ICP27_SHV21
ID ICP27_SHV21 Reviewed; 417 AA.
AC P13199;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=mRNA export factor ICP27 homolog;
DE AltName: Full=52 kDa immediate-early phosphoprotein;
DE AltName: Full=EB2 protein homolog;
GN Name=EJRF1; ORFNames=ORF57;
OS Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10383;
OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA Honess R.W.;
RT "Primary structure of the herpesvirus saimiri genome.";
RL J. Virol. 66:5047-5058(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1314457; DOI=10.1016/0042-6822(92)90759-i;
RA Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.;
RT "Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus
RT saimiri (HVS) L-DNA: general conservation of genetic organization between
RT HVS and Epstein-Barr virus.";
RL Virology 188:296-310(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-417.
RX PubMed=2841477; DOI=10.1128/jvi.62.9.3250-3257.1988;
RA Nicholas J., Gompels U.A., Craxton M.A., Honess R.W.;
RT "Conservation of sequence and function between the product of the 52-
RT kilodalton immediate-early gene of herpesvirus saimiri and the BMLF1-
RT encoded transcriptional effector (EB2) of Epstein-Barr virus.";
RL J. Virol. 62:3250-3257(1988).
RN [4]
RP INTERACTION WITH HOST ALYREF AND WITH MOUSE ALYREF2, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=C488;
RX PubMed=21253573; DOI=10.1371/journal.ppat.1001244;
RA Tunnicliffe R.B., Hautbergue G.M., Kalra P., Jackson B.R., Whitehouse A.,
RA Wilson S.A., Golovanov A.P.;
RT "Structural basis for the recognition of cellular mRNA export factor REF by
RT herpes viral proteins HSV-1 ICP27 and HVS ORF57.";
RL PLoS Pathog. 7:E1001244-E1001244(2011).
RN [5]
RP STRUCTURE BY NMR OF 103-120 IN COMPLEX WITH HOST ALYREF2, INTERACTION WITH
RP HOST ALYREF2, RNA-BINDING, REGION, AND SUBUNIT.
RX PubMed=24550725; DOI=10.1371/journal.ppat.1003907;
RA Tunnicliffe R.B., Hautbergue G.M., Wilson S.A., Kalra P., Golovanov A.P.;
RT "Competitive and cooperative interactions mediate RNA transfer from
RT herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF.";
RL PLoS Pathog. 10:E1003907-E1003907(2014).
CC -!- FUNCTION: Probably acts as a viral splicing factor that regulates viral
CC RNA splicing. Functions as a multifunctional regulator of the
CC expression of viral lytic genes (By similarity). Early protein that
CC promotes the accumulation and nuclear export of viral intronless RNA
CC transcripts by interacting with mRNAs and cellular export proteins.
CC {ECO:0000250, ECO:0000269|PubMed:21253573}.
CC -!- SUBUNIT: Homodimer. Homodimerization is required for transactivation
CC (By similarity). Interacts with host ALYREF and with mouse ALYREF2.
CC Associates in a complex with RNA, and host export factors NXF1/TAP and
CC ALYREF or ALYREF2; these interactions allow nuclear export of viral
CC transcripts. {ECO:0000250, ECO:0000269|PubMed:21253573,
CC ECO:0000269|PubMed:24550725}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host nucleus
CC {ECO:0000269|PubMed:21253573}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250}.
CC -!- INDUCTION: Transactivated by ORF50 protein.
CC -!- DOMAIN: Binds viral intronless RNAs; the RNA binding site overlaps
CC partially with the binding site for host ALYREF or ALYREF2.
CC -!- MISCELLANEOUS: ORF50 and ORF57 are the earliest genes expressed in the
CC lytic cycle. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46125.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X64346; CAA45680.1; -; Genomic_DNA.
DR EMBL; M86409; AAA46125.1; ALT_INIT; Genomic_DNA.
DR EMBL; M21943; AAA66558.1; -; Genomic_DNA.
DR RefSeq; NP_040259.1; NC_001350.1.
DR PDB; 2YKA; NMR; -; B=103-120.
DR PDB; 6HAT; X-ray; 1.86 A; A/B=146-417.
DR PDB; 6HAU; X-ray; 1.86 A; A/B=146-417.
DR PDBsum; 2YKA; -.
DR PDBsum; 6HAT; -.
DR PDBsum; 6HAU; -.
DR BMRB; P13199; -.
DR SMR; P13199; -.
DR GeneID; 1682520; -.
DR KEGG; vg:1682520; -.
DR Proteomes; UP000000587; 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 DisProt; DP03056; -.
DR InterPro; IPR008648; ICP27-like.
DR Pfam; PF05459; Herpes_UL69; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Early protein; Host cytoplasm; Host nucleus;
KW Metal-binding; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..417
FT /note="mRNA export factor ICP27 homolog"
FT /id="PRO_0000115832"
FT ZN_FING 295..394
FT /note="CHC2-type"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..120
FT /note="Interaction with RNA"
FT REGION 106..120
FT /note="Interaction with host ALYREF or mouse ALYREF2"
FT MOTIF 88..94
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 118..127
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:2YKA"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:6HAT"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6HAT"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:6HAT"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:6HAT"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 334..350
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 373..388
FT /evidence="ECO:0007829|PDB:6HAT"
FT HELIX 392..402
FT /evidence="ECO:0007829|PDB:6HAT"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:6HAT"
SQ SEQUENCE 417 AA; 46816 MW; 12F0EA3733F00940 CRC64;
MEDIIEGGIS SDDDFDSSDS SSDEEESDTS PQIMKSDVTM ASPPSTPEPS PDVSASTSNL
KRERQRSPIT WEHQSPLSRV YRSPSPMRFG KRPRISSNST SRSCKTSWAD RVREAAAQRR
PSRPFRKPYS HPRNGPLRNG PPRAPPLLKL FDISILPKSG EPKLFLPVPS LPCQEAEKTN
DKYVLAMAQR AMHDVPISSK QLTANLLPVK FKPLLSIVRY TPNYYYWVSM RKETIASANL
CTVAAFLDES LCWGQQYLKN DFIFSENGKD IILDTSSALL SQLVHKIKML PFCHCLMQTT
PQDHIVKQVC YLIASNNRIL DAVRYLQTSV IKSPIVLLLA YAVCLPAAII CTKNETQLYS
HCMRILKEYR PGDVMNILHE SLTQHLNKCP SSTCAYTTRA IVGTKANTTG LFFLPTQ
