ICP27_HCMVM
ID ICP27_HCMVM Reviewed; 742 AA.
AC Q6SW73; D2K3M6;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=mRNA export factor ICP27 homolog;
GN ORFNames=UL69;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND MULTIMERIZATION.
RX PubMed=17251556; DOI=10.1099/vir.0.82480-0;
RA Lischka P., Thomas M., Toth Z., Mueller R., Stamminger T.;
RT "Multimerization of human cytomegalovirus regulatory protein UL69 via a
RT domain that is conserved within its herpesvirus homologues.";
RL J. Gen. Virol. 88:405-410(2007).
CC -!- FUNCTION: Immediate early (EI) protein that plays many roles during
CC productive infection including regulation of host cell cycle
CC progression, regulation of viral gene expression or nuclear export of
CC intronless viral RNAs. Acts as a transcriptional transactivator via
CC interaction with the cellular transcription elongation factor SUPT6H
CC and as a nuclear RNA export factor via interaction with UAP56, a
CC component of the cellular mRNA export machinery (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Self-associates and forms high-molecular-mass complexes.
CC Interacts with host DDX39A and DDX39B; these interactions are required
CC for UL69 function in mRNA export. Interacts with host SUPT6H, EIF4A1
CC AND PABPC1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250}. Virion
CC {ECO:0000250}. Host nucleus {ECO:0000269|PubMed:17251556}. Host
CC cytoplasm {ECO:0000269|PubMed:17251556}. Note=Shuttles between host
CC nucleus and cytoplasm.
CC -!- PTM: Phosphorylated by UL97 and host CDK1, CDK7 and CD9.
CC Phosphorylation by CDKs impacts on UL69 nuclear localization and
CC activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
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DR EMBL; AY446894; AAR31623.1; -; Genomic_DNA.
DR RefSeq; YP_081517.1; NC_006273.2.
DR PRIDE; Q6SW73; -.
DR GeneID; 3077554; -.
DR KEGG; vg:3077554; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0072517; C:host cell viral assembly compartment; TAS:Reactome.
DR GO; GO:0019033; C:viral tegument; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR008648; ICP27-like.
DR Pfam; PF05459; Herpes_UL69; 1.
PE 3: Inferred from homology;
KW G1/S host cell cycle checkpoint dysregulation by virus; Host cytoplasm;
KW Host nucleus; Host-virus interaction; Metal-binding;
KW Modulation of host cell cycle by virus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Virion; Virion tegument; Zinc;
KW Zinc-finger.
FT CHAIN 1..742
FT /note="mRNA export factor ICP27 homolog"
FT /id="PRO_0000416711"
FT ZN_FING 387..501
FT /note="CHC2-type"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT REGION 1..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 494
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
SQ SEQUENCE 742 AA; 82397 MW; D6CF0E47B935A672 CRC64;
MELHSRGRHD APSLSSLSER ERRARRARRF CLDYEPVPRK FRRERSPTSP STRNGAAASE
YHLAEDTVGA ASHHHRPCVP ARRPRYSKDD DTEGDPDHYP PPLPPSSRHA LGGTGGHIIM
GTAGFRGGHR ASSSFKRRVA ASASVPLNPH YGKSYDNDDG EPHHHGGDST HLRRRVPSCP
TTFGSSHPSS ANNHHGSSAG PQQQQMLALI DDELDAMDED ELQQLSRLIE KKKRARLQRG
AASSGTSPSS TSPVYDLQRY TAESLRLAPY PADLKVPTAF PQDHQPRGRI LLSHDELMHT
DYLLHIRQQF DWLEEPLLRK LVVEKIFAVY NAPNLHTLLA IIDETLSYMK YHHLHGLPVN
PHDPYLETVG GMRQLLFNKL NNLDLGCILD HQDGWGDHCS TLKRLVKKPG QMSAWLRDDV
CDLQKRPPET FSQPMHRAMA YVCSFSRVAV SLRRRALQVT GTPQFFDQFD TNNAMGTYRC
GAVSDLILGA LQCHECQNEM CELRIQRALA PYRFMIAYCP FDEQSLLDLT VFAGTTTTTA
SNHATAGGQQ RGGDQIHPTD EQCASMESRT DPATLTAYDK KDREGSHRHP SPMIAAAAPP
AQPPSQPQQH YSEGELEEDE DSDDASSQDL VRATDRHGDT VVYKTTAVPP SPPAPLAGVR
SHRGELNLMT PSPSHGGSPP QVPHKQPIIP VQSANGNHST TATQQQQPPP PPPVPQEDDS
VVMRCQTPDY EDMLCYSDDM DD
