VP30_EBOZ5
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 03-AUG-2022, entry version 80.
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; Ebolavirus.
OX NCBI_TaxID=128951;
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].
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 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 Metal-binding; Phosphoprotein; Reference proteome; RNA-binding;
KW Suppressor of RNA silencing; Transcription; Viral nucleoprotein; Virion;
KW 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
