VP22_VZVO
ID VP22_VZVO Reviewed; 302 AA.
AC Q4JQW6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 23-FEB-2022, entry version 41.
DE RecName: Full=Tegument protein VP22;
DE AltName: Full=Tegument protein 9 {ECO:0000303|PubMed:34015248};
GN ORFNames=ORF9 {ECO:0000303|PubMed:34015248};
OS Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=341980;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT its parental virus.";
RL J. Virol. 76:11447-11459(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC Oka varicella vaccine Varivax (V-Oka-Merk);
RX PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA Vassilev V.;
RT "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL J. Virol. 82:11023-11044(2008).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GE.
RC STRAIN=Isolate Human/Japan/P-Oka/1970;
RX PubMed=18400847; DOI=10.1128/jvi.00303-08;
RA Che X., Reichelt M., Sommer M.H., Rajamani J., Zerboni L., Arvin A.M.;
RT "Functions of the ORF9-to-ORF12 gene cluster in varicella-zoster virus
RT replication and in the pathogenesis of skin infection.";
RL J. Virol. 82:5825-5834(2008).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST CGAS.
RX PubMed=34015248; DOI=10.1016/j.molcel.2021.05.002;
RA Xu G., Liu C., Zhou S., Li Q., Feng Y., Sun P., Feng H., Gao Y., Zhu J.,
RA Luo X., Zhan Q., Liu S., Zhu S., Deng H., Li D., Gao P.;
RT "Viral tegument proteins restrict cGAS-DNA phase separation to mediate
RT immune evasion.";
RL Mol. Cell 81:2823-2837(2021).
CC -!- FUNCTION: Tegument protein that plays different roles during the time
CC course of infection (By similarity). Participates in both the
CC accumulation of viral mRNAs and viral protein translation at late time
CC of infection (By similarity). Modulates the RNase activity of the
CC virion host shutoff protein ORF17 probably to ensure necessary levels
CC of key cellular mRNAs and proteins (By similarity). Plays a role in
CC microtubule reorganization that occurs after viral infection by
CC stabilizing microtubule network (By similarity). Plays a role in the
CC inhibition of host innate immune system by targeting the CGAS enzymatic
CC activity which is the principal cytosolic DNA sensor that detects
CC invading viral DNA (PubMed:34015248). Acts by mediating disruption of
CC liquid-like droplets in which CGAS is activated, thereby preventing
CC CGAS activity (PubMed:34015248). {ECO:0000250|UniProtKB:P10233,
CC ECO:0000269|PubMed:34015248}.
CC -!- SUBUNIT: Interacts with gE (via C-terminus); this interaction is
CC necessary for the recruitment of VP22/ORF9 to the Golgi and its
CC packaging into virions (PubMed:18400847). Interacts with gM (via C-
CC terminus) (By similarity). Interacts with VP16/ORF10; this interaction
CC allows the formation of a tripartite complex composed of VP16/ORF10,
CC VP22/ORF9 and VHS/ORF17 (By similarity). Interacts with the capsid-
CC binding protein ORF44 (By similarity). Interacts with host CGAS
CC (PubMed:34015248). {ECO:0000250|UniProtKB:P10233,
CC ECO:0000269|PubMed:18400847, ECO:0000269|PubMed:34015248}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:18400847}.
CC Host cytoplasm {ECO:0000250|UniProtKB:P10233}. Host nucleus
CC {ECO:0000250|UniProtKB:P10233}. Host Golgi apparatus
CC {ECO:0000250|UniProtKB:P10233}. Note=One of the most abundant tegument
CC protein (about 2000 copies per virion). Localizes in the cytoplasm at 8
CC hours postinfection and in the nucleus at 16 hours postinfection.
CC During virion morphogenesis, this protein probably accumulates at the
CC trans-Golgi where secondary envelopment occurs.
CC {ECO:0000250|UniProtKB:P10233}.
CC -!- PTM: Highly phosphorylated in the host cell. Packaging is selective for
CC underphosphorylated forms. {ECO:0000250|UniProtKB:P10233}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae VP22 tegument protein
CC family. {ECO:0000305}.
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DR EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57627.1; -; Genomic_DNA.
DR EMBL; DQ008355; AAY57698.1; -; Genomic_DNA.
DR SMR; Q4JQW6; -.
DR IntAct; Q4JQW6; 16.
DR MINT; Q4JQW6; -.
DR PRIDE; Q4JQW6; -.
DR Proteomes; UP000002603; Genome.
DR Proteomes; UP000008504; Genome.
DR Proteomes; UP000008505; Genome.
DR Proteomes; UP000008506; Genome.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IDA:UniProtKB.
DR InterPro; IPR006908; Herpes_UL49.
DR Pfam; PF04823; Herpes_UL49_2; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host Golgi apparatus; Host nucleus; Host-virus interaction;
KW Inhibition of host innate immune response by virus; Phosphoprotein;
KW Viral immunoevasion; Virion; Virion tegument.
FT CHAIN 1..302
FT /note="Tegument protein VP22"
FT /id="PRO_0000385496"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..244
FT /note="Interaction with gE"
FT /evidence="ECO:0000250|UniProtKB:P10233"
FT REGION 243..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 212..224
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P30022"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 32816 MW; 6557E734CAE76BF2 CRC64;
MASSDGDRLC RSNAVRRKTT PSYSGQYRTA RRSVVVGPPD DSDDSLGYIT TVGADSPSPV
YADLYFEHKN TTPRVHQPND SSGSEDDFED IDEVVAAFRE ARLRHELVED AVYENPLSVE
KPSRSFTKNA AVKPKLEDSP KRAPPGAGAI ASGRPISFST APKTATSSWC GPTPSYNKRV
FCEAVRRVAA MQAQKAAEAA WNSNPPRNNA ELDRLLTGAV IRITVHEGLN LIQAANEADL
GEGASVSKRG HNRKTGDLQG GMGNEPMYAQ VRKPKSRTDT QTTGRITNRS RARSASRTDA
RK
