ICP27_EBVB9
ID ICP27_EBVB9 Reviewed; 479 AA.
AC Q04360; Q777F7; Q8AZJ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 88.
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 B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP INTERACTION WITH HUMAN XPO1.
RX PubMed=10400785; DOI=10.1128/jvi.73.8.6872-6881.1999;
RA Boyle S.M., Ruvolo V., Gupta A.K., Swaminathan S.;
RT "Association with the cellular export receptor CRM 1 mediates function and
RT intracellular localization of Epstein-Barr virus SM protein, a regulator of
RT gene expression.";
RL J. Virol. 73:6872-6881(1999).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=10846090; DOI=10.1128/jvi.74.13.6068-6076.2000;
RA Farjot G., Buisson M., Duc Dodon M., Gazzolo L., Sergeant A., Mikaelian I.;
RT "Epstein-Barr virus EB2 protein exports unspliced RNA via a Crm-1-
RT independent pathway.";
RL J. Virol. 74:6068-6076(2000).
RN [4]
RP RNA-BINDING.
RX PubMed=11390605; DOI=10.1128/jvi.75.13.6033-6041.2001;
RA Ruvolo V., Gupta A.K., Swaminathan S.;
RT "Epstein-Barr virus SM protein interacts with mRNA in vivo and mediates a
RT gene-specific increase in cytoplasmic mRNA.";
RL J. Virol. 75:6033-6041(2001).
RN [5]
RP INTERACTION WITH HUMAN REF.
RX PubMed=12403791; DOI=10.1074/jbc.m208656200;
RA Hiriart E., Farjot G., Gruffat H., Nguyen M.V., Sergeant A., Manet E.;
RT "A novel nuclear export signal and a REF interaction domain both promote
RT mRNA export by the Epstein-Barr virus EB2 protein.";
RL J. Biol. Chem. 278:335-342(2003).
RN [6]
RP INTERACTION WITH HUMAN SPEN; OTT1 AND OTT3.
RX PubMed=16129689; DOI=10.1074/jbc.m501725200;
RA Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S., Meresse P.,
RA Mercher T., Bernard O.A., Sergeant A., Manet E.;
RT "Interaction of the Epstein-Barr virus mRNA export factor EB2 with human
RT Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links
RT Spen proteins with splicing regulation and mRNA export.";
RL J. Biol. Chem. 280:36935-36945(2005).
RN [7]
RP PHOSPHORYLATION BY HUMAN CK2.
RX PubMed=17699575; DOI=10.1128/jvi.01421-07;
RA Medina-Palazon C., Gruffat H., Mure F., Filhol O., Vingtdeux-Didier V.,
RA Drobecq H., Cochet C., Sergeant N., Sergeant A., Manet E.;
RT "Protein kinase CK2 phosphorylation of EB2 regulates its function in the
RT production of Epstein-Barr virus infectious viral particles.";
RL J. Virol. 81:11850-11860(2007).
RN [8]
RP FUNCTION IN ALTERNATIVE SPLICING.
RX PubMed=18463151; DOI=10.1128/jvi.00344-08;
RA Verma D., Swaminathan S.;
RT "Epstein-Barr virus SM protein functions as an alternative splicing
RT factor.";
RL J. Virol. 82:7180-7188(2008).
RN [9]
RP FUNCTION.
RX PubMed=19793817; DOI=10.1128/jvi.01276-09;
RA Juillard F., Hiriart E., Sergeant N., Vingtdeux-Didier V., Drobecq H.,
RA Sergeant A., Manet E., Gruffat H.;
RT "Epstein-Barr virus protein EB2 contains an N-terminal transferable nuclear
RT export signal that promotes nucleocytoplasmic export by directly binding
RT TAP/NXF1.";
RL J. Virol. 83:12759-12768(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH HUMAN SRSF1; SRSF3; SRSF7 AND SRPK1.
RX PubMed=22505578; DOI=10.1093/nar/gks319;
RA Juillard F., Bazot Q., Mure F., Tafforeau L., Macri C., Rabourdin-Combe C.,
RA Lotteau V., Manet E., Gruffat H.;
RT "Epstein-Barr virus protein EB2 stimulates cytoplasmic mRNA accumulation by
RT counteracting the deleterious effects of SRp20 on viral mRNAs.";
RL Nucleic Acids Res. 40:6834-6849(2012).
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. {ECO:0000269|PubMed:18463151, ECO:0000269|PubMed:19793817,
CC ECO:0000269|PubMed:22505578}.
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. {ECO:0000269|PubMed:10400785,
CC ECO:0000269|PubMed:12403791, ECO:0000269|PubMed:16129689,
CC ECO:0000269|PubMed:22505578}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:10846090}. Host
CC cytoplasm {ECO:0000269|PubMed:10846090}. Note=shuttles between the
CC nucleus and the cytoplasm.
CC -!- PTM: Phosphorylated by cellular protein kinase CK2.
CC {ECO:0000269|PubMed:17699575}.
CC -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24846.1; 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=CAD53409.1; 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; V01555; CAA24846.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ507799; CAD53409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ507799; CAD53410.1; -; Genomic_DNA.
DR PIR; S33000; S33000.
DR RefSeq; YP_401659.1; NC_007605.1.
DR RefSeq; YP_401660.1; NC_007605.1.
DR SMR; Q04360; -.
DR IntAct; Q04360; 10.
DR MINT; Q04360; -.
DR PRIDE; Q04360; -.
DR GeneID; 3783758; -.
DR KEGG; vg:3783758; -.
DR Proteomes; UP000153037; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044095; C:host cell nucleoplasm; IDA:UniProtKB.
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 Early protein; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host PKR by virus; Interferon antiviral system evasion;
KW Metal-binding; mRNA transport; Phosphoprotein; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation; Transport;
KW Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..479
FT /note="mRNA export factor ICP27 homolog"
FT /id="PRO_0000115833"
FT ZN_FING 354..454
FT /note="CHC2-type"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..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 91..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; 53492 MW; D83E6DFE09EC7B5A CRC64;
MVPSQRLSRT SSISSNEDPA ESHILELEAV SDTNTDCDLD PMEGSEEHST DGEISSSEEE
DEDPTPAHAI PARPSSVVIT 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 ILSPGTGSLG LFFVPGLNQ
