TEG5_HHV11
ID TEG5_HHV11 Reviewed; 693 AA.
AC P10231; Q09I87;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tegument protein UL47;
DE AltName: Full=82/81 kDa tegument protein;
DE AltName: Full=VMW82/81;
DE AltName: Full=VP13/14;
GN ORFNames=UL47;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION OF PROTEIN, AND SUBCELLULAR LOCATION.
RX PubMed=2177087; DOI=10.1099/0022-1317-71-12-2953;
RA McLean G., Rixon F., Langeland N., Haarr L., Marsden H.;
RT "Identification and characterization of the virion protein products of
RT herpes simplex virus type 1 gene UL47.";
RL J. Gen. Virol. 71:2953-2960(1990).
RN [5]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=11222679; DOI=10.1128/jvi.75.6.2566-2574.2001;
RA Donnelly M., Elliott G.;
RT "Nuclear localization and shuttling of herpes simplex virus tegument
RT protein VP13/14.";
RL J. Virol. 75:2566-2574(2001).
RN [6]
RP RNA-BINDING, NUCLEAR LOCALIZATION SIGNAL, AND SUBCELLULAR LOCATION.
RX PubMed=17166902; DOI=10.1128/jvi.01677-06;
RA Donnelly M., Verhagen J., Elliott G.;
RT "RNA binding by the herpes simplex virus type 1 nucleocytoplasmic shuttling
RT protein UL47 is mediated by an N-terminal arginine-rich domain that also
RT functions as its nuclear localization signal.";
RL J. Virol. 81:2283-2296(2007).
RN [7]
RP SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=18715912; DOI=10.1128/jvi.01403-08;
RA Williams P., Verhagen J., Elliott G.;
RT "Characterization of a CRM1-dependent nuclear export signal in the C
RT terminus of herpes simplex virus type 1 tegument protein UL47.";
RL J. Virol. 82:10946-10952(2008).
RN [8]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH US3.
RX PubMed=21734045; DOI=10.1128/jvi.00845-11;
RA Kato A., Liu Z., Minowa A., Imai T., Tanaka M., Sugimoto K., Nishiyama Y.,
RA Arii J., Kawaguchi Y.;
RT "Herpes simplex virus 1 protein kinase Us3 and major tegument protein UL47
RT reciprocally regulate their subcellular localization in infected cells.";
RL J. Virol. 85:9599-9613(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH UL41/VHS.
RX PubMed=23589852; DOI=10.1073/pnas.1305475110;
RA Shu M., Taddeo B., Zhang W., Roizman B.;
RT "Selective degradation of mRNAs by the HSV host shutoff RNase is regulated
RT by the UL47 tegument protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1669-E1675(2013).
RN [10]
RP FUNCTION, AND INTERACTION WITH UL31 AND UL34.
RX PubMed=24522907; DOI=10.1128/jvi.00137-14;
RA Liu Z., Kato A., Shindo K., Noda T., Sagara H., Kawaoka Y., Arii J.,
RA Kawaguchi Y.;
RT "Herpes simplex virus 1 UL47 interacts with viral nuclear egress factors
RT UL31, UL34, and Us3 and regulates viral nuclear egress.";
RL J. Virol. 88:4657-4667(2014).
CC -!- FUNCTION: Tegument protein that can bind to various RNA transcripts.
CC Plays a role in the attenuation of selective viral and cellular mRNA
CC degradation by modulating the activity of host shutoff RNase UL41/VHS.
CC Also plays a role in the primary envelopement of virions in the
CC perinuclear space, probably by interacting with two nuclear egress
CC proteins UL31 and UL34. {ECO:0000269|PubMed:23589852,
CC ECO:0000269|PubMed:24522907}.
CC -!- SUBUNIT: Interacts with US3 kinase. Interacts with UL31 and UL34; these
CC interactions seem important for efficient virion nuclear egress.
CC Interacts with UL41/VHS. {ECO:0000269|PubMed:21734045,
CC ECO:0000269|PubMed:23589852, ECO:0000269|PubMed:24522907}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:2177087}.
CC Host nucleus {ECO:0000269|PubMed:17166902, ECO:0000269|PubMed:18715912,
CC ECO:0000269|PubMed:21734045}. Host cytoplasm
CC {ECO:0000269|PubMed:17166902, ECO:0000269|PubMed:18715912}. Note=Major
CC tegument protein of the virion. Undergoes nucleocytoplasmic shuttling
CC during infection. Localizes to the major sites of transcription in the
CC infected cell nucleus.
CC -!- DOMAIN: The nuclear export signal is CRM1-dependent.
CC {ECO:0000269|PubMed:18715912}.
CC -!- PTM: Phosphorylated by US3. This phosphorylation is required for proper
CC nuclear localization. {ECO:0000269|PubMed:21734045}.
CC -!- MISCELLANEOUS: Expressed in late in the infection.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae HHV-1 UL47 family.
CC {ECO:0000305}.
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DR EMBL; X14112; CAA32297.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63508.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62270.1; -; Genomic_DNA.
DR PIR; B30089; TNBEF7.
DR RefSeq; YP_009137122.1; NC_001806.2.
DR BioGRID; 971442; 4.
DR IntAct; P10231; 1.
DR MINT; P10231; -.
DR PRIDE; P10231; -.
DR DNASU; 2703415; -.
DR GeneID; 2703415; -.
DR KEGG; vg:2703415; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR005029; Herpes_UL47.
DR Pfam; PF03362; Herpes_UL47; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Late protein; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation; Virion;
KW Virion tegument.
FT CHAIN 1..693
FT /note="Tegument protein UL47"
FT /id="PRO_0000116073"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..75
FT /note="RNA-binding"
FT MOTIF 63..75
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:11222679,
FT ECO:0000269|PubMed:17166902"
FT MOTIF 647..670
FT /note="Nuclear export signal"
FT COMPBIAS 56..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 73817 MW; 283737D7D33B5C93 CRC64;
MSAREPAGRR RRASTRPRAS PVADEPAGDG VGFMGYLRAV FRGDDDSELE ALEEMAGDEP
PVRRRREGPR ARRRRASEAP PTSHRRASRQ RPGPDAARSQ SVRGRLDDDD EVPRGPPQAR
QGGYLGPVDA RAILGRVGGS RVAPSPLFLE ELQYEEDDYP EAVGPEDGGG ARSPPKVEVL
EGRVPGPELR AAFPLDRLAP QVAVWDESVR SALALGHPAG FYPCPDSAFG LSRVGVMHFA
SPDNPAVFFR QTLQQGEALA WYITGDGILD LTDRRTKTSP AQAMSFLADA VVRLAINGWV
CGTRLHAEAR GSDLDDRAAE LRRQFASLTA LRPVGAAAVP LLSAGGLVSP QSGPDAAVFR
SSLGSLLYWP GVRALLDRDC RVAARYAGRM TYLATGALLA RFNPDAVRCV LTREAAFLGR
VLDVLAVMAE QTVQWLSVVV GARLHPHVHH PAFADVAREE LFRALPLGSP AVVGAEHEAL
GDTAARRLLA NSGLNAVLGA AVYALHTALA TVTLKYARAC GDAHRRRDDA AATRAILAAG
LVLQRLLGFA DTVVACVTLA AFDGGFTAPE VGTYTPLRYA CVLRATQPLY ARTTPAKFWA
DVRAAAEHVD LRPASSAPRA PVSGTADPAF LLKDLEPFPP APVSGGSVLG PRVRVVDIMS
QFRKLLMGDE GAAALRAHVS GRRATGLGGP PRP
