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mRNA export factor (Immediate-early protein IE63) (Infected cell protein 27) (ICP27) (VMW63)

 ICP27_HHV11             Reviewed;         512 AA.
P10238; B9VQI3; Q09I80;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
05-JUL-2017, entry version 99.
RecName: Full=mRNA export factor;
AltName: Full=Immediate-early protein IE63;
AltName: Full=Infected cell protein 27;
Short=ICP27;
AltName: Full=VMW63;
ORFNames=UL54;
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10299;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2846760; DOI=10.1099/0022-1317-69-11-2831;
Perry L.J., McGeoch D.J.;
"The DNA sequences of the long repeat region and adjoining parts of
the long unique region in the genome of herpes simplex virus type 1.";
J. Gen. Virol. 69:2831-2846(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C.,
McNab D., Perry L.J., Scott J.E., Taylor P.;
"The complete DNA sequence of the long unique region in the genome of
herpes simplex virus type 1.";
J. Gen. Virol. 69:1531-1574(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nonneuroinvasive mutant HF10;
PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
"Determination and analysis of the DNA sequence of highly attenuated
herpes simplex virus type 1 mutant HF10, a potential oncolytic
virus.";
Microbes Infect. 9:142-149(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17 syn+;
Cunningham C., Davison A.J.;
"Herpes simplex virus type 1 bacterial artificial chromosome.";
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH ICP4.
PubMed=8995681;
Panagiotidis C.A., Lium E.K., Silverstein S.J.;
"Physical and functional interactions between herpes simplex virus
immediate-early proteins ICP4 and ICP27.";
J. Virol. 71:1547-1557(1997).
[6]
SUBCELLULAR LOCATION.
PubMed=9501050; DOI=10.1006/viro.1997.9006;
Mears W.E., Rice S.A.;
"The herpes simplex virus immediate-early protein ICP27 shuttles
between nucleus and cytoplasm.";
Virology 242:128-137(1998).
[7]
FUNCTION.
PubMed=9512520; DOI=10.1101/gad.12.6.868;
Sandri-Goldin R.M.;
"ICP27 mediates HSV RNA export by shuttling through a leucine-rich
nuclear export signal and binding viral intronless RNAs through an RGG
motif.";
Genes Dev. 12:868-879(1998).
[8]
PHOSPHORYLATION AT SER-16; SER-18 AND SER-114.
PubMed=10074178;
Zhi Y., Sandri-Goldin R.M.;
"Analysis of the phosphorylation sites of herpes simplex virus type 1
regulatory protein ICP27.";
J. Virol. 73:3246-3257(1999).
[9]
FUNCTION.
PubMed=11287586; DOI=10.1128/JVI.75.9.4376-4385.2001;
Bryant H.E., Wadd S.E., Lamond A.I., Silverstein S.J., Clements J.B.;
"Herpes simplex virus IE63 (ICP27) protein interacts with spliceosome-
associated protein 145 and inhibits splicing prior to the first
catalytic step.";
J. Virol. 75:4376-4385(2001).
[10]
INTERACTION WITH HOST ALYREF/THOC4.
PubMed=12438613; DOI=10.1128/JVI.76.24.12877-12889.2002;
Chen I.-H.B., Sciabica K.S., Sandri-Goldin R.M.;
"ICP27 interacts with the RNA export factor Aly/REF to direct herpes
simplex virus type 1 intronless mRNAs to the TAP export pathway.";
J. Virol. 76:12877-12889(2002).
[11]
FUNCTION, AND INTERACTION WITH HOST SRPK1.
PubMed=12660167; DOI=10.1093/emboj/cdg166;
Sciabica K.S., Dai Q.J., Sandri-Goldin R.M.;
"ICP27 interacts with SRPK1 to mediate HSV splicing inhibition by
altering SR protein phosphorylation.";
EMBO J. 22:1608-1619(2003).
[12]
FUNCTION.
PubMed=16537625; DOI=10.1128/JVI.80.7.3567-3581.2006;
Dai-Ju J.Q., Li L., Johnson L.A., Sandri-Goldin R.M.;
"ICP27 interacts with the C-terminal domain of RNA polymerase II and
facilitates its recruitment to herpes simplex virus 1 transcription
sites, where it undergoes proteasomal degradation during infection.";
J. Virol. 80:3567-3581(2006).
[13]
REVIEW.
PubMed=18508584; DOI=10.2741/3078;
Sandri-Goldin R.M.;
"The many roles of the regulatory protein ICP27 during herpes simplex
virus infection.";
Front. Biosci. 13:5241-5256(2008).
[14]
METHYLATION AT ARG-138; ARG-148 AND ARG-150.
