ICP22_HHV11
ID ICP22_HHV11 Reviewed; 420 AA.
AC P04485;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Transcriptional regulator ICP22;
DE AltName: Full=Immediate-early protein IE68;
DE AltName: Full=Infected cell protein 22;
DE Short=ICP22;
GN Name=ICP22; ORFNames=US1;
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 [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].
RX PubMed=2984429; DOI=10.1016/0022-2836(85)90320-1;
RA McGeoch D.J., Dolan A., Donald S., Rixon F.J.;
RT "Sequence determination and genetic content of the short unique region in
RT the genome of herpes simplex virus type 1.";
RL J. Mol. Biol. 181:1-13(1985).
RN [3]
RP PHOSPHORYLATION AT TYR-193, AND MUTAGENESIS OF TYR-193.
RX PubMed=12504549; DOI=10.1006/viro.2002.1746;
RA O'Toole J.M., Aubert M., Kotsakis A., Blaho J.A.;
RT "Mutation of the protein tyrosine kinase consensus site in the herpes
RT simplex virus 1 alpha22 gene alters ICP22 posttranslational modification.";
RL Virology 305:153-167(2003).
RN [4]
RP ISOFORM US1.5.
RX PubMed=15956590; DOI=10.1128/jvi.79.13.8470-8479.2005;
RA Poon A.P., Roizman B.;
RT "Herpes simplex virus 1 ICP22 regulates the accumulation of a shorter mRNA
RT and of a truncated US3 protein kinase that exhibits altered functions.";
RL J. Virol. 79:8470-8479(2005).
RN [5]
RP FUNCTION.
RX PubMed=16571817; DOI=10.1128/jvi.80.8.4005-4016.2006;
RA Orlando J.S., Astor T.L., Rundle S.A., Schaffer P.A.;
RT "The products of the herpes simplex virus type 1 immediate-early US1/US1.5
RT genes downregulate levels of S-phase-specific cyclins and facilitate virus
RT replication in S-phase Vero cells.";
RL J. Virol. 80:4005-4016(2006).
RN [6]
RP FUNCTION.
RX PubMed=17344289; DOI=10.1128/jvi.00184-07;
RA Fraser K.A., Rice S.A.;
RT "Herpes simplex virus immediate-early protein ICP22 triggers loss of serine
RT 2-phosphorylated RNA polymerase II.";
RL J. Virol. 81:5091-5101(2007).
RN [7]
RP FUNCTION, INTERACTION WITH HOST SSRP1 AND SUPT16H, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28611249; DOI=10.1128/mbio.00745-17;
RA Fox H.L., Dembowski J.A., DeLuca N.A.;
RT "A Herpesviral Immediate Early Protein Promotes Transcription Elongation of
RT Viral Transcripts.";
RL MBio 8:0-0(2017).
CC -!- FUNCTION: Functions as a general transcriptional regulator of cellular
CC and viral mRNAs mainly by mediating changes on the host RNA polymerase
CC II. One change, which is UL13 independent, is the rapid loss of Pol II
CC forms bearing Ser-2 phosphorylation. A second change, which is UL13
CC dependent, is the appearance of an intermediate form of Pol II that
CC differs from the normal hypo- and hyperphosphorylated forms. These Pol
CC II modifications immediately inhibit host genome transcription, leading
CC to cell cycle deregulation and loss of efficient antiviral response.
CC Recruits also cellular transcription elongation factors to viral
CC genomes for efficient transcription elongation of viral genes.
CC {ECO:0000269|PubMed:16571817, ECO:0000269|PubMed:17344289}.
CC -!- SUBUNIT: Interacts with host FACT complex members SSRP1 and SUPT16H;
CC these interactions are required for the relocalization of the FACT
CC complex in infected cells and its association with viral genomes.
CC {ECO:0000269|PubMed:28611249}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:28611249}.
CC Note=Localizes in small nuclear bodies early in infection then moves to
CC a more diffuse distribution in viral compartments as infection
CC progresses.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=ICP22;
CC IsoId=P04485-1; Sequence=Displayed;
CC Name=US1.5;
CC IsoId=P04485-2; Sequence=VSP_025673;
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:12504549}.
CC -!- MISCELLANEOUS: ICP22 and protein US1.5 mRNAs are transcribed from two
CC different promoters on the US1 gene.
CC -!- SIMILARITY: Belongs to the herpesviridae ICP22 family. {ECO:0000305}.
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DR EMBL; X14112; CAA32287.1; -; Genomic_DNA.
DR EMBL; X02138; CAA26055.1; -; Genomic_DNA.
DR EMBL; L00036; AAA96687.1; -; Genomic_DNA.
DR PIR; A03723; EDBE17.
DR RefSeq; YP_009137136.1; NC_001806.2.
DR BioGRID; 971458; 5.
DR IntAct; P04485; 1.
DR MINT; P04485; -.
DR iPTMnet; P04485; -.
DR PRIDE; P04485; -.
DR GeneID; 2703435; -.
DR KEGG; vg:2703435; -.
DR Proteomes; UP000009294; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IDA:UniProtKB.
DR InterPro; IPR003403; IE68.
DR Pfam; PF02479; Herpes_IE68; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Early protein;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus;
KW Host gene expression shutoff by virus; Host nucleus;
KW Host-virus interaction; Inhibition of host RNA polymerase II by virus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..420
FT /note="Transcriptional regulator ICP22"
FT /id="PRO_0000115837"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 193
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000305|PubMed:12504549"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform US1.5)"
FT /evidence="ECO:0000305"
FT /id="VSP_025673"
FT MUTAGEN 193
FT /note="Y->A: Alteration of post-translational
FT modifications."
FT /evidence="ECO:0000269|PubMed:12504549"
SQ SEQUENCE 420 AA; 46525 MW; 94D56376545B1192 CRC64;
MADISPGAFA PCVKARRPAL RSPPLGTRKR KRPSRPLSSE SEVESDTALE SEVESETASD
STESGDQDEA PRIGGRRAPR RLGGRFFLDM SAESTTGTET DASVSDDPDD TSDWSYDDIP
PRPKRARVNL RLTSSPDRRD GVIFPKMGRV RSTRETQPRA PTPSAPSPNA MLRRSVRQAQ
RRSSARWTPD LGYMRQCINQ LFRVLRVARD PHGSANRLRH LIRDCYLMGY CRARLAPRTW
CRLLQVSGGT WGMHLRNTIR EVEARFDATA EPVCKLPCLE TRRYGPECDL SNLEIHLSAT
SDDEISDATD LEAAGSDHTL ASQSDTEDAP SPVTLETPEP RGSLAVRLED EFGEFDWTPQ
EGSQPWLSAV VADTSSVERP GPSDSGAGRA AEDRKCLDGC RKMRFSTACP YPCSDTFLRP
