ICP27_VZVO
ID ICP27_VZVO Reviewed; 452 AA.
AC Q4JQX1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=mRNA export factor ICP27 homolog;
DE AltName: Full=Immediate-early protein 4;
DE Short=IE4;
GN ORFNames=ORF4;
OS Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=341980;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT its parental virus.";
RL J. Virol. 76:11447-11459(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC Oka varicella vaccine Varivax V-Oka-Merk);
RX PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA Vassilev V.;
RT "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL J. Virol. 82:11023-11044(2008).
CC -!- FUNCTION: Multifunctional regulator of the expression of viral genes
CC that mediates nuclear export of viral intronless mRNAs. This immediate
CC early (EI) protein promotes the nuclear export of viral intronless
CC mRNAs by interacting with mRNAs and host NXF1/TAP (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Homodimerization is required for transactivation.
CC Associates in a complex with RNA, and host export factors NXF1/TAP and
CC ALYREF; these interactions allow nuclear export of viral transcripts.
CC Interacts with three host shuttling SR proteins SRSF1, SRSF3 and SRSF7.
CC Interacts with host SRPK1. Interacts with IE62; this interaction
CC enhances IE62 transactivation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host nucleus
CC {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. IE4
CC utilizes, at least, XPO1/CRM1 as a cofactor for nuclear export (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Binds viral intronless RNAs and SR proteins through the Arg-
CC rich region. {ECO:0000250}.
CC -!- PTM: Phosphorylated in vitro by SRPK1.
CC -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
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DR EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57623.1; -; Genomic_DNA.
DR EMBL; DQ008355; AAY57694.1; -; Genomic_DNA.
DR RefSeq; NP_040127.1; NC_001348.1.
DR SMR; Q4JQX1; -.
DR IntAct; Q4JQX1; 7.
DR GeneID; 1487672; -.
DR KEGG; vg:1487672; -.
DR Proteomes; UP000002603; Genome.
DR Proteomes; UP000008504; Genome.
DR Proteomes; UP000008505; Genome.
DR Proteomes; UP000008506; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; 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 Activator; Early protein; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Metal-binding; RNA-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..452
FT /note="mRNA export factor ICP27 homolog"
FT /id="PRO_0000385464"
FT ZN_FING 335..426
FT /note="CHC2-type"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT REGION 42..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
SQ SEQUENCE 452 AA; 51543 MW; 42926E4A71E380B4 CRC64;
MASASIPTDP DVSTICEDFM NLLPDEPSDD FALEVTDWAN DEAIGSTPGE DSTTSRTVYV
ERTADTAYNP RYSKRRHGRR ESYHHNRPKT LVVVLPDSNH HGGRDVETGY ARIERGHRRS
SRSYNTQSSR KHRDRSLSNR RRRPTTPPAM TTGERNDQTH DESYRLRFSK RDARRERIRK
EYDIPVDRIT GRAIEVVSTA GASVTIDSVR HLDETIEKLV VRYATIQEGD SWASGGCFPG
IKQNTSWPEL MLYGHELYRT FESYKMDSRI ARALRERVIR GESLIEALES ADELLTWIKM
LAAKNLPIYT NNPIVATSKS LLENLKLKLG PFVRCLLLNR DNDLGSRTLP ELLRQQRFSD
ITCITTYMFV MIARIANIVV RGSKFVEYDD ISCNVQVLQE YTPGSCLAGV LEALITHQRE
CGRVECTLST WAGHLSDARP YGKYFKCSTF NC