PubMed=19321610; DOI=10.1128/JVI.00238-09;
Souki S.K., Gershon P.D., Sandri-Goldin R.M.;
"Arginine methylation of the ICP27 RGG box regulates ICP27 export and
is required for efficient herpes simplex virus 1 replication.";
J. Virol. 83:5309-5320(2009).
[15]
INTERACTION WITH HOST SRPK1, AND FUNCTION.
PubMed=19553338; DOI=10.1128/JVI.00801-09;
Souki S.K., Sandri-Goldin R.M.;
"Arginine methylation of the ICP27 RGG box regulates the functional
interactions of ICP27 with SRPK1 and Aly/REF during herpes simplex
virus 1 infection.";
J. Virol. 83:8970-8975(2009).
[16]
INTERACTION WITH HOST NXF1, AND FUNCTION.
PubMed=19369354; DOI=10.1128/JVI.00375-09;
Johnson L.A., Li L., Sandri-Goldin R.M.;
"The cellular RNA export receptor TAP/NXF1 is required for ICP27-
mediated export of herpes simplex virus 1 RNA, but the TREX complex
adaptor protein Aly/REF appears to be dispensable.";
J. Virol. 83:6335-6346(2009).
[17]
INTERACTION WITH HOST NUP62, AND FUNCTION.
PubMed=22334672; DOI=10.1074/jbc.M111.331777;
Malik P., Tabarraei A., Kehlenbach R.H., Korfali N., Iwasawa R.,
Graham S.V., Schirmer E.C.;
"Herpes simplex virus ICP27 protein directly interacts with the
nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic
transport pathways.";
J. Biol. Chem. 287:12277-12292(2012).
[18]
STRUCTURE BY NMR OF 103-138 IN COMPLEX WITH ALYREF2, AND INTERACTION
WITH HOST ALYREF AND ALYREF2.
PubMed=21253573; DOI=10.1371/journal.ppat.1001244;
Tunnicliffe R.B., Hautbergue G.M., Kalra P., Jackson B.R.,
Whitehouse A., Wilson S.A., Golovanov A.P.;
"Structural basis for the recognition of cellular mRNA export factor
REF by herpes viral proteins HSV-1 ICP27 and HVS ORF57.";
PLoS Pathog. 7:E1001244-E1001244(2011).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 190-512 IN COMPLEX WITH ZINC
IONS, SUBUNIT, AND DOMAIN.
PubMed=26085142; DOI=10.1128/JVI.00441-15;
Patel V., Dahlroth S.L., Rajakannan V., Ho H.T., Cornvik T.,
Nordlund P.;
"Structure of C-Terminal Domain of the Multifunctional ICP27 Protein
from Herpes Simplex Virus-1.";
J. Virol. 89:8828-8839(2015).
[20]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 241-512 IN COMPLEX WITH ZINC
IONS, SUBUNIT, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
500-TYR--PHE-512.
PubMed=26062451; DOI=10.1038/srep11234;
Tunnicliffe R.B., Schacht M., Levy C., Jowitt T.A.,
Sandri-Goldin R.M., Golovanov A.P.;
"The structure of the folded domain from the signature multifunctional
protein ICP27 from herpes simplex virus-1 reveals an intertwined
dimer.";
Sci. Rep. 5:11234-11234(2015).
-!- FUNCTION: Multifunctional regulator of the expression of viral
genes that contributes to the shutoff of host protein synthesis
and mediates nuclear export of viral intronless mRNAs. Early in
infection, this immediate early (EI) protein mediates the
inhibition of cellular splicing. This results in the accumulation
of unprocessed 3'end pre-mRNAs which can't be exported from the
nucleus. Cellular protein synthesis is thereby shut off early
after virus infection. Later in the infection, it helps recruit
cellular RNA polymerase II to viral replication sites and promotes
the nuclear export of viral intronless mRNAs by interacting with
mRNAs and host NXF1/TAP. ICP27 binds to NUP62 which may provide
facilitated viral mRNA export and may indirectly compete with some
host cell transport receptors for binding and inhibit cellular
nucleocytoplasmic transport pathways (PubMed:22334672). Also
stimulates translation of viral transcripts. Repression of host
gene expression blocks the cell cycle at the G1 phase and prevents
apoptosis. Seems to silence the 3' splice site of the
promyelocytic leukemia (PML) intron 7a, thereby switching PML
isoforms from PML-II to PML-V. This could be linked to the
accelerated mRNA export induced by ICP27 which might not provide
sufficient time for PML pre-mRNA to be spliced in the nucleus.
{ECO:0000269|PubMed:11287586, ECO:0000269|PubMed:12660167,
ECO:0000269|PubMed:16537625, ECO:0000269|PubMed:19369354,
ECO:0000269|PubMed:19553338, ECO:0000269|PubMed:22334672,
ECO:0000269|PubMed:9512520}.
