ID   VP30_EBOZ5              Reviewed;         288 AA.
AC   Q77DJ5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Transcriptional activator VP30 {ECO:0000250|UniProtKB:Q05323};
DE   AltName: Full=EbolaVP30 {ECO:0000250|UniProtKB:Q05323};
DE            Short=eVP30 {ECO:0000250|UniProtKB:Q05323};
DE   AltName: Full=Minor nucleoprotein VP30;
GN   Name=VP30;
OS   Zaire ebolavirus (strain Kikwit-95) (ZEBOV) (Zaire Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus;
OC   Orthoebolavirus zairense; Zaire ebolavirus.
OX   NCBI_TaxID=128951;
OH   NCBI_TaxID=77231; Epomops franqueti (Franquet's epauletted fruit bat) (Epomophorus franqueti).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Chain P.S.G., Ichou M.A., Malfatti S.A., Hajjaj A., Vergez L.M.,
RA   Paragas J., Do L.H., Jahrling P.B., Smith K.L., McCready P.M.,
RA   Ibrahim M.S.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, INTERACTION WITH HOST DICER1, AND INTERACTION WITH HOST TARBP2.
RX   PubMed=21228243; DOI=10.1128/jvi.01160-10;
RA   Fabozzi G., Nabel C.S., Dolan M.A., Sullivan N.J.;
RT   "Ebolavirus proteins suppress the effects of small interfering RNA by
RT   direct interaction with the mammalian RNA interference pathway.";
RL   J. Virol. 85:2512-2523(2011).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 142-272.
RX   PubMed=17202263; DOI=10.1073/pnas.0606730104;
RA   Hartlieb B., Muziol T., Weissenhorn W., Becker S.;
RT   "Crystal structure of the C-terminal domain of Ebola virus VP30 reveals a
RT   role in transcription and nucleocapsid association.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:624-629(2007).
RN   [4] {ECO:0007744|PDB:6E5X}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 140-266, INTERACTION WITH HOST
RP   RBBP6 ISOFORM 1, AND MUTAGENESIS OF GLU-197; ASP-202; GLN-229 AND TRP-230.
RX   PubMed=30550789; DOI=10.1016/j.cell.2018.08.044;
RA   Batra J., Hultquist J.F., Liu D., Shtanko O., Von Dollen J., Satkamp L.,
RA   Jang G.M., Luthra P., Schwarz T.M., Small G.I., Arnett E., Anantpadma M.,
RA   Reyes A., Leung D.W., Kaake R., Haas P., Schmidt C.B., Schlesinger L.S.,
RA   LaCount D.J., Davey R.A., Amarasinghe G.K., Basler C.F., Krogan N.J.;
RT   "Protein Interaction Mapping Identifies RBBP6 as a Negative Regulator of
RT   Ebola Virus Replication.";
RL   Cell 175:1917-1930.e13(2018).
CC   -!- FUNCTION: Multifunctional protein that acts as a viral transcriptional
CC       activator. Promotes read-through of an RNA hairpin in the NP open
CC       reading frame to enhance viral transcription. Mechanistically,
CC       nonphosphorylated VP30 hexamers form a ternary complex with the viral
CC       leader RNA. Clamps the RNA template and the complex VP35-polymerase L
CC       together, thereby increasing the polymerase affinity for the RNA
CC       template to increase transcription initiation despite the presence of
CC       RNA secondary structures. Assists also stop-start transcription at gene
CC       junctions to promote transcription of downstream genes. Interaction
CC       with NP plays a critical role in transcription initiation by
CC       recognizing the RNA stem loop (By similarity). Interaction with host
CC       RBBP6 interferes with NP-VP30 interaction and inhibits viral RNA
CC       synthesis (PubMed:30550789). Also acts as a suppressor of RNA silencing
CC       by interacting with host DICER1 and TARBP2/TRBP (PubMed:21228243).
CC       {ECO:0000250|UniProtKB:Q05323, ECO:0000269|PubMed:21228243,
CC       ECO:0000269|PubMed:30550789}.
CC   -!- SUBUNIT: Homohexamer; hexamerization is essential for RNA binding.
CC       Interacts with the nucleoprotein/NP; this interaction plays both
CC       essential and inhibitory roles in viral RNA synthesis. Interacts with
CC       VP35. Interacts with host STAU1 (By similarity). Interacts (via C-
CC       terminus) with host ubiquitin ligase RBBP6 isoform 1 (PubMed:30550789).
CC       Interacts with host DICER1; this interaction prevents TARBP2/TRBP
CC       binding to DICER1 and thus allows the virus to counteract host RNA
CC       silencing (PubMed:21228243). Interacts with host TARBP2/TRBP; this
CC       interaction, which occurs only in the presence of siRNA, prevents
CC       TARBP2 binding to DICER1 and thus allows the virus to counteract host
CC       RNA silencing (PubMed:21228243). {ECO:0000250|UniProtKB:Q05323,
CC       ECO:0000269|PubMed:21228243, ECO:0000269|PubMed:30550789}.
