ICP27_EBVG
ID ICP27_EBVG Reviewed; 479 AA.
AC Q3KSU1; Q3KSU0;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=mRNA export factor ICP27 homolog;
DE AltName: Full=Mta;
DE AltName: Full=ORF57 protein homolog;
DE AltName: Full=Protein SM;
GN ORFNames=BMLF1;
GN and
GN ORFNames=BSLF2;
OS Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10376;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT nasopharyngeal carcinoma patient.";
RL J. Virol. 79:15323-15330(2005).
CC -!- FUNCTION: Promotes the nuclear export of a subset of early and late
CC viral mRNAs by interacting with mRNAs and cellular export proteins.
CC Additionally may prevent the establishment of cellular antiviral state,
CC by acting as an alternative splicing factor for cellular RNAs such as
CC STAT1, resulting in a STAT1 mRNA incapable of producing the STAT1alpha
CC isoform (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host XPO1 and with the XPO1 export pathway
CC components small GTPase RAN and nucleoporin NUP214. Interacts with host
CC SPEN, OTT1 and OTT3 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q3KSU1; Q3KSU1: BMLF1; NbExp=2; IntAct=EBI-2621113, EBI-2621113;
CC -!- SUBCELLULAR LOCATION: Host nucleus. Host cytoplasm. Note=shuttles
CC between the nucleus and the cytoplasm. {ECO:0000250}.
CC -!- PTM: Phosphorylated by cellular protein kinase CK2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY41109.1; Type=Erroneous gene model prediction; Note=Produced from a longuer mRNA than expected which is spliced so that BSFL2 and BMLF1 ORFs are fused.; Evidence={ECO:0000305};
CC Sequence=AAY41110.1; Type=Erroneous gene model prediction; Note=Produced from a longuer mRNA than expected which is spliced so that BSFL2 and BMLF1 ORFs are fused.; Evidence={ECO:0000305};
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DR EMBL; AY961628; AAY41109.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY961628; AAY41110.1; ALT_SEQ; Genomic_DNA.
DR PDB; 3MRE; X-ray; 1.10 A; P=300-308.
DR PDB; 3MRF; X-ray; 2.30 A; P=300-308.
DR PDB; 3O4L; X-ray; 2.54 A; C=300-308.
DR PDBsum; 3MRE; -.
DR PDBsum; 3MRF; -.
DR PDBsum; 3O4L; -.
DR SMR; Q3KSU1; -.
DR IntAct; Q3KSU1; 3.
DR EvolutionaryTrace; Q3KSU1; -.
DR Proteomes; UP000007641; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR008648; ICP27-like.
DR Pfam; PF05459; Herpes_UL69; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Early protein; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host PKR by virus; Metal-binding; mRNA transport;
KW Phosphoprotein; RNA-binding; Transcription; Transcription regulation;
KW Transport; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..479
FT /note="mRNA export factor ICP27 homolog"
FT /id="PRO_0000375954"
FT ZN_FING 354..454
FT /note="CHC2-type"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..210
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 92..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
SQ SEQUENCE 479 AA; 53482 MW; 40F10905F1C5507A CRC64;
MVPSQRLSRT SSISSNEDPA ESHILELEAV SDTNTDCDMD PMEGSEEHST DGEISSSEEE
DEDPTPAHAV PAQPSSVVIT PTSASFVIPR KKWDLQDKTV TLHRSPLCRD EDEKEETGNS
SYTRGHKRRR GEVHGCTDES YGKRRHLPPG ARAPRAPRAP RVPRAPRSPR APRSNRATRG
PRSESRGAGR STRKQARQER SQRPLPNKPW FDMSLVKPVS KITFVTLPSP LASLTLEPIQ
DPFLQSMLAV AAHPEIGAWQ KVQPRHELRR SYKTLREFFT KSTNKDTWLD ARMQAIQNAG
LCTLVAMLEE TIFWLQEITY HGDLPLAPAE DILLACAMSL SKVILTKLKE LAPCFLPNTR
DYNFVKQLFY ITCATARQNK VVETLSSSYV KQPLCLLAAY AAVAPAYINA NCRRRHDEVE
FLGHYIKNYN PGTLSSLLTE AVETHTRDCR SASCSRLVRA ILSPATGSLG LFFVPGLNQ