-!- SUBUNIT: Homodimer (PubMed:26085142, PubMed:26062451). Interacts
with host RBP1; this interaction facilitates the RNA polymerase
recruitment to viral transcription sites. Interacts (via the RGG
box) with host ALYREF/THOC4; this interaction recruits ALYREF to
viral replication compartments and probably directs viral mRNA to
the TAP/NFX1 pathway (PubMed:12438613). Interacts with host
ALYREF2 (PubMed:21253573). Interacts (via the RGG box) with host
SRPK1; this interaction relocalizes SRPK1 to the nucleus and seems
to alter its activity (PubMed:12660167, PubMed:19553338).
Interacts with ICP4; this interaction modulates ICP4 DNA-binding
activity (PubMed:8995681). Interacts with host NXF1; this
interaction allows efficient export of HHV-1 early and late
transcripts (PubMed:19369354). {ECO:0000269|PubMed:12438613,
ECO:0000269|PubMed:12660167, ECO:0000269|PubMed:19369354,
ECO:0000269|PubMed:19553338, ECO:0000269|PubMed:21253573,
ECO:0000269|PubMed:22334672, ECO:0000269|PubMed:26062451,
ECO:0000269|PubMed:26085142, ECO:0000269|PubMed:8995681}.
-!- INTERACTION:
P08392:ICP4; NbExp=5; IntAct=EBI-6883946, EBI-7185388;
P37198:NUP62 (xeno); NbExp=3; IntAct=EBI-6883946, EBI-347978;
Q9UBU9:NXF1 (xeno); NbExp=4; IntAct=EBI-6883946, EBI-398874;
-!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:9501050}.
Host nucleus {ECO:0000269|PubMed:26062451,
ECO:0000269|PubMed:9501050}. Note=Shuttles between the nucleus and
the cytoplasm. {ECO:0000269|PubMed:9501050}.
-!- DOMAIN: Binds viral intronless RNAs through the RGG region.
-!- DOMAIN: The C-terminus is essential for homodimerization.
{ECO:0000269|PubMed:26062451, ECO:0000269|PubMed:26085142}.
-!- PTM: Methylated within the RGG box possibly by host PRMT1. When
hypomethylated, ICP27 is exported to the cytoplasm earlier and
more rapidly. {ECO:0000269|PubMed:19321610}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:10074178}.
-!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family.
{ECO:0000305}.
-!- CAUTION: A role in degradation of host polymerase has been
suggested in PubMed 16537625, but this could be a consequence of
binding to immature mRNAs simultaneously to transcription by the
polymerase. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X14112; CAA32290.1; -; Genomic_DNA.
EMBL; DQ889502; ABI63515.1; -; Genomic_DNA.
EMBL; FJ593289; ACM62278.1; -; Genomic_DNA.
PIR; I30089; WMBEY4.
RefSeq; YP_009137130.1; NC_001806.2.
PDB; 2KT5; NMR; -; B=103-138.
PDB; 4YXP; X-ray; 1.92 A; A/B=241-512.
PDB; 5BQK; X-ray; 2.00 A; A/B/C=242-512.
PDBsum; 2KT5; -.
PDBsum; 4YXP; -.
PDBsum; 5BQK; -.
ProteinModelPortal; P10238; -.
SMR; P10238; -.
BioGrid; 971451; 2.
DIP; DIP-57688N; -.
IntAct; P10238; 4.
MINT; MINT-6732574; -.
iPTMnet; P10238; -.
PRIDE; P10238; -.
GeneID; 24271474; -.
KEGG; vg:24271474; -.
KO; K19443; -.
OrthoDB; VOG09000093; -.
Proteomes; UP000009294; Genome.
Proteomes; UP000180652; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0039652; P:activation by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039524; P:suppression by virus of host mRNA processing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR031752; HHV-1_REF-bd.
InterPro; IPR008648; ICP27-like.
Pfam; PF05459; Herpes_UL69; 1.
Pfam; PF16852; HHV-1_VABD; 1.
1: Evidence at protein level;
3D-structure; Activation of host NF-kappa-B by virus; Activator;
Complete proteome; Early protein;
Eukaryotic host gene expression shutoff by virus;
G1/S host cell cycle checkpoint dysregulation by virus;
Host cytoplasm; Host gene expression shutoff by virus;
Host mRNA suppression by virus; Host nucleus; Host-virus interaction;
Inhibition of host pre-mRNA processing by virus; Metal-binding;
Methylation; Modulation of host cell cycle by virus; Phosphoprotein;
Reference proteome; RNA-binding; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 512 mRNA export factor.
