RNB_HHV11
ID RNB_HHV11 Reviewed; 161 AA.
AC P04487;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 23-FEB-2022, entry version 104.
DE RecName: Full=Accessory factor US11;
DE AltName: Full=Vmw21;
GN Name=US11;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6324121; DOI=10.1093/nar/12.5.2473;
RA Rixon F.J., McGeoch D.J.;
RT "A 3' co-terminal family of mRNAs from the herpes simplex virus type 1
RT short region: two overlapping reading frames encode unrelated polypeptide
RT one of which has highly reiterated amino acid sequence.";
RL Nucleic Acids Res. 12:2473-2487(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2984429; DOI=10.1016/0022-2836(85)90320-1;
RA McGeoch D.J., Dolan A., Donald S., Rixon F.J.;
RT "Sequence determination and genetic content of the short unique region in
RT the genome of herpes simplex virus type 1.";
RL J. Mol. Biol. 181:1-13(1985).
RN [3]
RP CHARACTERIZATION.
RX PubMed=3037015; DOI=10.1099/0022-1317-68-7-1921;
RA McLean C.A., Rixon F.J., Marsden H.S.;
RT "The products of gene US11 of herpes simplex virus type 1 are DNA-binding
RT and localize to the nucleoli of infected cells.";
RL J. Gen. Virol. 68:1921-1937(1987).
RN [4]
RP ERRATUM OF PUBMED:3037015.
RA McLean C.A., Rixon F.J., Marsden H.S.;
RL J. Gen. Virol. 69:763-763(1988).
RN [5]
RP PHOSPHORYLATION.
RX PubMed=7498183; DOI=10.1002/elps.11501601216;
RA Simonin D., Diaz J.-J., Kindbeiter K., Pernas P., Madjar J.-J.;
RT "Phosphorylation of herpes simplex virus type 1 Us11 protein is independent
RT of viral genome expression.";
RL Electrophoresis 16:1317-1322(1995).
RN [6]
RP CHARACTERIZATION.
RX PubMed=8627758; DOI=10.1128/jvi.70.5.2842-2851.1996;
RA Roller R.J., Monk L.L., Stuart D., Roizman B.;
RT "Structure and function in the herpes simplex virus 1 RNA-binding protein
RT U(s)11: mapping of the domain required for ribosomal and nucleolar
RT association and RNA binding in vitro.";
RL J. Virol. 70:2842-2851(1996).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9680120; DOI=10.1099/0022-1317-79-7-1593;
RA Schaerer-Uthurralt N., Erard M., Kindbeiter K., Madjar J.-J., Diaz J.-J.;
RT "Distinct domains in herpes simplex virus type 1 US11 protein mediate post-
RT transcriptional transactivation of human T-lymphotropic virus type I
RT envelope glycoprotein gene expression and specific binding to the Rex
RT responsive element.";
RL J. Gen. Virol. 79:1593-1602(1998).
RN [8]
RP INTERACTION WITH HOST EIF2AK2.
RX PubMed=11836380; DOI=10.1128/jvi.76.5.2029-2035.2002;
RA Cassady K.A., Gross M.;
RT "The herpes simplex virus type 1 U(S)11 protein interacts with protein
RT kinase R in infected cells and requires a 30-amino-acid sequence adjacent
RT to a kinase substrate domain.";
RL J. Virol. 76:2029-2035(2002).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=20633584; DOI=10.1016/j.virusres.2010.07.009;
RA Xing J., Wu F., Pan W., Zheng C.;
RT "Molecular anatomy of subcellular localization of HSV-1 tegument protein
RT US11 in living cells.";
RL Virus Res. 153:71-81(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH HOST DDX58 AND IFIH1.
RX PubMed=22301138; DOI=10.1128/jvi.06713-11;
RA Xing J., Wang S., Lin R., Mossman K.L., Zheng C.;
RT "Herpes simplex virus 1 tegument protein US11 downmodulates the RLR
RT signaling pathway via direct interaction with RIG-I and MDA-5.";
RL J. Virol. 86:3528-3540(2012).
RN [11]
RP FUNCTION, AND INTERACTION WITH HOST NCL.
RX PubMed=22130536; DOI=10.1128/jvi.06194-11;
RA Greco A., Arata L., Soler E., Gaume X., Coute Y., Hacot S., Calle A.,
RA Monier K., Epstein A.L., Sanchez J.C., Bouvet P., Diaz J.J.;
RT "Nucleolin interacts with US11 protein of herpes simplex virus 1 and is
RT involved in its trafficking.";
RL J. Virol. 86:1449-1457(2012).
RN [12]
RP FUNCTION, AND INTERACTION WITH HOST EIF2AK2.
RX PubMed=23115300; DOI=10.1128/jvi.01158-12;
RA Lussignol M., Queval C., Bernet-Camard M.F., Cotte-Laffitte J., Beau I.,
RA Codogno P., Esclatine A.;
RT "The herpes simplex virus 1 Us11 protein inhibits autophagy through its
RT interaction with the protein kinase PKR.";
RL J. Virol. 87:859-871(2013).
RN [13]
RP FUNCTION.
RX PubMed=23773021; DOI=10.1111/1348-0421.12048;
RA Ishioka K., Ikuta K., Sato Y., Kaneko H., Sorimachi K., Fukushima E.,
RA Saijo M., Suzutani T.;
RT "Herpes simplex virus type 1 virion-derived US11 inhibits type 1
RT interferon-induced protein kinase R phosphorylation.";
RL Microbiol. Immunol. 57:426-436(2013).
RN [14]
RP FUNCTION, AND INTERACTION WITH HOST HSP90AA1.
