ID   ICP27_SUHVK             Reviewed;         361 AA.
AC   Q85232;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=mRNA export factor ICP27 homolog;
DE   AltName: Full=Protein UL54;
GN   ORFNames=UL54;
OS   Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS   Kaplan)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=33703;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7637001; DOI=10.1128/jvi.69.9.5560-5567.1995;
RA   Baumeister J., Klupp B.G., Mettenleiter T.C.;
RT   "Pseudorabies virus and equine herpesvirus 1 share a nonessential gene
RT   which is absent in other herpesviruses and located adjacent to a highly
RT   conserved gene cluster.";
RL   J. Virol. 69:5560-5567(1995).
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.
CC       {ECO:0000250}.
CC   -!- DOMAIN: Binds viral intronless RNAs and SR proteins through the Arg-
CC       rich region. {ECO:0000250}.
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; X87246; CAA60694.1; -; Genomic_DNA.
DR   SMR; Q85232; -.
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..361
FT                   /note="mRNA export factor ICP27 homolog"
FT                   /id="PRO_0000115834"
FT   ZN_FING         253..337
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..54
FT                   /note="RGG-box"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        14..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..61
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
SQ   SEQUENCE   361 AA;  40451 MW;  44887399D2224B70 CRC64;
     MEDSGNSSGS EASRSGSEER RPVRERLGSR PPERRPVRAR LGAIRRRRGG RGGRAARQAL
     RQRRRQQQQQ QRQQQHQRRR QEADRPDGGP DAPPDRLSES ARAAVSATHA RVGATRVNEL
     FASARHDLSR PVFNDGFRAA GSSPWAAVLE FGAEQFTPDG RRVTWETLMF HGADLHRLFE
     VRPHATEAAR VLREMVLLNE GLTESLASAD ETLTWVKLIL TKGLTLRTLD PIVATAGAVL
     QNLRLKLGPF LRCYLRDTPV DELVRRRRLR DVRCIVTYTL VMLARIARVV ERGSSCVLPE
     DLGDSPVPLE EYVPGACLGG IMDALDSHKT GCDAPTCRLT CSYTLVPVYM HGKYFYCNHL
     F