Tegument protein VP16 - Human herpesvirus 1 (strain 17) (HHV-1)

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P06492 (VP16_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tegument protein VP16

Alternative name(s):
Alpha trans-inducing protein
Alpha-TIF
ICP25
Vmw65

Gene names

ORF Names:

UL48

Organism

Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]

Taxonomic identifier

10299 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus ›

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional activator of immediate-early (IE) gene products (alpha genes). Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F 1. VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection. May play a role in the aggregation of tegument proteins around nucleocapsids during virus morphogenesis Potential.
Subunit structure	Interacts with VP22. Interacts with gH (via C-terminus). Interacts with the virion host shutoff protein (vhs). Interacts with VP11/12. Associates with the VP16-induced complex; binding to host HCFC1 activates VP16 for association with the octamer motif-binding host protein POU2F1, to form a multiprotein-DNA complex responsible for activating transcription of the viral immediate early genes. Ref.6 Ref.7 Ref.9 Ref.10 Ref.12
Subcellular location	Virion tegument By similarity. Host nucleus By similarity.
Domain	The transcriptional activation region seems to target many proteins of the RNA polymerase II transcription machinery.
Sequence similarities	Belongs to the herpesviridae tegument protein VP16 protein family.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Host nucleus Virion Virion tegument
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell viral tegument Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 490

490

Tegument protein VP16

PRO_0000115798

Regions

Region

411 – 490

Transcriptional activation

Sites

Site

442

Critical role in activation

Amino acid modifications

Modified residue

Phosphoserine Ref.8

Modified residue

353

Phosphoserine Ref.8

Modified residue

411

Phosphoserine Ref.8

Modified residue

452

Phosphoserine Ref.8

Natural variations

Natural variant

A → S in strain: Nonneuroinvasive mutant HF10.

Natural variant

124

T → A in strain: Nonneuroinvasive mutant HF10.

Natural variant

235

T → A in strain: 17 syn+.

Natural variant

390

E → K in strain: Nonneuroinvasive mutant HF10.

Natural variant

413

A → P in strain: Nonneuroinvasive mutant HF10.

Secondary structure

490

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P06492 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 8DDDEDEDB2A699D3
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FASTA

490

54,345

        10         20         30         40         50         60 
MDLLVDELFA DMNADGASPP PPRPAGGPKN TPAAPPLYAT GRLSQAQLMP SPPMPVPPAA 

        70         80         90        100        110        120 
LFNRLLDDLG FSAGPALCTM LDTWNEDLFS ALPTNADLYR ECKFLSTLPS DVVEWGDAYV 

       130        140        150        160        170        180 
PERTQIDIRA HGDVAFPTLP ATRDGLGLYY EALSRFFHAE LRAREESYRT VLANFCSALY 

       190        200        210        220        230        240 
RYLRASVRQL HRQAHMRGRD RDLGEMLRAT IADRYYRETA RLARVLFLHL YLFLTREILW 

       250        260        270        280        290        300 
AAYAEQMMRP DLFDCLCCDL ESWRQLAGLF QPFMFVNGAL TVRGVPIEAR RLRELNHIRE 

       310        320        330        340        350        360 
HLNLPLVRSA ATEEPGAPLT TPPTLHGNQA RASGYFMVLI RAKLDSYSSF TTSPSEAVMR 

       370        380        390        400        410        420 
EHAYSRARTK NNYGSTIEGL LDLPDDDAPE EAGLAAPRLS FLPAGHTRRL STAPPTDVSL 

       430        440        450        460        470        480 
GDELHLDGED VAMAHADALD DFDLDMLGDG DSPGPGFTPH DSAPYGALDM ADFEFEQMFT 

       490 
DALGIDEYGG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence of the herpes simplex virus type 1 gene whose product is responsible for transcriptional activation of immediate early promoters." Dalrymple M.A., McGeoch D.J., Davison A.J., Preston C.M. Nucleic Acids Res. 13:7865-7879(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1." McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P. J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus." Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y. Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nonneuroinvasive mutant HF10.
[4]	"Herpes simplex virus type 1 bacterial artificial chromosome." Cunningham C., Davison A.J. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 17 syn+.
[5]	"The C-terminal 79 amino acids of the herpes simplex virus regulatory protein, Vmw65, efficiently activate transcription in yeast and mammalian cells in chimeric DNA-binding proteins." Cousens D.J., Greaves R.F., Goding C.R., O'Hare P. EMBO J. 8:2337-2342(1989) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING.
[6]	"Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs." Smibert C.A., Popova B., Xiao P., Capone J.P., Smiley J.R. J. Virol. 68:2339-2346(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VIRION HOST SHUTOFF PROTEIN. Strain: KOS.
[7]	"The cytoplasmic tail of Herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo." Gross S.T., Harley C.A., Wilson D.W. Virology 317:1-12(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GH. Strain: SC16.
[8]	"Phosphorylation of the VP16 transcriptional activator protein during herpes simplex virus infection and mutational analysis of putative phosphorylation sites." Ottosen S., Herrera F.J., Doroghazi J.R., Hull A., Mittal S., Lane W.S., Triezenberg S.J. Virology 345:468-481(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-18; SER-353; SER-411 AND SER-452.
[9]	"Virion incorporation of the herpes simplex virus type 1 tegument protein VP22 occurs via glycoprotein E-specific recruitment to the late secretory pathway." Stylianou J., Maringer K., Cook R., Bernard E., Elliott G. J. Virol. 83:5204-5218(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VP22.
[10]	"The herpes simplex virus VP16-induced complex: the makings of a regulatory switch." Wysocka J., Herr W. Trends Biochem. Sci. 28:294-304(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW, IDENTIFICATION IN THE VP16-INDUCED COMPLEX.
[11]	"Structural properties of the promiscuous VP16 activation domain." Jonker H.R., Wechselberger R.W., Boelens R., Folkers G.E., Kaptein R. Biochemistry 44:827-839(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 465-490.
[12]	"Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16." Liu Y., Gong W., Huang C.C., Herr W., Cheng X. Genes Dev. 13:1692-1703(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 49-412, INTERACTION WITH HUMAN HCFC1 AND HUMAN POU2F1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14112 Genomic DNA. Translation: CAA32298.1.
X03141 Genomic DNA. Translation: CAA26913.1.
DQ889502 Genomic DNA. Translation: ABI63509.1.
FJ593289 Genomic DNA. Translation: ACM62271.1.

PIR

IXBE17. A24118.

RefSeq

NP_044650.1. NC_001806.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
16VP	X-ray	2.10	A	49-412	[»]
2PHE	NMR	-	C	465-490	[»]
2PHG	NMR	-	B	465-490	[»]

ProteinModelPortal

P06492.

SMR

P06492. Positions 59-349, 456-490.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-275736.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2703416.

Phylogenomic databases

ProtClustDB

PHA3380.

Family and domain databases

Gene3D

1.10.1290.10. 1 hit.

InterPro

IPR003174. Alpha_TIF.
IPR021051. HSV_VP16_C.
[Graphical view]

Pfam

PF02232. Alpha_TIF. 1 hit.
PF12149. HSV_VP16_C. 1 hit.
[Graphical view]

SMART

SM00814. Alpha_TIF. 1 hit.
[Graphical view]

SUPFAM

SSF56548. VP16_like. 1 hit.

ProtoNet

Search...

Other

BindingDB

P06492.

ChEMBL

CHEMBL4218.

EvolutionaryTrace

P06492.

Entry information

Entry name

VP16_HHV11

Accession

Primary (citable) accession number: P06492
Secondary accession number(s): B9VQH6, Q09I86

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents