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E3 ubiquitin-protein ligase ICP0 (EC 2.3.2.27) (Alpha-0 protein) (Immediate-early protein IE110) (RING-type E3 ubiquitin transferase ICP0) (Trans-acting transcriptional protein ICP0) (VMW110)

 ICP0_HHV11              Reviewed;         775 AA.
P08393;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
25-OCT-2017, entry version 128.
RecName: Full=E3 ubiquitin-protein ligase ICP0;
EC=2.3.2.27;
AltName: Full=Alpha-0 protein;
AltName: Full=Immediate-early protein IE110;
AltName: Full=RING-type E3 ubiquitin transferase ICP0 {ECO:0000305};
AltName: Full=Trans-acting transcriptional protein ICP0;
AltName: Full=VMW110;
Name=ICP0; Synonyms=IE110;
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10299;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C.,
McNab D., Perry L.J., Scott J.E., Taylor P.;
"The complete DNA sequence of the long unique region in the genome of
herpes simplex virus type 1.";
J. Gen. Virol. 69:1531-1574(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3023529; DOI=10.1099/0022-1317-67-11-2365;
Perry L.J., Rixon F.J., Everett R.D., Frame M.C., McGeoch D.J.;
"Characterization of the IE110 gene of herpes simplex virus type 1.";
J. Gen. Virol. 67:2365-2380(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2846760; DOI=10.1099/0022-1317-69-11-2831;
Perry L.J., McGeoch D.J.;
"The DNA sequences of the long repeat region and adjoining parts of
the long unique region in the genome of herpes simplex virus type 1.";
J. Gen. Virol. 69:2831-2846(1988).
[4]
INTERACTION WITH HUMAN CENPA.
PubMed=11053442; DOI=10.1074/jbc.M008547200;
Lomonte P., Sullivan K.F., Everett R.D.;
"Degradation of nucleosome-associated centromeric histone H3-like
protein CENP-A induced by herpes simplex virus type 1 protein ICP0.";
J. Biol. Chem. 276:5829-5835(2001).
[5]
INTERACTION WITH HUMAN CDC34.
PubMed=11447293; DOI=10.1073/pnas.161283098;
Van Sant C., Hagglund R., Lopez P., Roizman B.;
"The infected cell protein 0 of herpes simplex virus 1 dynamically
interacts with proteasomes, binds and activates the cdc34 E2
ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin
ligase activity.";
Proc. Natl. Acad. Sci. U.S.A. 98:8815-8820(2001).
[6]
INTERACTION WITH HUMAN USP7.
PubMed=14506283; DOI=10.1074/jbc.M307200200;
Holowaty M.N., Sheng Y., Nguyen T., Arrowsmith C., Frappier L.;
"Protein interaction domains of the ubiquitin-specific protease,
USP7/HAUSP.";
J. Biol. Chem. 278:47753-47761(2003).
[7]
AUTOUBIQUITINATION.
PubMed=15247261; DOI=10.1074/jbc.M402885200;
Canning M., Boutell C., Parkinson J., Everett R.D.;
"A RING finger ubiquitin ligase is protected from autocatalyzed
ubiquitination and degradation by binding to ubiquitin-specific
protease USP7.";
J. Biol. Chem. 279:38160-38168(2004).
[8]
FUNCTION, AND INTERACTION WITH HUMAN RCOR1.
PubMed=15897453; DOI=10.1073/pnas.0502658102;
Gu H., Liang Y., Mandel G., Roizman B.;
"Components of the REST/CoREST/histone deacetylase repressor complex
are disrupted, modified, and translocated in HSV-1-infected cells.";
Proc. Natl. Acad. Sci. U.S.A. 102:7571-7576(2005).
[9]
FUNCTION.
PubMed=16160161; DOI=10.1128/JVI.79.19.12342-12354.2005;
Boutell C., Canning M., Orr A., Everett R.D.;
"Reciprocal activities between herpes simplex virus type 1 regulatory
protein ICP0, a ubiquitin E3 ligase, and ubiquitin-specific protease
USP7.";
J. Virol. 79:12342-12354(2005).
[10]
INTERACTION WITH HUMAN USP7, AND DEUBIQUITINATION BY HUMAN USP7.
PubMed=18590780; DOI=10.1016/j.virusres.2008.05.017;
Antrobus R., Boutell C.;
"Identification of a novel higher molecular weight isoform of
USP7/HAUSP that interacts with the Herpes simplex virus type-1
immediate early protein ICP0.";
Virus Res. 137:64-71(2008).
[11]
FUNCTION.
PubMed=20075863; DOI=10.1038/emboj.2009.400;
Lilley C.E., Chaurushiya M.S., Boutell C., Landry S., Suh J.,
Panier S., Everett R.D., Stewart G.S., Durocher D., Weitzman M.D.;
"A viral E3 ligase targets RNF8 and RNF168 to control histone
ubiquitination and DNA damage responses.";
EMBO J. 29:943-955(2010).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20454685; DOI=10.1371/journal.pone.0010428;
Paladino P., Collins S.E., Mossman K.L.;
"Cellular localization of the herpes simplex virus ICP0 protein
dictates its ability to block IRF3-mediated innate immune responses.";
PLoS ONE 5:E10428-E10428(2010).
[13]
FUNCTION.
PubMed=20106921; DOI=10.1128/JVI.02544-09;
Everett R.D., Boutell C., McNair C., Grant L., Orr A.;
"Comparison of the biological and biochemical activities of several
members of the alphaherpesvirus ICP0 family of proteins.";
J. Virol. 84:3476-3487(2010).
[14]
FUNCTION, INTERACTION WITH HUMAN RNF8, PHOSPHORYLATION AT THR-67, AND
MUTAGENESIS OF THR-67.
PubMed=22405594; DOI=10.1016/j.molcel.2012.02.004;
Chaurushiya M.S., Lilley C.E., Aslanian A., Meisenhelder J.,
Scott D.C., Landry S., Ticau S., Boutell C., Yates J.R. III,
Schulman B.A., Hunter T., Weitzman M.D.;
"Viral E3 ubiquitin ligase-mediated degradation of a cellular E3:
viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA
domain.";
Mol. Cell 46:79-90(2012).
[15]
FUNCTION.
PubMed=23027953; DOI=10.1073/pnas.1211302109;
Orzalli M.H., DeLuca N.A., Knipe D.M.;
"Nuclear IFI16 induction of IRF-3 signaling during herpesviral
infection and degradation of IFI16 by the viral ICP0 protein.";
Proc. Natl. Acad. Sci. U.S.A. 109:E3008-E3017(2012).
[16]
INTERACTION WITH HOST TRIM27.
PubMed=25320289; DOI=10.1128/JVI.02635-14;
Conwell S.E., White A.E., Harper J.W., Knipe D.M.;
"Identification of TRIM27 as a novel degradation target of Herpes
Simplex Virus 1 ICP0.";
J. Virol. 89:220-229(2015).
-!- FUNCTION: Evades nuclear antiviral defenses triggered by dsDNA
viruses. Acts during the initial stages of lytic infection and the
reactivation of latent viral genome. Prevents the antiviral effect
of nuclear bodies by degrading host PML and SP100. Prevents
antiviral response to viral DNA induced by IFI16 by degrading it.
