ICP27_HHV1E
ID ICP27_HHV1E Reviewed; 511 AA.
AC P36295;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=mRNA export factor;
DE AltName: Full=Immediate-early protein IE63;
DE AltName: Full=Infected cell protein 27;
DE Short=ICP27;
GN ORFNames=UL54;
OS Human herpesvirus 1 (strain HFEM) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10303;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1332274; DOI=10.1016/0168-1702(92)90133-t;
RA Rosen-Wolff A., Frank S., Raab K., Moyal M., Becker Y., Darai G.;
RT "Determination of the coding capacity of the BamHI DNA fragment B of
RT apathogenic Herpes simplex virus type 1 strain HFEM by DNA nucleotide
RT sequence analysis.";
RL Virus Res. 25:189-199(1992).
CC -!- FUNCTION: Multifunctional regulator of the expression of viral genes
CC that contributes to the shutoff of host protein synthesis and mediates
CC nuclear export of viral intronless mRNAs. Early in infection, this
CC immediate early (EI) protein mediates the inhibition of cellular
CC splicing. This results in the accumulation of unprocessed 3'end pre-
CC mRNAs which can't be exported from the nucleus. Cellular protein
CC synthesis is thereby shut off early after virus infection. Later in the
CC infection, it helps recruit cellular RNA polymerase II to viral
CC replication sites and promotes the nuclear export of viral intronless
CC mRNAs by interacting with mRNAs and host NXF1/TAP. ICP27 binds to NUP62
CC which may provide facilitated viral mRNA export and may compete with
CC some host cell transport receptors for binding and inhibit cellular
CC nucleocytoplasmic transport pathways. Also stimulates translation of
CC viral transcripts. Repression of host gene expression blocks the cell
CC cycle at the G1 phase and prevents apoptosis. Seems to silence the 3'
CC splice site of the promyelocytic leukemia (PML) intron 7a, thereby
CC switching PML isoforms from PML-II to PML-V. This could be linked to
CC the accelerated mRNA export induced by ICP27 which might not provide
CC sufficient time for PML pre-mRNA to be spliced in the nucleus (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host RBP1; this interaction facilitates the RNA
CC polymerase recruitment to viral transcription sites. Interacts (via the
CC RGG box) with host ALYREF/THOC4; this interaction recruits ALYREF to
CC viral replication compartments and probably directs viral mRNA to the
CC TAP/NFX1 pathway. Interacts (via the RGG box) with host SRPK1; this
CC interaction relocalizes SRPK1 to the nucleus and seems to alter its
CC activity. Interacts with ICP4; this interaction modulates ICP4 DNA-
CC binding activity. Interacts with host NXF1; this interaction allows
CC efficient export of HSV-1 early and late transcripts (By similarity).
CC {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 through the RGG region.
CC {ECO:0000250}.
CC -!- PTM: Methylated within the RGG box possibly by host PRMT1. When
CC hypomethylated, ICP27 is exported to the cytoplasm earlier and more
CC rapidly (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
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DR EMBL; M90438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A48560; A48560.
DR PDB; 6FAD; X-ray; 2.80 A; E/F/G/H=137-152.
DR PDBsum; 6FAD; -.
DR BMRB; P36295; -.
DR SMR; P36295; -.
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:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039524; P:suppression by virus of host mRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR031752; HHV-1_REF-bd.
DR InterPro; IPR008648; ICP27-like.
DR Pfam; PF05459; Herpes_UL69; 1.
DR Pfam; PF16852; HHV-1_VABD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host NF-kappa-B by virus; Activator;
KW Early protein; Eukaryotic host gene expression shutoff by virus;
KW G1/S host cell cycle checkpoint dysregulation by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host mRNA suppression by virus;
KW Host nucleus; Host-virus interaction;
KW Inhibition of host pre-mRNA processing by virus; Metal-binding;
KW Methylation; Modulation of host cell cycle by virus; Phosphoprotein;
KW RNA-binding; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..511
FT /note="mRNA export factor"
FT /id="PRO_0000115824"
FT ZN_FING 399..487
FT /note="CHC2-type"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT REGION 1..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..112
FT /note="Interaction with host ALYREF"
FT /evidence="ECO:0000250"
FT REGION 138..152
FT /note="RGG-box"
FT /evidence="ECO:0000250"
FT MOTIF 5..17
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 110..138
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 487
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT MOD_RES 16
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 114
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 138
FT /note="Dimethylated arginine; by host"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT MOD_RES 148
FT /note="Omega-N-methylarginine; by host"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT MOD_RES 150
FT /note="Dimethylated arginine; by host"
FT /evidence="ECO:0000250|UniProtKB:P10238"
SQ SEQUENCE 511 AA; 55143 MW; 7BE7A8F841A98174 CRC64;
MATDIDMLID LGLDLSDSDL DEDPPEPAES RRDDLESDSS GECSSSDEDM EDPHGEDGPE
PILDAARPAV RPSRPEDPGV PSTQTPRPTE RQGPNDPQPA PHSVWSRLGA RRPSCSPEQH
GGKVARLQPP PTKAQPARGG RRGRRRGRGR GGPGAADGLS DPRRRAPRTN RNPGDRPGAG
WTDGPGAPHG EAWRGSEQPD PPGGPRTRGV RQAPPPLMTL AIAPPPADPR APAPERKAPA
ADTIDATTRL VLRSISERAA VDRISESFGR SAQVMPDPFG GQPFPAANSP WAPVLAGQGG
PFDAETRRVS WETLVAHGPS LYRTFAGNPR AASTAKAMRD CVLRQENFIE ALASADETLA
WCKMCIHHNL PLRPQDPIIG TTAAVLDNLA TRLRPFLQCY LKARGLCGLD ELCSRRRLAD
IKDIASFVFV ILARLANRVE RGVAEIDYAT LGVGVGEKMH FYLPGACMAG LIEILDTHRQ
ECSSRVCELT ASHIVAPPYV HGKYFYCNSL F
