ID   VP22_EHV1B              Reviewed;         304 AA.
AC   P28960; Q6DLK0;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 73.
DE   RecName: Full=Tegument protein VP22;
DE   AltName: Full=Gene 11 protein;
GN   OrderedLocusNames=11;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
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; AY665713; AAT67268.1; -; Genomic_DNA.
DR   PIR; C36796; WZBEA9.
DR   RefSeq; YP_053056.1; NC_001491.2.
DR   SMR; P28960; -.
DR   GeneID; 1487566; -.
DR   KEGG; vg:1487566; -.
DR   Proteomes; UP000001189; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IDA:CACAO.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IDA:CACAO.
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..304
FT                   /note="Tegument protein VP22"
FT                   /id="PRO_0000116095"
FT   REGION          23..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           160..163
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P30022"
FT   MOTIF           233..245
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P30022"
FT   COMPBIAS        24..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..142
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  33241 MW;  937CE27366E79879 CRC64;
     MSDTWRRRRS GCNDANATEE LVYSTVRSDH RQRRPSRGTF VMRENDLYDK QSVSKENDLY
     ESASPNDDKV YTRRGMSTAA HYRDSEHIYE TCEGDEFYDA CEYSLIGGGK LSTSNGRQSP
     AKAQPPPRGA AAAPPPRVPT RPPTRAAATS TTPRQQDCAP KQRASPGVNS IKSGKGLAFS
     GTPKTPKSQW YGATHLFNKN VFCAAVSRVA AAHASDAASA LWDLNPPKTN EDLDRFLKAA
     AIRILVCEGA QLLEVANSTM ESTPDGYAAA GPNGYDRRPR TASRRRSLKC KPPADDFFDD
     TNSG