Additionally, inhibits host IRF3 nuclear signaling to prevent
interferon production by the infected cells. Interestingly, the E3
ubiquitin ligase activity associated with the RING finger domain
does not seem to be directly required to inhibit the activation of
IRF3 but instead plays a critical role in modulating the cellular
localization of ICP0. Upon reactivation of latent genome,
suppresses the silencing of viral DNA by dissociating either HDAC1
or HDAC2 from the HDAC-RCOR1-REST-KDM1A complex localized at the
ND10 structures and causes their dispersal. Two cellular histone
ubiquitin ligases RNF8 and RNF168 are also targeted by ICP0 for
degradation, leading to a loss of ubiquitinated forms of H2A, a
relief of transcriptional repression, and the activation of latent
viral genomes. Enhances the localization of host CCND3 to ND10
bodies that serve as precursors of replication compartments to
enable efficient viral replication. Like many RING-finger E3
ubiquitin ligases, ICP0 can induce its own ubiquitination, an
activity that promotes its instability due to its targeting to the
26S proteasome for degradation. ICP0 restricts this process by
recruiting the cellular ubiquitin-specific protease USP7 that
cleaves the anchored ubiquitin chains from ICP0, thereby promoting
its stabilization. {ECO:0000269|PubMed:15897453,
ECO:0000269|PubMed:16160161, ECO:0000269|PubMed:20075863,
ECO:0000269|PubMed:20106921, ECO:0000269|PubMed:20454685,
ECO:0000269|PubMed:22405594, ECO:0000269|PubMed:23027953}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBUNIT: Interacts directly with human RCOR1/CoREST protein,
leading to the disruption of the human BHC corepressor complex.
Interacts with human CENPA, leading to its degradation. Interacts
with human USP7; this interaction modulates ICP0 stability.
Interacts with human CDC34. Interacts (when phosphorylated) with
human RNF8 (via FHA domain). Interacts with human TRIM27.
{ECO:0000269|PubMed:11053442, ECO:0000269|PubMed:11447293,
ECO:0000269|PubMed:14506283, ECO:0000269|PubMed:15897453,
ECO:0000269|PubMed:18590780, ECO:0000269|PubMed:22405594,
ECO:0000269|PubMed:25320289}.
-!- INTERACTION:
P30281:CCND3 (xeno); NbExp=3; IntAct=EBI-6148881, EBI-375013;
O15379:HDAC3 (xeno); NbExp=3; IntAct=EBI-6148881, EBI-607682;
P56524:HDAC4 (xeno); NbExp=3; IntAct=EBI-6148881, EBI-308629;
Q9UQL6:HDAC5 (xeno); NbExp=3; IntAct=EBI-6148881, EBI-715576;
Q8WUI4:HDAC7 (xeno); NbExp=3; IntAct=EBI-6148881, EBI-1048378;
Q9UKL0:RCOR1 (xeno); NbExp=2; IntAct=EBI-6148881, EBI-926563;
Q93008:USP9X (xeno); NbExp=3; IntAct=EBI-6148881, EBI-302524;
-!- SUBCELLULAR LOCATION: Host cytoplasm
{ECO:0000269|PubMed:20454685}. Host nucleus
{ECO:0000269|PubMed:20454685}.
-!- PTM: Phosphorylated at Thr-67, leading to promote interaction with
host RNF8. {ECO:0000269|PubMed:22405594}.
-!- PTM: Auto-ubiquitinated. Deubiquitinated by host USP7; leading to
stabilize it. {ECO:0000269|PubMed:15247261,
ECO:0000269|PubMed:18590780}.
-!- SIMILARITY: Belongs to the simplexviruses ICp0 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X14112; CAA32336.1; -; Genomic_DNA.
EMBL; X14112; CAA32293.1; -; Genomic_DNA.
EMBL; X04614; CAA28285.1; -; Genomic_DNA.
PIR; A29152; EDBE11.
RefSeq; YP_009137074.1; NC_001806.2.
RefSeq; YP_009137133.1; NC_001806.2.
PDB; 4WPH; X-ray; 2.92 A; C/D=617-627.
PDB; 4WPI; X-ray; 3.40 A; C/D=617-627.
PDB; 5C56; X-ray; 2.69 A; B=613-633.
PDBsum; 4WPH; -.
PDBsum; 4WPI; -.
PDBsum; 5C56; -.
ProteinModelPortal; P08393; -.
SMR; P08393; -.
BioGrid; 971426; 5.
BioGrid; 971427; 24.
DIP; DIP-42446N; -.
IntAct; P08393; 21.
MINT; MINT-1345075; -.
iPTMnet; P08393; -.
