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   27-MAR-2024, entry version 98.
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; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
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 envelopment 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   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 DNA-templated transcription; 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
//