VIRF1_HHV8P
ID VIRF1_HHV8P Reviewed; 449 AA.
AC F5HF68;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=VIRF-1;
GN Name=vIRF-1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE 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 [3]
RP FUNCTION.
RX PubMed=9365244; DOI=10.1038/sj.onc.1201571;
RA Gao S.J., Boshoff C., Jayachandra S., Weiss R.A., Chang Y., Moore P.S.;
RT "KSHV ORF K9 (vIRF) is an oncogene which inhibits the interferon signaling
RT pathway.";
RL Oncogene 15:1979-1985(1997).
RN [4]
RP FUNCTION.
RX PubMed=9420276; DOI=10.1128/jvi.72.1.701-707.1998;
RA Zimring J.C., Goodbourn S., Offermann M.K.;
RT "Human herpesvirus 8 encodes an interferon regulatory factor (IRF) homolog
RT that represses IRF-1-mediated transcription.";
RL J. Virol. 72:701-707(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST IRF3; IRF7 AND CREBBP.
RX PubMed=11314014; DOI=10.1038/sj.onc.1204163;
RA Lin R., Genin P., Mamane Y., Sgarbanti M., Battistini A.,
RA Harrington W.J. Jr., Barber G.N., Hiscott J.;
RT "HHV-8 encoded vIRF-1 represses the interferon antiviral response by
RT blocking IRF-3 recruitment of the CBP/p300 coactivators.";
RL Oncogene 20:800-811(2001).
CC -!- FUNCTION: Plays a role in the inhibition of host innate response by
CC repressing the expression of interferon-inducible genes and blocking
CC host IRF1- and IRF3-mediated transcription. Blocks the interaction
CC between host IRF3 and CREBBP. {ECO:0000269|PubMed:11314014,
CC ECO:0000269|PubMed:9365244, ECO:0000269|PubMed:9420276}.
CC -!- SUBUNIT: Interacts with host IRF3, IRF7, and CREBBP.
CC {ECO:0000269|PubMed:11314014}.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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DR EMBL; AF148805; ABD28909.1; -; Genomic_DNA.
DR RefSeq; YP_001129411.1; NC_009333.1.
DR PDB; 4HLY; X-ray; 1.48 A; A/B=88-196.
DR PDB; 4YSI; X-ray; 1.02 A; B=44-51.
DR PDBsum; 4HLY; -.
DR PDBsum; 4YSI; -.
DR SMR; F5HF68; -.
DR BioGRID; 1776967; 21.
DR IntAct; F5HF68; 2.
DR PRIDE; F5HF68; -.
DR GeneID; 4961464; -.
DR KEGG; vg:4961464; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042025; C:host cell nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0039650; P:suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0036472; P:suppression by virus of host protein-protein interaction; IDA:ParkinsonsUK-UCL.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR CDD; cd00103; IRF; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.200.10; -; 1.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR019471; Interferon_reg_factor-3.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00605; IRF; 1.
DR Pfam; PF10401; IRF-3; 1.
DR SMART; SM00348; IRF; 1.
DR SMART; SM01243; IRF-3; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW Reference proteome; Viral immunoevasion.
FT CHAIN 1..449
FT /note="VIRF-1"
FT /id="PRO_0000423778"
FT DNA_BIND 89..195
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:4HLY"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4HLY"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:4HLY"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4HLY"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:4HLY"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4HLY"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:4HLY"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:4HLY"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:4HLY"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:4HLY"
SQ SEQUENCE 449 AA; 48460 MW; 3C6A4E48FD57521A CRC64;
MDPGQRPNPF GAPGAIPKKP CLSQGSPGTS GSGAPCDEPS RSESPGEGPS GTGGSAAAGD
ITRQAVVAAI TEWSRTRQLR ISTGASEGKA SIKDWIVCQV NSGKFPGVEW EDEERTRFRI
PVTPLADPCF EWRRDGELGV VYIRERGNMP VDASFKGTRG RRRMLAALRR TRGLQEIGKG
ISQDGHHFLV FRVRKPEEEQ CVECGVVAGA VHDFNNMARL LQEGFFSPGQ CLPGEIVTPV
PSCTTAEGQE AVIDWGRLFI RMYYNGEQVH ELLTTSQSGC RISSALRRDP AVHYCAVGSP
GQVWLPNVPN LACEIAKREL CDTLDACAKG ILLTSSCNGI FCVCYHNGPV HFIGNTVPPD
SGPLLLPQGK PTRIFNPNTF LVGLANSPLP APSHVTCPLV KLWLGKPVAV GKLEPHAPSP
RDFAARCSNF SDACVVLEIM PKPLWDAMQ
