VP16_HHV2H
ID VP16_HHV2H Reviewed; 490 AA.
AC P68336; P23990; P29793;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 1.
DT 02-JUN-2021, entry version 81.
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 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=1653757; DOI=10.1016/0378-1119(91)90278-j;
RA Cress A., Triezenberg S.J.;
RT "Nucleotide and deduced amino acid sequences of the gene encoding virion
RT protein 16 of herpes simplex virus type 2.";
RL Gene 103:235-238(1991).
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).
RN [3]
RP INTERACTION WITH VP11/12.
RC STRAIN=186;
RX PubMed=11087097; DOI=10.1007/s007050070045;
RA Kato K., Daikoku T., Goshima F., Kume H., Yamaki K., Nishiyama Y.;
RT "Synthesis, subcellular localization and VP16 interaction of the herpes
RT simplex virus type 2 UL46 gene product.";
RL Arch. Virol. 145:2149-2162(2000).
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; M60050; AAA45863.1; -; Genomic_DNA.
DR EMBL; Z86099; CAB06734.1; -; Genomic_DNA.
DR PIR; JS0689; JS0689.
DR RefSeq; YP_009137200.1; NC_001798.2.
DR SMR; P68336; -.
DR BioGRID; 1677940; 1.
DR IntAct; P68336; 9.
DR PRIDE; P68336; -.
DR DNASU; 1487335; -.
DR GeneID; 1487335; -.
DR KEGG; vg:1487335; -.
DR Proteomes; UP000001874; Genome.
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 DisProt; DP00087; -.
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 1: Evidence at protein level;
KW DNA-binding; Host nucleus; Host-virus interaction; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Virion;
KW Virion tegument.
FT CHAIN 1..490
FT /note="Tegument protein VP16"
FT /id="PRO_0000115801"
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"
FT CONFLICT 12
FT /note="A -> R (in Ref. 1; AAA45863)"
FT /evidence="ECO:0000305"
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
