ID ICP27_VZVD Reviewed; 452 AA. AC P09269; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 12-AUG-2020, entry version 76. DE RecName: Full=mRNA export factor ICP27 homolog; DE AltName: Full=Immediate-early protein 4; DE Short=IE4; DE AltName: Full=Transcriptional transactivator IE4; GN ORFNames=ORF4; OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus. OX NCBI_TaxID=10338; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759; RA Davison A.J., Scott J.E.; RT "The complete DNA sequence of varicella-zoster virus."; RL J. Gen. Virol. 67:1759-1816(1986). RN [2] RP FUNCTION. RX PubMed=9261438; RA Defechereux P., Debrus S., Baudoux L., Rentier B., Piette J.; RT "Varicella-zoster virus open reading frame 4 encodes an immediate-early RT protein with posttranscriptional regulatory properties."; RL J. Virol. 71:7073-7079(1997). RN [3] RP INTERACTION WITH IE62. RX PubMed=10873781; DOI=10.1006/viro.2000.0389; RA Spengler M.L., Ruyechan W.T., Hay J.; RT "Physical interaction between two varicella zoster virus gene regulatory RT proteins, IE4 and IE62."; RL Virology 272:375-381(2000). RN [4] RP SUBUNIT. RX PubMed=10889190; DOI=10.1074/jbc.m001444200; RA Baudoux L., Defechereux P., Rentier B., Piette J.; RT "Gene activation by Varicella-zoster virus IE4 protein requires its RT dimerization and involves both the arginine-rich sequence, the central RT part, and the carboxyl-terminal cysteine-rich region."; RL J. Biol. Chem. 275:32822-32831(2000). RN [5] RP FUNCTION, AND INTERACTION WITH HUMAN SRSF1; SRSF3; SRSF7 AND SRPK1. RC STRAIN=NIK; RX PubMed=19924249; DOI=10.1371/journal.pone.0007882; RA Ote I., Lebrun M., Vandevenne P., Bontems S., Medina-Palazon C., Manet E., RA Piette J., Sadzot-Delvaux C.; RT "Varicella-zoster virus IE4 protein interacts with SR proteins and exports RT mRNAs through the TAP/NXF1 pathway."; RL PLoS ONE 4:E7882-E7882(2009). 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, ECO:0000269|PubMed:19924249, ECO:0000269|PubMed:9261438}. 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. {ECO:0000269|PubMed:10873781, CC ECO:0000269|PubMed:10889190, ECO:0000269|PubMed:19924249}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host nucleus CC {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm CC (Probable). IE4 utilizes, at least, XPO1/CRM1 as a cofactor for nuclear CC export. {ECO:0000305}. CC -!- DOMAIN: Binds viral intronless RNAs and SR proteins through the Arg- CC rich region. CC -!- PTM: Phosphorylated in vitro by SRPK1. CC -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04370; CAA27887.1; -; Genomic_DNA. DR PIR; D27212; WZBE4. DR SMR; P09269; -. DR PRIDE; P09269; -. DR Proteomes; UP000002602; 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 GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR InterPro; IPR008648; ICP27-like. DR Pfam; PF05459; Herpes_UL69; 1. PE 1: Evidence at protein level; KW Activator; Early protein; Host cytoplasm; Host nucleus; KW Host-virus interaction; Metal-binding; Reference proteome; RNA-binding; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..452 FT /note="mRNA export factor ICP27 homolog" FT /id="PRO_0000115831" FT ZN_FING 335..426 FT /note="CHC2-type" FT /evidence="ECO:0000250|UniProtKB:P10238" FT COMPBIAS 71..143 FT /note="Arg-rich" FT COMPBIAS 405..452 FT /note="Cys-rich" FT METAL 335 FT /note="Zinc" FT /evidence="ECO:0000250|UniProtKB:P10238" FT METAL 417 FT /note="Zinc" FT /evidence="ECO:0000250|UniProtKB:P10238" FT METAL 421 FT /note="Zinc" FT /evidence="ECO:0000250|UniProtKB:P10238" FT METAL 426 FT /note="Zinc" 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 //