ID   VP22_VZVD               Reviewed;         302 AA.
AC   P09272;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   23-FEB-2022, entry version 68.
DE   RecName: Full=Tegument protein VP22;
DE   AltName: Full=ORF9 protein;
DE   AltName: Full=Tegument protein 9;
GN   ORFNames=ORF9;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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. Acts by mediating disruption of liquid-like
CC       droplets in which CGAS is activated, thereby preventing CGAS activity
CC       (By similarity). {ECO:0000250|UniProtKB:P10233}.
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 (By similarity). 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 (By
CC       similarity). {ECO:0000250|UniProtKB:P10233}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P10233}.
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; X04370; CAA27892.1; -; Genomic_DNA.
DR   PIR; I27212; WZBE9.
DR   SMR; P09272; -.
DR   PRIDE; P09272; -.
DR   Proteomes; UP000002602; 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   InterPro; IPR006908; Herpes_UL49.
DR   Pfam; PF04823; Herpes_UL49_2; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host Golgi apparatus; Host nucleus; Phosphoprotein;
KW   Reference proteome; Virion; Virion tegument.
FT   CHAIN           1..302
FT                   /note="Tegument protein VP22"
FT                   /id="PRO_0000116097"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..170
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;  32846 MW;  6557FB44CAE76BF2 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 RARSASRTDT
     RK