ID   VP16_HHV23              Reviewed;         490 AA.
AC   P68335; P23990; P29793;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 1.
DT   02-JUN-2021, entry version 64.
DE   RecName: Full=Tegument protein VP16;
DE   AltName: Full=Alpha trans-inducing protein;
DE   AltName: Full=Alpha-TIF;
DE   AltName: Full=ICP25;
DE   AltName: Full=Vmw65;
GN   ORFNames=UL48;
OS   Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10313;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1658370; DOI=10.1128/jvi.65.12.6705-6713.1991;
RA   Greaves R.F., O'Hare P.;
RT   "Sequence, function, and regulation of the Vmw65 gene of herpes simplex
RT   virus type 2.";
RL   J. Virol. 65:6705-6713(1991).
CC   -!- FUNCTION: Transcriptional activator of immediate-early (IE) gene
CC       products (alpha genes). Acts as a key activator of lytic infection by
CC       initiating the lytic program through the assembly of the
CC       transcriptional regulatory VP16-induced complex composed of VP16 and
CC       two cellular factors, HCFC1 and POU2F 1. VP16-induced complex
CC       represents a regulatory switch: when it is on, it promotes IE-gene
CC       expression and thus lytic infection, and when it is off, it limits IE-
CC       gene transcription favoring latent infection (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: May play a role in the aggregation of tegument proteins
CC       around nucleocapsids during virus morphogenesis. {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with VP22. Interacts with gH (via C-terminus).
CC       Interacts with the virion host shutoff protein (vhs). Interacts with
CC       VP11/12. Associates with the VP16-induced complex; binding to host
CC       HCFC1 activates VP16 for association with the octamer motif-binding
CC       host protein POU2F1, to form a multiprotein-DNA complex responsible for
CC       activating transcription of the viral immediate early genes (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P04486}.
CC       Host nucleus {ECO:0000250|UniProtKB:P04486}.
CC   -!- DOMAIN: The transcriptional activation region seems to target many
CC       proteins of the RNA polymerase II transcription machinery.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae tegument protein VP16 protein
CC       family. {ECO:0000305}.
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DR   EMBL; M75098; AAA45862.1; -; Genomic_DNA.
DR   PIR; A41562; IXBE33.
DR   RefSeq; YP_009137200.1; NC_001798.2.
DR   SMR; P68335; -.
DR   BioGRID; 1677940; 1.
DR   DNASU; 1487335; -.
DR   GeneID; 1487335; -.
DR   KEGG; vg:1487335; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0039695; P:DNA-templated viral transcription; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.1290.10; -; 1.
DR   InterPro; IPR003174; Alpha_TIF.
DR   InterPro; IPR036538; Alpha_TIF_sf.
DR   InterPro; IPR021051; HSV_VP16_C.
DR   Pfam; PF02232; Alpha_TIF; 1.
DR   Pfam; PF12149; HSV_VP16_C; 1.
DR   SMART; SM00814; Alpha_TIF; 1.
DR   SUPFAM; SSF56548; SSF56548; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Host nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Virion; Virion tegument.
FT   CHAIN           1..490
FT                   /note="Tegument protein VP16"
FT                   /id="PRO_0000115800"
FT   REGION          11..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..490
FT                   /note="Transcriptional activation"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        15..29
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            443
FT                   /note="Critical role in activation"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   490 AA;  54621 MW;  2E9FDA8D0D8BC174 CRC64;
     MDLLVDDLFA DADGVSPPPP RPAGGPKNTP AAPPLYATGR LSQAQLMPSP PMPVPPAALF
     NRLLDDLGFS AGPALCTMLD TWNEDLFSGF PTNADMYREC KFLSTLPSDV IDWGDAHVPE
     RSPIDIRAHG DVAFPTLPAT RDELPSYYEA MAQFFRGELR AREESYRTVL ANFCSALYRY
     LRASVRQLHR QAHMRGRNRD LREMLRTTIA DRYYRETARL ARVLFLHLYL FLSREILWAA
     YAEQMMRPDL FDGLCCDLES WRQLACLFQP LMFINGSLTV RGVPVEARRL RELNHIREHL
     NLPLVRSAAA EEPGAPLTTP PVLQGNQARS SGYFMLLIRA KLDSYSSVAT SEGESVMREH
     AYSRGRTRNN YGSTIEGLLD LPDDDDAPAE AGLVAPRMSF LSAGQRPRRL STTAPITDVS
     LGDELRLDGE EVDMTPADAL DDFDLEMLGD VESPSPGMTH DPVSYGALDV DDFEFEQMFT
     DAMGIDDFGG