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Protein

Tegument protein UL47

Gene

UL47

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Tegument protein that can bind to various RNA transcripts. Plays a role in the attenuation of selective viral and cellular mRNA degradation by modulating the activity of host shutoff RNase UL41/VHS. Plays also a role in the primary envelopement of virions in the perinuclear space, probably by interacting with two nuclear egress proteins UL31 and UL34.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tegument protein UL47
Alternative name(s):
82/81 kDa tegument protein
VMW82/81
VP13/14
Gene namesi
ORF Names:UL47
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000009294 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus, Virion, Virion tegument

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 693693Tegument protein UL47PRO_0000116073Add
BLAST

Post-translational modificationi

Phosphorylated by US3. This phosphorylation is required for proper nuclear localization.1 Publication

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with US3 kinase. Interacts with UL31 and UL34; these interactions seem important for efficient virion nuclear egress. Interacts with UL41/VHS.3 Publications

Protein-protein interaction databases

IntActiP10231. 1 interaction.
MINTiMINT-6732739.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 7526RNA-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi63 – 7513Nuclear localization signal2 PublicationsAdd
BLAST
Motifi647 – 67024Nuclear export signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 124Poly-Arg
Compositional biasi107 – 1104Poly-Asp

Domaini

The nuclear export signal is CRM1-dependent.1 Publication

Sequence similaritiesi

Family and domain databases

InterProiIPR005029. Herpes_UL47.
[Graphical view]
PfamiPF03362. Herpes_UL47. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10231-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAREPAGRR RRASTRPRAS PVADEPAGDG VGFMGYLRAV FRGDDDSELE
60 70 80 90 100
ALEEMAGDEP PVRRRREGPR ARRRRASEAP PTSHRRASRQ RPGPDAARSQ
110 120 130 140 150
SVRGRLDDDD EVPRGPPQAR QGGYLGPVDA RAILGRVGGS RVAPSPLFLE
160 170 180 190 200
ELQYEEDDYP EAVGPEDGGG ARSPPKVEVL EGRVPGPELR AAFPLDRLAP
210 220 230 240 250
QVAVWDESVR SALALGHPAG FYPCPDSAFG LSRVGVMHFA SPDNPAVFFR
260 270 280 290 300
QTLQQGEALA WYITGDGILD LTDRRTKTSP AQAMSFLADA VVRLAINGWV
310 320 330 340 350
CGTRLHAEAR GSDLDDRAAE LRRQFASLTA LRPVGAAAVP LLSAGGLVSP
360 370 380 390 400
QSGPDAAVFR SSLGSLLYWP GVRALLDRDC RVAARYAGRM TYLATGALLA
410 420 430 440 450
RFNPDAVRCV LTREAAFLGR VLDVLAVMAE QTVQWLSVVV GARLHPHVHH
460 470 480 490 500
PAFADVAREE LFRALPLGSP AVVGAEHEAL GDTAARRLLA NSGLNAVLGA
510 520 530 540 550
AVYALHTALA TVTLKYARAC GDAHRRRDDA AATRAILAAG LVLQRLLGFA
560 570 580 590 600
DTVVACVTLA AFDGGFTAPE VGTYTPLRYA CVLRATQPLY ARTTPAKFWA
610 620 630 640 650
DVRAAAEHVD LRPASSAPRA PVSGTADPAF LLKDLEPFPP APVSGGSVLG
660 670 680 690
PRVRVVDIMS QFRKLLMGDE GAAALRAHVS GRRATGLGGP PRP
Length:693
Mass (Da):73,817
Last modified:July 1, 1989 - v1
Checksum:i283737D7D33B5C93
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32297.1.
DQ889502 Genomic DNA. Translation: ABI63508.1.
FJ593289 Genomic DNA. Translation: ACM62270.1.
PIRiB30089. TNBEF7.

Genome annotation databases

KEGGivg:2703415.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32297.1.
DQ889502 Genomic DNA. Translation: ABI63508.1.
FJ593289 Genomic DNA. Translation: ACM62270.1.
PIRiB30089. TNBEF7.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP10231. 1 interaction.
MINTiMINT-6732739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGivg:2703415.

Family and domain databases

InterProiIPR005029. Herpes_UL47.
[Graphical view]
PfamiPF03362. Herpes_UL47. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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.
  3. "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+.
  4. "Identification and characterization of the virion protein products of herpes simplex virus type 1 gene UL47."
    McLean G., Rixon F., Langeland N., Haarr L., Marsden H.
    J. Gen. Virol. 71:2953-2960(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROTEIN, SUBCELLULAR LOCATION.
  5. "Nuclear localization and shuttling of herpes simplex virus tegument protein VP13/14."
    Donnelly M., Elliott G.
    J. Virol. 75:2566-2574(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
  6. "RNA binding by the herpes simplex virus type 1 nucleocytoplasmic shuttling protein UL47 is mediated by an N-terminal arginine-rich domain that also functions as its nuclear localization signal."
    Donnelly M., Verhagen J., Elliott G.
    J. Virol. 81:2283-2296(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION.
  7. "Characterization of a CRM1-dependent nuclear export signal in the C terminus of herpes simplex virus type 1 tegument protein UL47."
    Williams P., Verhagen J., Elliott G.
    J. Virol. 82:10946-10952(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL.
  8. "Herpes simplex virus 1 protein kinase Us3 and major tegument protein UL47 reciprocally regulate their subcellular localization in infected cells."
    Kato A., Liu Z., Minowa A., Imai T., Tanaka M., Sugimoto K., Nishiyama Y., Arii J., Kawaguchi Y.
    J. Virol. 85:9599-9613(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH US3.
  9. "Selective degradation of mRNAs by the HSV host shutoff RNase is regulated by the UL47 tegument protein."
    Shu M., Taddeo B., Zhang W., Roizman B.
    Proc. Natl. Acad. Sci. U.S.A. 110:E1669-E1675(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UL41/VHS.
  10. "Herpes simplex virus 1 UL47 interacts with viral nuclear egress factors UL31, UL34, and Us3 and regulates viral nuclear egress."
    Liu Z., Kato A., Shindo K., Noda T., Sagara H., Kawaoka Y., Arii J., Kawaguchi Y.
    J. Virol. 88:4657-4667(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UL31 AND UL34.

Entry informationi

Entry nameiTEG5_HHV11
AccessioniPrimary (citable) accession number: P10231
Secondary accession number(s): Q09I87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 22, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Expressed in late in the infection.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.