VP22_EHV4
ID VP22_EHV4 Reviewed; 290 AA.
AC Q00039;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Tegument protein VP22;
DE AltName: Full=Gene 11 protein;
GN Name=11; Synonyms=B4;
OS Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10333;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1850013; DOI=10.1128/jvi.65.5.2320-2326.1991;
RA Whittaker G.R., Riggio M.P., Halliburton I.W., Killington R.A., Allen G.P.,
RA Meredith D.M.;
RT "Antigenic and protein sequence homology between VP13/14, a herpes simplex
RT virus type 1 tegument protein, and gp10, a glycoprotein of equine
RT herpesvirus 1 and 4.";
RL J. Virol. 65:2320-2326(1991).
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; X17684; CAA35674.1; -; Genomic_DNA.
DR PIR; S36706; S36706.
DR SMR; Q00039; -.
DR PRIDE; Q00039; -.
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; Virion;
KW Virion tegument.
FT CHAIN 1..290
FT /note="Tegument protein VP22"
FT /id="PRO_0000116096"
FT REGION 98..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..149
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P30022"
FT MOTIF 219..231
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P30022"
FT COMPBIAS 100..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 31462 MW; BD57CE14436295FC CRC64;
MLTPQRSSYT LQFVTKIGKD DLLAEALLCE KTNFTINSVY LGKMICMTVH AVTMTKFTPD
KAERAAHYNP QEHIYETCPG DEFYDACEYS LVGGGKLSTS HGRLSPTKTT PHPKSAGVTP
PQRVPARPAT RAAAPSATPT QPDCVAKQRT SPGVNSIKSG KSLAFSCTPK TPKTPWYGAT
HLFNKNVFCA AVSRVAAAHA SDAASALWDL DPPKTNEDLD RFLKAAAIRI LVCEGSKLLE
MANATMERSP DGAAAVAPIG YDRRPRLASR RRSIKCKPPA DDFFDDTDSR