CC   -!- INTERACTION:
CC       Q77DJ5; Q77DJ5: VP30; NbExp=4; IntAct=EBI-15617769, EBI-15617769;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:Q05323}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:Q05323}. Note=Present in viral
CC       inclusion bodies due to its interaction with NP.
CC       {ECO:0000250|UniProtKB:Q05323}.
CC   -!- PTM: Phosphorylated by host. Phosphorylation negatively regulates the
CC       transcription activation. Phosphorylation and dephosphorylation take
CC       place in viral inclusion bodies and are largely influenced by the
CC       presence of NP. Dephosphorylated by host PPP2R5C; this
CC       dephosphorylation enhances viral transcription and is mediated by NP.
CC       {ECO:0000250|UniProtKB:Q05323}.
CC   -!- SIMILARITY: Belongs to the filoviridae transcriptional activator VP30
CC       family. {ECO:0000305}.
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DR   EMBL; AY354458; AAQ55051.1; -; Genomic_RNA.
DR   RefSeq; NP_066249.1; NC_002549.1.
DR   PDB; 2I8B; X-ray; 2.00 A; A/B=142-272.
DR   PDB; 5VAO; X-ray; 2.56 A; A/B/C/D=139-267.
DR   PDB; 5VAP; X-ray; 1.85 A; A/B=142-253.
DR   PDB; 6E5X; X-ray; 1.50 A; A=140-266.
DR   PDBsum; 2I8B; -.
DR   PDBsum; 5VAO; -.
DR   PDBsum; 5VAP; -.
DR   PDBsum; 6E5X; -.
DR   SMR; Q77DJ5; -.
DR   DIP; DIP-60797N; -.
DR   DNASU; 911826; -.
DR   GeneID; 911826; -.
DR   KEGG; vg:911826; -.
DR   EvolutionaryTrace; Q77DJ5; -.
DR   Proteomes; UP000007208; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.20.120.1160; -; 1.
DR   InterPro; IPR014459; VP30_FiloV.
DR   Pfam; PF11507; Transcript_VP30; 1.
DR   PIRSF; PIRSF011356; VP30_FiloV; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Host cytoplasm; Host-virus interaction;
KW   Inhibition of host innate immune response by virus; Metal-binding;
KW   Phosphoprotein; RNA-binding; Suppressor of RNA silencing; Transcription;
KW   Viral immunoevasion; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..288
FT                   /note="Transcriptional activator VP30"
FT                   /id="PRO_0000245074"
FT   ZN_FING         72..90
FT                   /note="C3H1-type; atypical"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          26..40
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q05323"
FT   REGION          94..112
FT                   /note="Oligomerization"
FT   REGION          180..197
FT                   /note="Interaction with the nucleoprotein"
FT   REGION          268..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         197
FT                   /note="E->A: Complete loss of binding to host RBBP6 and to
FT                   NP."
FT                   /evidence="ECO:0000269|PubMed:30550789"
FT   MUTAGEN         202
FT                   /note="D->A: No effect on binding to host RBBP6 and to NP."
FT                   /evidence="ECO:0000269|PubMed:30550789"
FT   MUTAGEN         229
FT                   /note="Q->A: No effect on binding to host RBBP6 and to NP."
FT                   /evidence="ECO:0000269|PubMed:30550789"
FT   MUTAGEN         230
FT                   /note="W->A: Complete loss of binding to host RBBP6 and to
FT                   NP."
FT                   /evidence="ECO:0000269|PubMed:30550789"
FT   HELIX           144..155
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   HELIX           164..178
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   HELIX           186..196
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   HELIX           204..215
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:2I8B"
FT   HELIX           221..229
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   HELIX           232..245
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:6E5X"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:2I8B"
FT   HELIX           255..262
FT                   /evidence="ECO:0007829|PDB:6E5X"
SQ   SEQUENCE   288 AA;  32521 MW;  1FE40E93AB80454B CRC64;
     MEASYERGRP RAARQHSRDG HDHHVRARSS SRENYRGEYR QSRSASQVRV PTVFHKKRVE
     PLTVPPAPKD ICPTLKKGFL CDSSFCKKDH QLESLTDREL LLLIARKTCG SVEQQLNITA
     PKDSRLANPT ADDFQQEEGP KITLLTLIKT AEHWARQDIR TIEDSKLRAL LTLCAVMTRK
     FSKSQLSLLC ETHLRREGLG QDQAEPVLEV YQRLHSDKGG SFEAALWQQW DRQSLIMFIT
     AFLNIALQLP CESSAVVVSG LRTLVPQSDN EEASTNPGTC SWSDEGTP
//