VIRF3_HHV8P
ID VIRF3_HHV8P Reviewed; 566 AA.
AC F5HIC6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 23-FEB-2022, entry version 44.
DE RecName: Full=Viral IRF3-like protein;
DE Short=VIRF-3;
GN Name=vIRF-3;
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=10933732; DOI=10.1128/jvi.74.17.8194-8201.2000;
RA Lubyova B., Pitha P.M.;
RT "Characterization of a novel human herpesvirus 8-encoded protein, vIRF-3,
RT that shows homology to viral and cellular interferon regulatory factors.";
RL J. Virol. 74:8194-8201(2000).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST SKP2.
RX PubMed=22453922; DOI=10.1074/jbc.m111.335216;
RA Baresova P., Pitha P.M., Lubyova B.;
RT "Kaposi sarcoma-associated herpesvirus vIRF-3 protein binds to F-box of
RT Skp2 protein and acts as a regulator of c-Myc protein function and
RT stability.";
RL J. Biol. Chem. 287:16199-16208(2012).
RN [5]
RP FUNCTION.
RX PubMed=23449805; DOI=10.1128/jvi.00250-13;
RA Zuo J., Hislop A.D., Leung C.S., Sabbah S., Rowe M.;
RT "Kaposi's sarcoma-associated herpesvirus-encoded viral IRF3 modulates major
RT histocompatibility complex class II (MHC-II) antigen presentation through
RT MHC-II transactivator-dependent and -independent mechanisms: implications
RT for oncogenesis.";
RL J. Virol. 87:5340-5350(2013).
CC -!- FUNCTION: Plays a role in the inhibition of host immune response.
CC Interferes with the transactivating potential of cellular IRFs IRF3 and
CC IRF7 that play a critical role in the induction of IFNA and IFNB genes.
CC Additionally, interferes with surface major histocompatibility complex
CC class II (MHC-II) antigen presentation. {ECO:0000269|PubMed:10933732,
CC ECO:0000269|PubMed:22453922, ECO:0000269|PubMed:23449805}.
CC -!- SUBUNIT: Interacts with host SKP2. {ECO:0000269|PubMed:22453922}.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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DR EMBL; AF148805; ABD28911.1; -; Genomic_DNA.
DR RefSeq; YP_001129413.1; NC_009333.1.
DR SMR; F5HIC6; -.
DR BioGRID; 1776996; 9.
DR PRIDE; F5HIC6; -.
DR DNASU; 4961493; -.
DR GeneID; 4961493; -.
DR KEGG; vg:4961493; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0039505; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II; IEA:UniProtKB-KW.
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 Pfam; PF10401; IRF-3; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Host-virus interaction;
KW Inhibition of host adaptive immune response by virus;
KW Inhibition of host MHC class II molecule presentation by virus;
KW Reference proteome; Transcription; Transcription regulation;
KW Viral immunoevasion.
FT CHAIN 1..566
FT /note="Viral IRF3-like protein"
FT /id="PRO_0000423779"
FT REGION 151..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 62508 MW; 822C557407A8C84B CRC64;
MAGRRLTWIS EFIVGALDSD KYPLVKWLDR STGTFLAPAA RNDVIPLDSL QFFIDFKREC
LSKGLHPRDL LGSPITAFGK ICTTSRRLRR LPGEEYEVVQ GINCRRWRLL CAEVKECWWC
VHARTHLHSG SSLWEILYQH SVRLEKHRRR PRPFVGENSD SSEEDHPAFC DVPVTQTGAE
SEDSGDEGPS TRHSASGVQP VDDANADSPG SGDEGPSTRH SDSQPPPADE TTVHTDNVED
DLTLLDKESA CALMYHVGQE MDMLMRAMCD EDLFDLLGIP EDVIATSQPG GDTDASGVVT
EGSIAASAVG AGVEDVYLAG ALEAQNVAGE YVLEISDEEV DDGAGLPPAS RRRPVVGEFL
WDDGPRRHER PTTRRIRHRK LRSAYYRVAR PPVMITDRLG VEVFYFGRPA MSLEVERKVF
ILCSQNPLAD ISHSCLHSRK GLRVLLPKPD DNNTGPGDVN LLAAVLRSFA SGLVIVSLRS
GIYVKNLCKS TVLYHGNNPP KKFGVICGLS SRAVLDVFNV AQYRIQGHEH IKKTTVFIGG
DPTSAEQFDM VPLVIKLRLR SVTCDD
