ID   VP22_GAHVM              Reviewed;         249 AA.
AC   Q9E6M7; A8DIW8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   23-FEB-2022, entry version 54.
DE   RecName: Full=Tegument protein VP22;
GN   Name=MDV062;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
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 UL41 probably to ensure necessary levels of
CC       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 to the Golgi and its packaging
CC       into virions (By similarity). Interacts with gM (via C-terminus) (By
CC       similarity). Interacts with VP16; this interaction allows the formation
CC       of a tripartite complex composed of VP16, VP22 and UL41/VHS (By
CC       similarity). Interacts with the capsid-binding protein UL16 (By
CC       similarity). Interacts with host CGAS (By similarity).
CC       {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; AF243438; AAG14242.1; -; Genomic_DNA.
DR   PIR; S60741; S60741.
DR   RefSeq; YP_001033978.1; NC_002229.3.
DR   SMR; Q9E6M7; -.
DR   PRIDE; Q9E6M7; -.
DR   GeneID; 4811523; -.
DR   KEGG; vg:4811523; -.
DR   Proteomes; UP000008072; 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..249
FT                   /note="Tegument protein VP22"
FT                   /id="PRO_0000406528"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  27626 MW;  58F00BCB7631F65D CRC64;
     MGDSERRKSE RRRSLGYPSA YDDVSIPARR PSTRTQRNLN QDDLSKHGPF TDHPTQKHKS
     AKAVSEDVSS TTRGGFTNKP RAKPGVRAVQ SNKFAFSTAP SSASSTWRSN TVAFNQRMFC
     GAVATVAQYH AYQGALALWR QDPPRTNEEL DAFLSRAVIK ITIQEGPNLM GEAETCARKL
     LEESGLSQGN ENVKSKSERT TKSERTRRGG EIEIKSPDPG SHRTHNPRTP ATSRRHHSSA
     RGYRSSDSE