RX PubMed=29743370; DOI=10.1128/jvi.00402-18;
RA Liu X., Main D., Ma Y., He B.;
RT "Herpes Simplex Virus 1 Inhibits TANK-Binding Kinase 1 through Formation of
RT the Us11-Hsp90 Complex.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: Plays a role in the inhibition of host immune response.
CC Participates in the inhibition of host autophagy by interacting with
CC and inhibiting host PKR/EIF2AK2. This interaction also prevents the
CC interferon-induced shut down of protein synthesis following viral
CC infection. Downmodulates the host RLR signaling pathway via direct
CC interaction with host DDX58 and IFIH1. Associates with endogenous HSP90
CC to disrupt the HSP90-TBK1 complex and induces destabilization of host
CC TBK1 through a proteasome-dependent pathway. May also participate in
CC nuclear egress of viral particles through interactions with host NCL
CC and regulation of the viral UL34 mRNA. {ECO:0000269|PubMed:22130536,
CC ECO:0000269|PubMed:22301138, ECO:0000269|PubMed:23115300,
CC ECO:0000269|PubMed:23773021, ECO:0000269|PubMed:29743370}.
CC -!- SUBUNIT: Associates with RNA derived from the 60S ribosomal subunits.
CC Seems to form large heterogeneous polymers of up to 200 identical
CC subunits in the cytoplasm. Interacts with host EIF2AK2. Interacts with
CC host NCL. Interacts with host DDX58; this interaction prevents DDX58
CC binding to host MAVS. Interacts with host IFIH1; this interaction
CC prevents host IFH1 binding to MAVS. Interacts with host HSP90; this
CC interaction inhibits TBK1-induced interferon induction.
CC {ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:22130536,
CC ECO:0000269|PubMed:22301138, ECO:0000269|PubMed:23115300,
CC ECO:0000269|PubMed:29743370}.
CC -!- INTERACTION:
CC P04487; O95786: DDX58; Xeno; NbExp=4; IntAct=EBI-6150681, EBI-995350;
CC P04487; P19525: EIF2AK2; Xeno; NbExp=3; IntAct=EBI-6150681, EBI-640775;
CC P04487; Q9BYX4: IFIH1; Xeno; NbExp=4; IntAct=EBI-6150681, EBI-6115771;
CC -!- SUBCELLULAR LOCATION: Host nucleus, host nucleolus
CC {ECO:0000269|PubMed:20633584}. Host cytoplasm
CC {ECO:0000269|PubMed:20633584}. Note=Following infection, it is released
CC into the cell cytoplasm.
CC -!- DOMAIN: The N-terminal tetrapeptide may be responsible for virion
CC incorporation.
CC -!- DOMAIN: The C-terminal half, rich in Arg and Pro residues, seems to be
CC responsible for the RNA-binding activity, and for the association with
CC ribosomes and the localization to the nucleolus. This region may adopt
CC a poly-L-proline II helix secondary structure.
CC -!- PTM: May be phosphorylated on Ser residues by host kinases.
CC {ECO:0000269|PubMed:7498183}.
CC -!- SIMILARITY: Belongs to the simplex virus US11 protein family.
CC {ECO:0000305}.
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DR EMBL; L00036; AAA96677.1; -; Genomic_DNA.
DR EMBL; X14112; CAA32276.1; -; Genomic_DNA.
DR EMBL; X02138; CAA26065.1; -; Genomic_DNA.
DR EMBL; X00428; CAA25125.1; -; Genomic_RNA.
DR PIR; A03728; DNBE17.
DR RefSeq; YP_009137147.1; NC_001806.2.
DR BioGRID; 971460; 3.
DR IntAct; P04487; 145.
DR MINT; P04487; -.
DR PRIDE; P04487; -.
DR DNASU; 2703439; -.
DR GeneID; 2703439; -.
DR KEGG; vg:2703439; -.
DR Proteomes; UP000009294; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0044196; C:host cell nucleolus; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host process; NAS:UniProtKB.
DR GO; GO:0039521; P:suppression by virus of host autophagy; IDA:UniProtKB.
DR GO; GO:0046792; P:suppression by virus of host cell cycle arrest; NAS:UniProtKB.
DR GO; GO:0039580; P:suppression by virus of host PKR signaling; IDA:UniProtKB.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity; IEA:UniProtKB-KW.
DR GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I 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.
PE 1: Evidence at protein level;
KW DNA-binding; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Inhibition of host autophagy by virus;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host MDA5 by virus; Inhibition of host PKR by virus;
KW Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW Inhibition of host TBK1 by virus; Inhibition of host TLR pathway by virus;
KW Late protein; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Viral immunoevasion.
FT CHAIN 1..161
FT /note="Accessory factor US11"
FT /id="PRO_0000115740"
FT REPEAT 85..90
FT /note="1"
FT REPEAT 91..96
FT /note="2"
FT REPEAT 97..102
FT /note="3"
FT REPEAT 103..108
FT /note="4"
FT REPEAT 109..114
FT /note="5"
FT REPEAT 115..120
FT /note="6"
FT REPEAT 121..126
FT /note="7"
FT REPEAT 127..132
FT /note="8"
FT REPEAT 133..138
FT /note="9"
FT REPEAT 139..144
FT /note="10"
FT REPEAT 145..150
FT /note="11"
FT REPEAT 151..156
FT /note="12"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..156
FT /note="12 X 6 AA approximate tandem repeats"
FT COMPBIAS 91..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 161 AA; 17757 MW; 1CECA86CF1B9F2FF CRC64;
MSQTQPPAPV GPGDPDVYLK GVPSAGMHPR GVHAPRGHPR MISGPPQRGD NDQAAGQCGD
SGLLRVGADT TISKPSEAVR PPTIPRTPRV PREPRVPRPP REPREPRVPR APRDPRVPRD
PRDPRQPRSP REPRSPREPR SPREPRTPRT PREPRTARGS V