PRIDE; P08393; -.
GeneID; 2703389; -.
GeneID; 2703390; -.
KEGG; vg:2703389; -.
KEGG; vg:2703390; -.
KO; K19436; -.
OrthoDB; VOG09000091; -.
Proteomes; UP000009294; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; NAS:UniProtKB.
GO; GO:0019033; C:viral tegument; IDA:CACAO.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:AgBase.
GO; GO:0075342; P:disruption by symbiont of host cell PML body; IDA:UniProtKB.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0045732; P:positive regulation of protein catabolic process; TAS:AgBase.
GO; GO:0000209; P:protein polyubiquitination; IDA:AgBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019046; P:release from viral latency; TAS:AgBase.
GO; GO:0034340; P:response to type I interferon; IDA:BHF-UCL.
GO; GO:0039593; P:suppression by virus of host exit from mitosis; IEA:UniProtKB-KW.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00097; zf-C3HC4; 1.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; DNA-binding;
Early protein; Host cytoplasm; Host nucleus; Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host IRF3 by virus;
Inhibition of host mitotic exit by virus;
Inhibition of host RLR pathway by virus; Metal-binding;
Modulation of host cell cycle by virus;
Modulation of host ubiquitin pathway by viral E3 ligase;
Modulation of host ubiquitin pathway by virus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Ubl conjugation pathway;
Viral immunoevasion; Viral latency; Viral reactivation from latency;
Zinc; Zinc-finger.
CHAIN 1 775 E3 ubiquitin-protein ligase ICP0.
/FTId=PRO_0000056352.
ZN_FING 116 157 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COMPBIAS 233 243 Poly-Asp.
COMPBIAS 305 308 Poly-Gly.
COMPBIAS 558 568 Poly-Ser.
MOD_RES 67 67 Phosphothreonine; by host; by CK1.
{ECO:0000269|PubMed:22405594}.
MUTAGEN 67 67 T->A: Abolishes interaction host RNF8.
{ECO:0000269|PubMed:22405594}.
SEQUENCE 775 AA; 78457 MW; DF38A1C539DAB15C CRC64;
MEPRPGASTR RPEGRPQREP APDVWVFPCD RDLPDSSDSE AETEVGGRGD ADHHDDDSAS
EADSTDTELF ETGLLGPQGV DGGAVSGGSP PREEDPGSCG GAPPREDGGS DEGDVCAVCT
DEIAPHLRCD TFPCMHRFCI PCMKTWMQLR NTCPLCNAKL VYLIVGVTPS GSFSTIPIVN
DPQTRMEAEE AVRAGTAVDF IWTGNQRFAP RYLTLGGHTV RALSPTHPEP TTDEDDDDLD
DADYVPPAPR RTPRAPPRRG AAAPPVTGGA SHAAPQPAAA RTAPPSAPIG PHGSSNTNTT
TNSSGGGGSR QSRAAAPRGA SGPSGGVGVG VGVVEAEAGR PRGRTGPLVN RPAPLANNRD
PIVISDSPPA SPHRPPAAPM PGSAPRPGPP ASAAASGPAR PRAAVAPCVR APPPGPGPRA
PAPGAEPAAR PADARRVPQS HSSLAQAANQ EQSLCRARAT VARGSGGPGV EGGHGPSRGA
APSGAAPLPS AASVEQEAAV RPRKRRGSGQ ENPSPQSTRP PLAPAGAKRA ATHPPSDSGP
GGRGQGGPGT PLTSSAASAS SSSASSSSAP TPAGAASSAA GAASSSASAS SGGAVGALGG
RQEETSLGPR AASGPRGPRK CARKTRHAET SGAVPAGGLT RYLPISGVSS VVALSPYVNK
TITGDCLPIL DMETGNIGAY VVLVDQTGNM ATRLRAAVPG WSRRTLLPET AGNHVMPPEY
PTAPASEWNS LWMTPVGNML FDQGTLVGAL DFRSLRSRHP WSGEQGASTR DEGKQ


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