VP22_HHV2H
ID VP22_HHV2H Reviewed; 300 AA.
AC P89468;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 23-FEB-2022, entry version 60.
DE RecName: Full=Tegument protein VP22;
GN ORFNames=UL49;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3027242; DOI=10.1099/0022-1317-68-1-19;
RA McGeoch D.J., Moss H.W.M., McNab D., Frame M.C.;
RT "DNA sequence and genetic content of the HindIII l region in the short
RT unique component of the herpes simplex virus type 2 genome: identification
RT of the gene encoding glycoprotein G, and evolutionary comparisons.";
RL J. Gen. Virol. 68:19-38(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
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; Z86099; CAB06735.1; -; Genomic_DNA.
DR RefSeq; YP_009137201.1; NC_001798.2.
DR SMR; P89468; -.
DR PRIDE; P89468; -.
DR DNASU; 1487336; -.
DR GeneID; 1487336; -.
DR KEGG; vg:1487336; -.
DR Proteomes; UP000001874; 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..300
FT /note="Tegument protein VP22"
FT /id="PRO_0000385495"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..267
FT /note="Interaction with gE"
FT /evidence="ECO:0000250|UniProtKB:P10233"
FT REGION 269..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..166
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P30022"
FT MOTIF 232..244
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P30022"
FT COMPBIAS 33..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 31791 MW; FC72D09F7FB7B096 CRC64;
MTSRRSVKSC PREAPRGTHE ELYYGPVSPA DPESPRDDFR RGAGPMRARP RGEVRFLHYD
EAGYALYRDS SSDDDESRDT ARPRRSASVA GSHGPGPARA PPPPGGPVGA GGRSHAPPAR
TPKMTRGAPK ASATPATDPA RGRRPAQADS AVLLDAPAPT ASGRTKTPAQ GLAKKLHFST
APPSPTAPWT PRVAGFNKRV FCAAVGRLAA THARLAAVQL WDMSRPHTDE DLNELLDLTT
IRVTVCEGKN LLQRANELVN PDAAQDVDAT AAARGRPAGR AAATARAPAR SASRPRRPLE
