VP8_BTV10
ID VP8_BTV10 Reviewed; 229 AA.
AC P08363;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 12-AUG-2020, entry version 62.
DE RecName: Full=Non-structural protein P8;
DE AltName: Full=Non-structural protein NS3;
DE Contains:
DE RecName: Full=Non-structural protein NS3A;
GN Name=Segment-10;
OS Bluetongue virus 10 (isolate USA) (BTV 10).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Orbivirus.
OX NCBI_TaxID=10900;
OH NCBI_TaxID=9891; Antilocapra americana (Pronghorn).
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=46212; Culicoides variipennis (Biting midge).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3025349; DOI=10.1099/0022-1317-67-12-2833;
RA Lee J.W., Roy P.;
RT "Nucleotide sequence of a cDNA clone of RNA segment 10 of bluetongue virus
RT (serotype 10).";
RL J. Gen. Virol. 67:2833-2837(1986).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=1654377; DOI=10.1099/0022-1317-72-9-2263;
RA Hyatt A.D., Gould A.R., Coupar B., Eaton B.T.;
RT "Localization of the non-structural protein NS3 in bluetongue virus-
RT infected cells.";
RL J. Gen. Virol. 72:2263-2267(1991).
RN [3]
RP FUNCTION.
RX PubMed=8384747; DOI=10.1006/viro.1993.1167;
RA Hyatt A.D., Zhao Y., Roy P.;
RT "Release of bluetongue virus-like particles from insect cells is mediated
RT by BTV nonstructural protein NS3/NS3A.";
RL Virology 193:592-603(1993).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=15292261; DOI=10.1074/jbc.m403663200;
RA Han Z., Harty R.N.;
RT "The NS3 protein of bluetongue virus exhibits viroporin-like properties.";
RL J. Biol. Chem. 279:43092-43097(2004).
RN [5]
RP FUNCTION.
RX PubMed=23658442; DOI=10.1128/jvi.00678-13;
RA Chauveau E., Doceul V., Lara E., Breard E., Sailleau C., Vidalain P.O.,
RA Meurs E.F., Dabo S., Schwartz-Cornil I., Zientara S., Vitour D.;
RT "NS3 of bluetongue virus interferes with the induction of type I
RT interferon.";
RL J. Virol. 87:8241-8246(2013).
RN [6]
RP SUBUNIT.
RX PubMed=26318174; DOI=10.1007/s11262-015-1230-9;
RA Chacko N., Mohanty N.N., Biswas S.K., Chand K., Yogisharadhya R.,
RA Pandey A.B., Mondal B., Shivachandra S.B.;
RT "A coiled-coil motif in non-structural protein 3 (NS3) of bluetongue virus
RT forms an oligomer.";
RL Virus Genes 51:244-251(2015).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST OPTN.
RX PubMed=27538435; DOI=10.1186/s12915-016-0292-z;
RA Pourcelot M., Zemirli N., Silva Da Costa L., Loyant R., Garcin D.,
RA Vitour D., Munitic I., Vazquez A., Arnoult D.;
RT "The Golgi apparatus acts as a platform for TBK1 activation after viral RNA
RT sensing.";
RL BMC Biol. 14:69-69(2016).
CC -!- FUNCTION: Plays a role in the inhibition of host innate immune
CC response. Interacts with host OPTN and thus inhibits the recruitment of
CC TBK1 to the host Golgi apparatus. In turn, downstream partner IRF3
CC cannot be activated and IFN-beta production is impaired.
CC {ECO:0000269|PubMed:23658442, ECO:0000269|PubMed:27538435}.
CC -!- FUNCTION: Facilitates viral particle release either by increasing
CC plasma membrane permeability through a viroporin-like activity
CC (PubMed:15292261) or by viral budding. {ECO:0000269|PubMed:15292261,
CC ECO:0000269|PubMed:8384747}.
CC -!- SUBUNIT: Forms homooligomers via coiled-coil motif (PubMed:15292261,
CC PubMed:26318174). Interacts with host OPTN; this interaction inhibits
CC innate immune response (PubMed:27538435). {ECO:0000269|PubMed:15292261,
CC ECO:0000269|PubMed:26318174, ECO:0000269|PubMed:27538435}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000269|PubMed:15292261,
CC ECO:0000269|PubMed:1654377}; Multi-pass membrane protein {ECO:0000255}.
CC Host Golgi apparatus {ECO:0000269|PubMed:15292261,
CC ECO:0000269|PubMed:27538435}.
CC -!- SIMILARITY: Belongs to the orbivirus NS3 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; M28981; AAA42840.1; -; Genomic_RNA.
DR PIR; A29153; P8XR10.
DR RefSeq; YP_052960.1; NC_006015.1.
DR ELM; P08363; -.
DR GeneID; 2943154; -.
DR KEGG; vg:2943154; -.
DR Proteomes; UP000007662; Genome.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR002565; Orbi_NS3.
DR Pfam; PF01616; Orbi_NS3; 1.
PE 1: Evidence at protein level;
KW Host cell membrane; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Inhibition of host innate immune response by virus;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral immunoevasion.
FT CHAIN 1..229
FT /note="Non-structural protein P8"
FT /id="PRO_0000040628"
FT CHAIN 14..229
FT /note="Non-structural protein NS3A"
FT /id="PRO_0000040629"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 14..26
FT /note="CCM-I"
FT /evidence="ECO:0000269|PubMed:26318174"
FT REGION 94..116
FT /note="CCM-III"
FT /evidence="ECO:0000269|PubMed:26318174"
FT REGION 185..198
FT /note="CCM-II"
FT /evidence="ECO:0000269|PubMed:26318174"
SQ SEQUENCE 229 AA; 25602 MW; 1A23B53198ECB684 CRC64;
MLSGLIQRFE EEKMKHNQDR VEELSLVRVD DTISQPPRYA PSAPMPSSMP TVALEILDKA
MSNTTGATQT QKAEKAAFAS YAEAFRDDVR LRQIKRHVNE QILPKLKSDL SELKKKRAII
HTTLLVAAVV ALLTSVCTLS SDMSVAFKIN GTKTEVPSWF KSLNPMLGVV NLGATFLMMV
CAKSERALNQ QIDMIKKEVM KKQSYNDAVR MSFTEFSSIP LDGFEMPLT
