P04486 (VP16_HHV1F) Reviewed, UniProtKB/Swiss-Prot

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 F) (HHV-1) (Human herpes simplex virus 1)

Taxonomic identifier

10304 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus › Human herpesvirus 1

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 By similarity. Ref.2 May play a role in the aggregation of tegument proteins around nucleocapsids during virus morphogenesis Potential. Ref.2
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 By similarity. Ref.2 Ref.5
Subcellular location	Virion tegument. Host nucleus Ref.3 Ref.4.
Domain	The transcriptional activation region seems to target many proteins of the RNA polymerase II transcription machinery By similarity.
Sequence similarities	Belongs to the herpesviridae tegument protein VP16 protein family.
Sequence caution	The sequence AAA45766.1 differs from that shown. Reason: Erroneous initiation.

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
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_0000115799

Regions

Region

411 – 490

80

Transcriptional activation By similarity

Sites

Site

442

1

Critical role in activation By similarity

Amino acid modifications

Modified residue

18

1

Phosphoserine By similarity

Modified residue

353

1

Phosphoserine By similarity

Modified residue

411

1

Phosphoserine By similarity

Modified residue

452

1

Phosphoserine By similarity

Secondary structure

1

.

.

.

490

Helix Strand Turn

Details...

Helix

471 – 477

7

Sequences

	Sequence		Length	Mass (Da)
	P04486 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: 014372DE8FE6C417	FASTA	490	54,316
	10 20 30 40 50 60 MDLLVDELFA DMDADGASPP PPRPAGGPKN TPAAPPLYAT GRLSQAQLMP SPPMPVPPAA 70 80 90 100 110 120 LFNRLLDDLG FSAGPALCTM LDTWNEDLFS ALPTNADLYR ECKFLSTLPS DVVEWGDAYV 130 140 150 160 170 180 PERAQIDIRA 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

References

[1]	"Nucleotide sequence and predicted amino acid sequence of a protein encoded in a small herpes simplex virus DNA fragment capable of trans-inducing alpha genes." Pellett P.E., McKnight J.L.C., Jenkins F.J., Roizman B. Proc. Natl. Acad. Sci. U.S.A. 82:5870-5874(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Combinatorial transcription of herpes simplex virus and varicella zoster virus immediate early genes is strictly determined by the cellular coactivator HCF-1." Narayanan A., Nogueira M.L., Ruyechan W.T., Kristie T.M. J. Biol. Chem. 280:1369-1375(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HUMAN HCFC1.
[3]	"Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear import." Yedowitz J.C., Kotsakis A., Schlegel E.F., Blaho J.A. J. Virol. 79:4730-4743(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"Comprehensive characterization of extracellular herpes simplex virus type 1 virions." Loret S., Guay G., Lippe R. J. Virol. 82:8605-8618(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53." Langlois C., Mas C., Di Lello P., Jenkins L.M., Legault P., Omichinski J.G. J. Am. Chem. Soc. 130:10596-10604(2008) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 445-479 IN COMPLEX WITH THE TFB1 SUBUNIT OF TFIIH.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K03350 Genomic DNA. Translation: AAA45766.1. Different initiation.

PIR

IXBE1F. A03727.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K2U	NMR	-	B	456-490	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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

EvolutionaryTrace

P04486.

Entry information

Entry name

VP16_HHV1F

Accession

Primary (citable) accession number: P04486

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	September 22, 2009
Last modified:	April 3, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program