ICP22_VZVD
ID ICP22_VZVD Reviewed; 278 AA.
AC P09255;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 77.
DE RecName: Full=Transcriptional regulator ICP22 homolog;
DE AltName: Full=Immediate-early protein 63;
DE Short=IE63;
DE AltName: Full=Transcriptional regulator IE63;
GN ORFNames=ORF63;
GN and
GN ORFNames=ORF70;
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 FUNCTION.
RX PubMed=1316489; DOI=10.1128/jvi.66.6.3899-3903.1992;
RA Jackers P., Defechereux P., Baudoux L., Lambert C., Massaer M.,
RA Merville-Louis M.P., Rentier B., Piette J.;
RT "Characterization of regulatory functions of the varicella-zoster virus
RT gene 63-encoded protein.";
RL J. Virol. 66:3899-3903(1992).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9618542; DOI=10.1073/pnas.95.12.7080;
RA Lungu O., Panagiotidis C.A., Annunziato P.W., Gershon A.A.,
RA Silverstein S.J.;
RT "Aberrant intracellular localization of Varicella-Zoster virus regulatory
RT proteins during latency.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7080-7085(1998).
RN [5]
RP PHOSPHORYLATION BY ORF47 PROTEIN SERINE KINASE.
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 [6]
RP INTERACTION WITH IE62.
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 [7]
RP FUNCTION, AND INTERACTION WITH HOST GTF2E1; GTF2H2 AND POLR2A.
RX PubMed=15843171; DOI=10.1515/bc.2005.031;
RA Di Valentin E., Bontems S., Habran L., Jolois O., Markine-Goriaynoff N.,
RA Vanderplasschen A., Sadzot-Delvaux C., Piette J.;
RT "Varicella-zoster virus IE63 protein represses the basal transcription
RT machinery by disorganizing the pre-initiation complex.";
RL Biol. Chem. 386:255-267(2005).
RN [8]
RP INTERACTION WITH HOST ASF1A.
RX PubMed=18971269; DOI=10.1128/jvi.00645-08;
RA Ambagala A.P., Bosma T., Ali M.A., Poustovoitov M., Chen J.J.,
RA Gershon M.D., Adams P.D., Cohen J.I.;
RT "Varicella-zoster virus immediate-early 63 protein interacts with human
RT antisilencing function 1 protein and alters its ability to bind histones
RT h3.1 and h3.3.";
RL J. Virol. 83:200-209(2009).
CC -!- FUNCTION: Immediate early (EI) protein that functions as a
CC transcriptional regulator of cellular and viral mRNAs mainly by
CC interacting with several general transcription factors thereby
CC disorganizing the preinitiation complex at certain promoters. May
CC additionally help to regulate levels of histones in virus-infected
CC cells by interacting with host ASF1. By inhibiting host transcriptional
CC program, IE63 plays a major role in the ability of VZV to overcome the
CC innate immune response to the virus. {ECO:0000269|PubMed:1316489,
CC ECO:0000269|PubMed:15843171}.
CC -!- SUBUNIT: Interacts with IE62; this interaction modulates the function
CC of IE62. Interacts with several components of host pre-initiation
CC complex including GTF2E1, GTF2H2 and POLR2A; these interactions lead to
CC repression of gene transcription. Interacts with host ASF1A; altering
CC its ability to bind histones. {ECO:0000269|PubMed:12429517,
CC ECO:0000269|PubMed:15843171, ECO:0000269|PubMed:18971269}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:9618542}. Host
CC nucleus {ECO:0000269|PubMed:9618542}. Virion tegument
CC {ECO:0000269|PubMed:9618542}. Note=During the first stage of infection,
CC IE63 is mostly expressed in the nucleus and also slightly in the
CC cytoplasm, and during latency, IE63 localizes in the cytoplasm quite
CC exclusively.
CC -!- PTM: Phosphorylated in vitro by host and by protein kinase ORF47.
CC {ECO:0000269|PubMed:11507231}.
CC -!- SIMILARITY: Belongs to the herpesviridae ICP22 family. {ECO:0000305}.
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DR EMBL; X04370; CAA27953.1; -; Genomic_DNA.
DR EMBL; X04370; CAA27946.1; -; Genomic_DNA.
DR EMBL; X02132; CAA26045.1; -; Genomic_DNA.
DR PIR; B27345; EDBE63.
DR RefSeq; NP_040185.1; NC_001348.1.
DR RefSeq; NP_040192.1; NC_001348.1.
DR BioGRID; 971533; 1.
DR iPTMnet; P09255; -.
DR PRIDE; P09255; -.
DR GeneID; 1487700; -.
DR GeneID; 1487711; -.
DR KEGG; vg:1487700; -.
DR KEGG; vg:1487711; -.
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:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-KW.
DR InterPro; IPR003403; IE68.
DR Pfam; PF02479; Herpes_IE68; 1.
PE 1: Evidence at protein level;
KW Early protein; Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host nucleus;
KW Host-virus interaction;
KW Inhibition of eukaryotic host transcription initiation by virus;
KW Inhibition of host RNA polymerase II by virus; Reference proteome;
KW Transcription; Transcription regulation; Virion; Virion tegument.
FT CHAIN 1..278
FT /note="Transcriptional regulator ICP22 homolog"
FT /id="PRO_0000115843"
FT REGION 1..142
FT /note="IE62-binding"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 30495 MW; 2CFA03C199F9A385 CRC64;
MFCTSPATRG DSSESKPGAS VDVNGKMEYG SAPGPLNGRD TSRGPGAFCT PGWEIHPARL
VEDINRVFLC IAQSSGRVTR DSRRLRRICL DFYLMGRTRQ RPTLACWEEL LQLQPTQTQC
LRATLMEVSH RPPRGEDGFI EAPNVPLHRS ALECDVSDDG GEDDSDDDGS TPSDVIEFRD
SDAESSDGED FIVEEESEES TDSCEPDGVP GDCYRDGDGC NTPSPKRPQR AIERYAGAET
AEYTAAKALT ALGEGGVDWK RRRHEAPRRH DIPPPHGV