/FTId=PRO_0000115823.
ZN_FING 400 488 CHC2-type. {ECO:0000269|PubMed:26062451,
ECO:0000269|PubMed:26085142}.
REGION 104 112 Interaction with host ALYREF.
REGION 138 152 RGG-box.
REGION 500 512 Important for homodimerization.
{ECO:0000269|PubMed:26062451}.
MOTIF 5 17 Nuclear export signal.
MOTIF 110 138 Nuclear localization signal.
METAL 400 400 Zinc. {ECO:0000269|PubMed:26062451,
ECO:0000269|PubMed:26085142}.
METAL 479 479 Zinc. {ECO:0000269|PubMed:26062451,
ECO:0000269|PubMed:26085142}.
METAL 483 483 Zinc. {ECO:0000269|PubMed:26062451,
ECO:0000269|PubMed:26085142}.
METAL 488 488 Zinc. {ECO:0000269|PubMed:26062451,
ECO:0000269|PubMed:26085142}.
MOD_RES 16 16 Phosphoserine; by host.
{ECO:0000305|PubMed:10074178}.
MOD_RES 18 18 Phosphoserine; by host.
{ECO:0000305|PubMed:10074178}.
MOD_RES 114 114 Phosphoserine; by host.
{ECO:0000305|PubMed:10074178}.
MOD_RES 138 138 Omega-N-methylated arginine; by host.
{ECO:0000305|PubMed:19321610}.
MOD_RES 148 148 Omega-N-methylated arginine; by host.
{ECO:0000305|PubMed:19321610}.
MOD_RES 150 150 Omega-N-methylated arginine; by host.
{ECO:0000305|PubMed:19321610}.
VARIANT 137 137 A -> V (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 206 206 Q -> P (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 383 383 T -> A (in strain: Nonneuroinvasive
mutant HF10 and 17 syn+).
MUTAGEN 500 512 Missing: Impaired homodimerization.
{ECO:0000269|PubMed:26062451}.
HELIX 247 254 {ECO:0000244|PDB:4YXP}.
HELIX 256 259 {ECO:0000244|PDB:4YXP}.
HELIX 262 275 {ECO:0000244|PDB:4YXP}.
TURN 279 282 {ECO:0000244|PDB:4YXP}.
HELIX 293 296 {ECO:0000244|PDB:4YXP}.
TURN 305 308 {ECO:0000244|PDB:4YXP}.
HELIX 312 328 {ECO:0000244|PDB:4YXP}.
HELIX 330 346 {ECO:0000244|PDB:4YXP}.
HELIX 349 368 {ECO:0000244|PDB:4YXP}.
HELIX 378 381 {ECO:0000244|PDB:4YXP}.
HELIX 383 405 {ECO:0000244|PDB:4YXP}.
HELIX 410 416 {ECO:0000244|PDB:4YXP}.
HELIX 419 421 {ECO:0000244|PDB:4YXP}.
HELIX 425 442 {ECO:0000244|PDB:4YXP}.
STRAND 445 447 {ECO:0000244|PDB:4YXP}.
HELIX 449 452 {ECO:0000244|PDB:4YXP}.
HELIX 467 478 {ECO:0000244|PDB:4YXP}.
HELIX 479 481 {ECO:0000244|PDB:4YXP}.
HELIX 486 496 {ECO:0000244|PDB:4YXP}.
SEQUENCE 512 AA; 55253 MW; 97DF74A2B7E63A85 CRC64;
MATDIDMLID LGLDLSDSDL DEDPPEPAES RRDDLESDSS GECSSSDEDM EDPHGEDGPE
PILDAARPAV RPSRPEDPGV PSTQTPRPTE RQGPNDPQPA PHSVWSRLGA RRPSCSPEQH
GGKVARLQPP PTKAQPARGG RRGRRRGRGR GGPGAADGLS DPRRRAPRTN RNPGGPRPGA
GWTDGPGAPH GEAWRGSEQP DPPGGQRTRG VRQAPPPLMT LAIAPPPADP RAPAPERKAP
AADTIDATTR LVLRSISERA AVDRISESFG RSAQVMHDPF GGQPFPAANS PWAPVLAGQG
GPFDAETRRV SWETLVAHGP SLYRTFAGNP RAASTAKAMR DCVLRQENFI EALASADETL
AWCKMCIHHN LPLRPQDPII GTTAAVLDNL ATRLRPFLQC YLKARGLCGL DELCSRRRLA
DIKDIASFVF VILARLANRV ERGVAEIDYA TLGVGVGEKM HFYLPGACMA GLIEILDTHR
QECSSRVCEL TASHIVAPPY VHGKYFYCNS LF


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