ICP4_VZVD
ID ICP4_VZVD Reviewed; 1310 AA.
AC P09310;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 97.
DE RecName: Full=Major viral transcription factor ICP4 homolog;
DE AltName: Full=Immediate-early protein 62;
DE Short=IE62;
GN ORFNames=ORF62;
GN and
GN ORFNames=ORF71;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2981964; DOI=10.1099/0022-1317-66-2-207;
RA Davison A.J., Scott J.E.;
RT "DNA sequence of the major inverted repeat in the varicella-zoster virus
RT genome.";
RL J. Gen. Virol. 66:207-220(1985).
RN [3]
RP CHARACTERIZATION.
RX PubMed=3023701; DOI=10.1128/jvi.61.1.225-228.1987;
RA Felser J.M., Straus S.E., Ostrove J.M.;
RT "Varicella-zoster virus complements herpes simplex virus type 1
RT temperature-sensitive mutants.";
RL J. Virol. 61:225-228(1987).
RN [4]
RP FUNCTION.
RX PubMed=2835512; DOI=10.1128/jvi.62.6.2076-2082.1988;
RA Felser J.M., Kinchington P.R., Inchauspe G., Straus S.E., Ostrove J.M.;
RT "Cell lines containing varicella-zoster virus open reading frame 62 and
RT expressing the 'IE' 175 protein complement ICP4 mutants of herpes simplex
RT virus type 1.";
RL J. Virol. 62:2076-2082(1988).
RN [5]
RP MUTAGENESIS OF GLN-545; ASN-546 AND LYS-548.
RX PubMed=7907417; DOI=10.1093/nar/22.3.270;
RA Tyler J.K., Allen K.E., Everett R.D.;
RT "Mutation of a single lysine residue severely impairs the DNA recognition
RT and regulatory functions of the VZV gene 62 transactivator protein.";
RL Nucleic Acids Res. 22:270-278(1994).
RN [6]
RP INTERACTION WITH IE4.
RX PubMed=10873781; DOI=10.1006/viro.2000.0389;
RA Spengler M.L., Ruyechan W.T., Hay J.;
RT "Physical interaction between two varicella zoster virus gene regulatory
RT proteins, IE4 and IE62.";
RL Virology 272:375-381(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10666257; DOI=10.1128/jvi.74.5.2265-2277.2000;
RA Kinchington P.R., Fite K., Turse S.E.;
RT "Nuclear accumulation of IE62, the varicella-zoster virus (VZV) major
RT transcriptional regulatory protein, is inhibited by phosphorylation
RT mediated by the VZV open reading frame 66 protein kinase.";
RL J. Virol. 74:2265-2277(2000).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11533174; DOI=10.1128/jvi.75.19.9106-9113.2001;
RA Kinchington P.R., Fite K., Seman A., Turse S.E.;
RT "Virion association of IE62, the varicella-zoster virus (VZV) major
RT transcriptional regulatory protein, requires expression of the VZV open
RT reading frame 66 protein kinase.";
RL J. Virol. 75:9106-9113(2001).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=11507231; DOI=10.1128/jvi.75.18.8854-8858.2001;
RA Kenyon T.K., Lynch J.M., Hay J., Ruyechan W.T., Grose C.;
RT "Varicella-zoster virus ORF47 protein serine kinase: characterization of a
RT cloned, biologically active phosphotransferase and two viral substrates,
RT ORF62 and ORF63.";
RL J. Virol. 75:8854-8858(2001).
RN [10]
RP INTERACTION WITH IE63.
RX PubMed=12429517; DOI=10.1006/viro.2002.1555;
RA Lynch J.M., Kenyon T.K., Grose C., Hay J., Ruyechan W.T.;
RT "Physical and functional interaction between the varicella zoster virus
RT IE63 and IE62 proteins.";
RL Virology 302:71-82(2002).
RN [11]
RP INTERACTION WITH HUMAN USF1 PROTEIN.
