VP30_EBORR
ID VP30_EBORR Reviewed; 287 AA.
AC Q8JPX6; Q5UAK6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-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 Reston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=386032;
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).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12191779; DOI=10.1016/s0168-1702(02)00087-4;
RA Groseth A., Stroeher U., Theriault S., Feldmann H.;
RT "Molecular characterization of an isolate from the 1989/90 epizootic of
RT Ebola virus Reston among macaques imported into the United States.";
RL Virus Res. 87:155-163(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Pennsylvania-89;
RX PubMed=15661171; DOI=10.1016/j.virol.2004.11.018;
RA Boehmann Y., Enterlein S., Randolf A., Muehlberger E.I.;
RT "A reconstituted replication and transcription system for Ebola virus
RT Reston and comparison with Ebola virus Zaire.";
RL Virology 332:406-417(2005).
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. Also acts as a suppressor of RNA silencing by interacting
CC with host DICER1 and TARBP2/TRBP (By similarity).
CC {ECO:0000250|UniProtKB:Q05323, ECO:0000250|UniProtKB:Q77DJ5}.
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 RBBP6 isoform 1 (By similarity). Interacts with
CC host DICER1; this interaction prevents TARBP2/TRBP binding to DICER1
CC and thus allows the virus to counteract host RNA silencing (By
CC similarity). Interacts with host TARBP2/TRBP; this interaction, which
CC occurs only in the presence of siRNA, prevents TARBP2 binding to DICER1
CC and thus allows the virus to counteract host RNA silencing (By
CC similarity). {ECO:0000250|UniProtKB:Q05323,
CC ECO:0000250|UniProtKB:Q77DJ5}.
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}.
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; AF522874; AAN04452.1; -; Genomic_RNA.
DR EMBL; AY769362; AAV48579.1; -; Genomic_RNA.
DR RefSeq; NP_690585.1; NC_004161.1.
DR PDB; 3V7O; X-ray; 2.25 A; A/B=142-272.
DR PDBsum; 3V7O; -.
DR SMR; Q8JPX6; -.
DR GeneID; 955196; -.
DR KEGG; vg:955196; -.
DR Proteomes; UP000007207; Genome.
DR Proteomes; UP000138664; 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: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; RNA-binding; Suppressor of RNA silencing;
KW Transcription; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT CHAIN 1..287
FT /note="Transcriptional activator VP30"
FT /id="PRO_0000245072"
FT ZN_FING 72..90
FT /note="C3H1-type; atypical"
FT REGION 1..52
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 /evidence="ECO:0000250"
FT REGION 180..197
FT /note="Interaction with the nucleoprotein"
FT /evidence="ECO:0000250"
FT REGION 268..287
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 VARIANT 67
FT /note="A -> T (in strain: Isolate Pennsylvania-89)"
FT VARIANT 136
FT /note="Q -> H (in strain: Isolate Pennsylvania-89)"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3V7O"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:3V7O"
SQ SEQUENCE 287 AA; 32401 MW; FC76BDA604A769CE CRC64;
MEHSRERGRS SNMRHNSREP YENPSRSRSL SRDPNQVDRR QPRSASQIRV PNLFHRKKTD
ALIVPPAPKD ICPTLKKGFL CDSKFCKKDH QLDSLNDHEL LLLIARRTCG IIESNSQITS
PKDMRLANPT AEDFSQGNSP KLTLAVLLQI AEHWATRDLR QIEDSKLRAL LTLCAVLTRK
FSKSQLGLLC ETHLRHEGLG QDQADSVLEV YQRLHSDKGG NFEAALWQQW DRQSLIMFIS
AFLNIALQIP CESSSVVVSG LATLYPAQDN STPSEATNDT TWSSTVE
