 2.40 A; A/B=15-59.
DR PDB; 6GBO; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=82-145.
DR PDB; 6GBP; X-ray; 3.49 A; A/B/C/D/E/F/G/H/I/J/K/L=82-145.
DR PDBsum; 3FKE; -.
DR PDBsum; 3L25; -.
DR PDBsum; 3L26; -.
DR PDBsum; 3L27; -.
DR PDBsum; 3L28; -.
DR PDBsum; 3L29; -.
DR PDBsum; 4IBB; -.
DR PDBsum; 4IBC; -.
DR PDBsum; 4IBD; -.
DR PDBsum; 4IBE; -.
DR PDBsum; 4IBF; -.
DR PDBsum; 4IBG; -.
DR PDBsum; 4IBI; -.
DR PDBsum; 4IBJ; -.
DR PDBsum; 4IBK; -.
DR PDBsum; 4IJE; -.
DR PDBsum; 4IJF; -.
DR PDBsum; 4YPI; -.
DR PDBsum; 4ZTA; -.
DR PDBsum; 4ZTG; -.
DR PDBsum; 4ZTI; -.
DR PDBsum; 6GBO; -.
DR PDBsum; 6GBP; -.
DR SMR; Q05127; -.
DR DIP; DIP-48771N; -.
DR IntAct; Q05127; 62.
DR iPTMnet; Q05127; -.
DR ABCD; Q05127; 5 sequenced antibodies.
DR DNASU; 911827; -.
DR GeneID; 911827; -.
DR KEGG; vg:911827; -.
DR EvolutionaryTrace; Q05127; -.
DR Proteomes; UP000007209; Genome.
DR Proteomes; UP000109874; Genome.
DR Proteomes; UP000149419; Genome.
DR Proteomes; UP000150973; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IDA:CACAO.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:CACAO.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IDA:CACAO.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IMP:CACAO.
DR GO; GO:0039505; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II; IMP:CACAO.
DR GO; GO:0046775; P:suppression by virus of host cytokine production; IDA:CACAO.
DR GO; GO:0039613; P:suppression by virus of host protein phosphorylation; IDA:CACAO.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039501; P:suppression by virus of host type I interferon production; IMP:CACAO.
DR GO; GO:0039724; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity; IEA:UniProtKB-KW.
DR GO; GO:0039557; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity; IEA:UniProtKB-KW.
DR GO; GO:0039723; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity; IEA:UniProtKB-KW.
DR GO; GO:0044414; P:suppression of host defenses by symbiont; IMP:CACAO.
DR DisProt; DP00998; -.
DR Gene3D; 1.10.8.950; -; 1.
DR Gene3D; 2.10.10.70; -; 1.
DR InterPro; IPR002953; Filo_VP35.
DR InterPro; IPR031163; VP35_IID.
DR InterPro; IPR043061; VP35_IID_b-sht.
DR InterPro; IPR043060; VP35_IID_hlx.
DR Pfam; PF02097; Filo_VP35; 1.
DR PIRSF; PIRSF018326; VP35_FiloV; 1.
DR PRINTS; PR01240; FILOVP35.
DR PROSITE; PS51735; VP35_IID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Host cytoplasm; Host-virus interaction;
KW Inhibition of host IKBKE by virus;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host IRF7 by virus; Inhibition of host RLR pathway by virus;
KW Inhibition of host TBK1 by virus; Inhibition of host TLR pathway by virus;
KW Interferon antiviral system evasion; Isopeptide bond; Phosphoprotein;
KW Reference proteome; RNA-binding; Suppressor of RNA silencing;
KW Transcription; Ubl conjugation; Viral immunoevasion; Viral RNA replication;
KW Virion.
FT CHAIN 1..340
FT /note="Polymerase cofactor VP35"
FT /id="PRO_0000222161"
FT DOMAIN 215..340
FT /note="VP35 IID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01071"
FT REGION 1..49
FT /note="Chaperones the nucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q5XX07"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..48
FT /note="Disordered"
FT /evidence="ECO:0000269|PubMed:25865894"
FT REGION 33..48
FT /note="NP binding region"
FT /evidence="ECO:0000269|PubMed:25865894"
FT REGION 83..145
FT /note="Homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q8JPY0"
FT COILED 96..116
FT /evidence="ECO:0000255"
FT MOTIF 71..75
FT /note="Required for host DYNLL1 interaction"
FT /evidence="ECO:0000269|PubMed:19403681"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 187
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:31562565,
FT ECO:0000269|PubMed:31694758"
FT MOD_RES 205
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:31562565,
FT ECO:0000269|PubMed:31694758"
FT MOD_RES 206
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:31562565,
FT ECO:0000269|PubMed:31694758"
FT MOD_RES 207
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:31562565"
FT MOD_RES 208
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:31562565,
FT ECO:0000269|PubMed:31694758"
FT MOD_RES 210
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:31562565"
FT MOD_RES 310
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:31562565"
FT MOD_RES 317
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:31562565,
FT ECO:0000269|PubMed:31694758"
FT CROSSLNK 309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28679761"
FT VARIANT 12
FT /note="A -> V (in strain: Isolate mouse-adapted)"
FT MUTAGEN 90..93
FT /note="LASL->AASA: Complete loss of homotrimerization; when
FT associated with A-107."