RX PubMed=14573800; DOI=10.1099/vir.0.19335-0;
RA Rahaus M., Desloges N., Yang M., Ruyechan W.T., Wolff M.H.;
RT "Transcription factor USF, expressed during the entire phase of Varicella-
RT zoster virus infection, interacts physically with the major viral
RT transactivator IE62 and plays a significant role in virus replication.";
RL J. Gen. Virol. 84:2957-2967(2003).
RN [12]
RP INTERACTION WITH HUMAN SP1 PROTEIN.
RX PubMed=12855699; DOI=10.1074/jbc.m302259200;
RA Peng H., He H., Hay J., Ruyechan W.T.;
RT "Interaction between the varicella zoster virus IE62 major transactivator
RT and cellular transcription factor Sp1.";
RL J. Biol. Chem. 278:38068-38075(2003).
RN [13]
RP NUCLEAR LOCALIZATION SIGNAL, AND PHOSPHORYLATION AT SER-686 AND SER-722.
RX PubMed=16439528; DOI=10.1128/jvi.80.4.1710-1723.2006;
RA Eisfeld A.J., Turse S.E., Jackson S.A., Lerner E.C., Kinchington P.R.;
RT "Phosphorylation of the varicella-zoster virus (VZV) major transcriptional
RT regulatory protein IE62 by the VZV open reading frame 66 protein kinase.";
RL J. Virol. 80:1710-1723(2006).
CC -!- FUNCTION: Transcriptional transactivator. May interact with and recruit
CC specific components of the general transcription machinery to viral
CC promoters and stabilize their formation for transcription initiation.
CC Negatively regulates its own transcription. This immediate early (EI)
CC protein may be necessary in virion for viral pathogenesis.
CC {ECO:0000269|PubMed:2835512}.
CC -!- SUBUNIT: Interacts with IE4 and IE63. Interacts with host USF1 and SP1.
CC {ECO:0000269|PubMed:10873781, ECO:0000269|PubMed:12429517,
CC ECO:0000269|PubMed:12855699, ECO:0000269|PubMed:14573800}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Virion tegument {ECO:0000250}. Note=Localizes to the
CC cytoplasm when phosphorylated. {ECO:0000269|PubMed:10666257,
CC ECO:0000269|PubMed:11533174}.
CC -!- PTM: Phosphorylated by ORF66 protein kinase on Ser-686 and Ser-722.
CC Also phosphorylated by ORF47 protein kinase and by human CSNK2A1/CKII.
CC {ECO:0000269|PubMed:11507231, ECO:0000269|PubMed:16439528}.
CC -!- MISCELLANEOUS: Encoded both by ORF62 and ORF71 within the inverted
CC repeat sequences bounding the Us region of the VZV genome.
CC -!- SIMILARITY: Belongs to the herpesviridae ICP4 family. {ECO:0000305}.
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DR EMBL; X04370; CAA27954.1; -; Genomic_DNA.
DR EMBL; X04370; CAA27945.1; -; Genomic_DNA.
DR EMBL; X02132; CAA26044.1; -; Genomic_DNA.
DR PIR; A27345; WZBE62.
DR RefSeq; NP_040184.1; NC_001348.1.
DR RefSeq; NP_040193.1; NC_001348.1.
DR SMR; P09310; -.
DR iPTMnet; P09310; -.
DR PRIDE; P09310; -.
DR DNASU; 1487699; -.
DR GeneID; 1487695; -.
DR GeneID; 1487699; -.
DR KEGG; vg:1487695; -.
DR KEGG; vg:1487699; -.
DR Proteomes; UP000002602; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR005205; Herpes_ICP4_C.
DR InterPro; IPR005206; Herpes_ICP4_N.
DR Pfam; PF03585; Herpes_ICP4_C; 1.
DR Pfam; PF03584; Herpes_ICP4_N; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Early protein; Host cytoplasm; Host nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Virion; Virion tegument.
