ICP27_HHV8P
ID ICP27_HHV8P Reviewed; 455 AA.
AC Q2HR75; O40938;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=mRNA export factor ICP27 homolog;
DE AltName: Full=EB2 protein homolog;
GN ORFNames=ORF57;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Neipel F., Albrecht J.-C., Ensser A., Huang Y.-Q., Li J.J.,
RA Friedman-Kien A.E., Fleckenstein B.;
RT "The genome of human herpesvirus 8 cloned from Kaposi's sarcoma.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INTERACTION WITH HUMAN ALYREF.
RX PubMed=15155762; DOI=10.1074/jbc.m313008200;
RA Malik P., Blackbourn D.J., Clements J.B.;
RT "The evolutionarily conserved Kaposi's sarcoma-associated herpesvirus ORF57
RT protein interacts with REF protein and acts as an RNA export factor.";
RL J. Biol. Chem. 279:33001-33011(2004).
RN [4]
RP REVIEW.
RX PubMed=19273144; DOI=10.2741/3322;
RA Majerciak V., Zheng Z.-M.;
RT "Kaposi's sarcoma-associated herpesvirus ORF57 in viral RNA processing.";
RL Front. Biosci. 14:1516-1528(2009).
RN [5]
RP INTERACTION WITH PROTEIN KBZIP/K8.
RX PubMed=23365430; DOI=10.1128/jvi.03459-12;
RA Hunter O.V., Sei E., Richardson R.B., Conrad N.K.;
RT "Chromatin immunoprecipitation and microarray analysis suggest functional
RT cooperation between Kaposi's Sarcoma-associated herpesvirus ORF57 and K-
RT bZIP.";
RL J. Virol. 87:4005-4016(2013).
CC -!- FUNCTION: Early protein that promotes the accumulation and nuclear
CC export of viral intronless RNA transcripts by interacting with mRNAs
CC and cellular export proteins. Probably acts as a viral splicing factor
CC that regulates viral RNA splicing. Functions as a multifunctional
CC regulator of the expression of viral lytic genes.
CC {ECO:0000269|PubMed:15155762}.
CC -!- SUBUNIT: Homodimer. Homodimerization is required for transactivation
CC (By similarity). Interacts with host ALYREF (PubMed:15155762).
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 (Probable). Interacts with protein K-bZIP/K8; this interaction promotes
CC viral gene expression during lytic infection. {ECO:0000250,
CC ECO:0000269|PubMed:15155762, ECO:0000269|PubMed:23365430, ECO:0000305}.
CC -!- INTERACTION:
CC Q2HR75; Q2HR82: K8; NbExp=5; IntAct=EBI-6884751, EBI-9006943;
CC Q2HR75; Q86V81: ALYREF; Xeno; NbExp=4; IntAct=EBI-6884751, EBI-347640;
CC Q2HR75; Q96QD9: FYTTD1; Xeno; NbExp=9; IntAct=EBI-6884751, EBI-724553;
CC Q2HR75; Q9BRP8: PYM1; Xeno; NbExp=4; IntAct=EBI-6884751, EBI-2352802;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host nucleus
CC {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm.
CC -!- INDUCTION: Transactivated by ORF50 protein.
CC -!- DOMAIN: Binds viral intronless RNAs. {ECO:0000250}.
CC -!- MISCELLANEOUS: ORF50 and ORF57 are the earliest genes expressed in the
CC lytic cycle.
CC -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
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DR EMBL; AF148805; ABD28908.1; -; Genomic_DNA.
DR EMBL; U93872; AAB62615.1; -; Genomic_DNA.
DR RefSeq; YP_001129410.1; NC_009333.1.
DR PDB; 5ZB1; X-ray; 3.06 A; A=168-455.
DR PDB; 5ZB3; X-ray; 3.51 A; A/B=168-455.
DR PDBsum; 5ZB1; -.
DR PDBsum; 5ZB3; -.
DR SMR; Q2HR75; -.
DR BioGRID; 1777028; 15.
DR IntAct; Q2HR75; 9.
DR MINT; Q2HR75; -.
DR PRIDE; Q2HR75; -.
DR DNASU; 4961525; -.
DR GeneID; 4961525; -.
DR KEGG; vg:4961525; -.
DR Proteomes; UP000000942; 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 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..455
FT /note="mRNA export factor ICP27 homolog"
FT /id="PRO_0000387979"
FT ZN_FING 333..432
FT /note="CHC2-type"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT REGION 17..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 101..107
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 121..130
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 143..152
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 23..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT CONFLICT 1..16
FT /note="MVQAMIDMDIMKGILE -> RIVLSSSPGGPSPHPSFIAFDIT (in Ref.
FT 2; AAB62615)"
FT /evidence="ECO:0000305"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 279..298
FT /evidence="ECO:0007829|PDB:5ZB1"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:5ZB1"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 357..366
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 372..387
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 394..405
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 411..423
FT /evidence="ECO:0007829|PDB:5ZB1"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:5ZB1"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:5ZB1"
SQ SEQUENCE 455 AA; 51012 MW; D3262C05AA472515 CRC64;
MVQAMIDMDI MKGILEDSVS SSEFDESRDD ETDAPTLEDE QLSEPAEPPA DERIRGTQSA
QGIPPPLGRI PKKSQGRSQL RSEIQFCSPL SRPRSPSPVN RYGKKIKFGT AGQNTRPPPE
KRPRRRPRDR LQYGRTTRGG QCRAAPKRAT RRPQVNCQRQ DDDVRQGVSD AVKKLRLPAS
MIIDGESPRF DDSIIPRHHG ACFNVFIPAP PSHVPEVFTD RDITALIRAG GKDDELINKK
ISAKKIDHLH RQMLSFVTSR HNQAYWVSCR RETAAAGGLQ TLGAFVEEQM TWAQTVVRHG
GWFDEKDIDI ILDTAIFVCN AFVTRFRLLH LSCVFDKQSE LALIKQVAYL VAMGNRLVEA
CNLLGEVKLN FRGGLLLAFV LTIPGMQSRR SISARGQELF RTLLEYYRPG DVMGLLNVIV
MEHHSLCRNS ECAAATRAAM GSAKFNKGLF FYPLS