FT /evidence="ECO:0000269|PubMed:16095644"
FT MUTAGEN 107
FT /note="L->A: Complete loss of homotrimerization; when
FT associated with 90-AASA-93."
FT /evidence="ECO:0000269|PubMed:16095644"
FT MUTAGEN 187
FT /note="S->A: Impaired viral replication."
FT /evidence="ECO:0000269|PubMed:31694758"
FT MUTAGEN 187
FT /note="S->D: No effect on viral replication."
FT /evidence="ECO:0000269|PubMed:31694758"
FT MUTAGEN 210
FT /note="T->A: Loss of viral transcription and reduced
FT binding to the nucleoprotein."
FT /evidence="ECO:0000269|PubMed:31562565"
FT MUTAGEN 210
FT /note="T->D: No effect on viral transcription and binding
FT to the nucleoprotein."
FT /evidence="ECO:0000269|PubMed:31562565"
FT MUTAGEN 239
FT /note="F->A: Complete loss of interaction with host PRKRA
FT and subsequent immune response inhibition."
FT /evidence="ECO:0000269|PubMed:23870315"
FT MUTAGEN 305
FT /note="R->A: No effect on IRF3 promoter inhibition."
FT /evidence="ECO:0000269|PubMed:15464838"
FT MUTAGEN 309
FT /note="K->A: Partial loss of IRF3 promoter inhibition.
FT Complete loss of dsRNA-binding."
FT /evidence="ECO:0000269|PubMed:15464838,
FT ECO:0000269|PubMed:16698997"
FT MUTAGEN 312
FT /note="R->A: Complete loss of IRF3 promoter inhibition;
FT dsRNA-binding and interaction with host PRKRA."
FT /evidence="ECO:0000269|PubMed:15464838,
FT ECO:0000269|PubMed:16698997, ECO:0000269|PubMed:23870315"
FT MUTAGEN 317
FT /note="S->A: Impaired viral replication."
FT /evidence="ECO:0000269|PubMed:31694758"
FT MUTAGEN 317
FT /note="S->D: No effect on viral replication."
FT /evidence="ECO:0000269|PubMed:31694758"
FT MUTAGEN 319
FT /note="K->A: Complete loss of dsRNA binding activity; when
FT associated with A-322."
FT /evidence="ECO:0000269|PubMed:20071589"
FT MUTAGEN 322
FT /note="R->A: Complete loss of dsRNA binding activity; when
FT associated with A-319."
FT /evidence="ECO:0000269|PubMed:20071589"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:4ZTA"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4ZTA"
FT HELIX 83..118
FT /evidence="ECO:0007829|PDB:6GBO"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:6GBO"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:6GBO"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:3FKE"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3FKE"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:3FKE"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:3FKE"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:3FKE"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3FKE"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:3FKE"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:3FKE"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:3FKE"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:3FKE"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:3FKE"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4IJF"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:3FKE"
SQ SEQUENCE 340 AA; 37362 MW; B171C7FDBB5B1FBD CRC64;
MTTRTKGRGH TAATTQNDRM PGPELSGWIS EQLMTGRIPV SDIFCDIENN PGLCYASQMQ
QTKPNPKTRN SQTQTDPICN HSFEEVVQTL ASLATVVQQQ TIASESLEQR ITSLENGLKP
VYDMAKTISS LNRVCAEMVA KYDLLVMTTG RATATAAATE AYWAEHGQPP PGPSLYEESA
IRGKIESRDE TVPQSVREAF NNLNSTTSLT EENFGKPDIS AKDLRNIMYD HLPGFGTAFH
QLVQVICKLG KDSNSLDIIH AEFQASLAEG DSPQCALIQI TKRVPIFQDA APPVIHIRSR
GDIPRACQKS LRPVPPSPKI DRGWVCVFQL QDGKTLGLKI