FT CHAIN 1..1310
FT /note="Major viral transcription factor ICP4 homolog"
FT /id="PRO_0000115820"
FT REGION 117..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 677..685
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 686
FT /note="Phosphoserine; by viral VZV ORF66"
FT /evidence="ECO:0000269|PubMed:16439528"
FT MOD_RES 722
FT /note="Phosphoserine; by viral VZV ORF66"
FT /evidence="ECO:0000269|PubMed:16439528"
FT MUTAGEN 545
FT /note="Q->L: Decreases DNA-binding."
FT /evidence="ECO:0000269|PubMed:7907417"
FT MUTAGEN 546
FT /note="N->L: Decreases DNA-binding."
FT /evidence="ECO:0000269|PubMed:7907417"
FT MUTAGEN 548
FT /note="K->E: Complete loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:7907417"
SQ SEQUENCE 1310 AA; 139998 MW; AF58321D95CD9B56 CRC64;
MDTPPMQRST PQRAGSPDTL ELMDLLDAAA AAAEHRARVV TSSQPDDLLF GENGVMVGRE
HEIVSIPSVS GLQPEPRTED VGEELTQDDY VCEDGQDLMG SPVIPLAEVF HTRFSEAGAR
EPTGADRSLE TVSLGTKLAR SPKPPMNDGE TGRGTTPPFP QAFSPVSPAS PVGDAAGNDQ
REDQRSIPRQ TTRGNSPGLP SVVHRDRQTQ SISGKKPGDE QAGHAHASGD GVVLQKTQRP
AQGKSPKKKT LKVKVPLPAR KPGGPVPGPV EQLYHVLSDS VPAKGAKADL PFETDDTRPR
KHDARGITPR VPGRSSGGKP RAFLALPGRS HAPDPIEDDS PVEKKPKSRE FVSSSSSSSS
WGSSSEDEDD EPRRVSVGSE TTGSRSGREH APSPSNSDDS DSNDGGSTKQ NIQPGYRSIS
GPDPRIRKTK RLAGEPGRQR QKSFSLPRSR TPIIPPVSGP LMMPDGSPWP GSAPLPSNRV
RFGPSGETRE GHWEDEAVRA ARARYEASTE PVPLYVPELG DPARQYRALI NLIYCPDRDP
IAWLQNPKLT GVNSALNQFY QKLLPPGRAG TAVTGSVASP VPHVGEAMAT GEALWALPHA
AAAVAMSRRY DRAQKHFILQ SLRRAFASMA YPEATGSSPA ARISRGHPSP TTPATQAPDP
QPSAAARSLS VCPPDDRLRT PRKRKSQPVE SRSLLDKIRE TPVADARVAD DHVVSKAKRR
VSEPVTITSG PVVDPPAVIT MPLDGPAPNG GFRRIPRGAL HTPVPSDQAR KAYCTPETIA
RLVDDPLFPT AWRPALSFDP GALAEIAARR PGGGDRRFGP PSGVEALRRR CAWMRQIPDP
EDVRLLIIYD PLPGEDINGP LESTLATDPG PSWSPSRGGL SVVLAALSNR LCLPSTHAWA
GNWTGPPDVS ALNARGVLLL STRDLAFAGA VEYLGSRLAS ARRRLLVLDA VALERWPRDG
PALSQYHVYV RAPARPDAQA VVRWPDSAVT EGLARAVFAS SRTFGPASFA RIETAFANLY
PGEQPLCLCR GGNVAYTVCT RAGPKTRVPL SPREYRQYVL PGFDGCKDLA RQSRGLGLGA
ADFVDEAAHS HRAANRWGLG AALRPVFLPE GRRPGAAGPE AGDVPTWARV FCRHALLEPD
PAAEPLVLPP VAGRSVALYA SADEARNALP PIPRVMWPPG FGAAETVLEG SDGTRFVFGH
HGGSERPSET QAGRQRRTAD DREHALELDD WEVGCEDAWD SEEGGGDDGD APGSSFGVSI
VSVAPGVLRD RRVGLRPAVK VELLSSSSSS EDEDDVWGGR GGRSPPQSRG
