VIRF4_HHV8P
ID VIRF4_HHV8P Reviewed; 911 AA.
AC Q2HR73; D0UZS2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 23-FEB-2022, entry version 72.
DE RecName: Full=Viral IRF4-like protein;
DE Short=vIRF-4;
GN Name=vIRF-4;
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, AND INTERACTION WITH HOST MDM2.
RX PubMed=19369353; DOI=10.1128/jvi.02353-08;
RA Lee H.R., Toth Z., Shin Y.C., Lee J.S., Chang H., Gu W., Oh T.K., Kim M.H.,
RA Jung J.U.;
RT "Kaposi's sarcoma-associated herpesvirus viral interferon regulatory factor
RT 4 targets MDM2 to deregulate the p53 tumor suppressor pathway.";
RL J. Virol. 83:6739-6747(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 202-216.
RX PubMed=22056774; DOI=10.1038/nsmb.2142;
RA Lee H.R., Choi W.C., Lee S., Hwang J., Hwang E., Guchhait K., Haas J.,
RA Toth Z., Jeon Y.H., Oh T.K., Kim M.H., Jung J.U.;
RT "Bilateral inhibition of HAUSP deubiquitinase by a viral interferon
RT regulatory factor protein.";
RL Nat. Struct. Mol. Biol. 18:1336-1344(2011).
CC -!- FUNCTION: Plays a role in host cell apoptosis modulation by promoting
CC TP53/p53 ubiquitination and subsequent degradation and thus down-
CC regulating TP53/p53-mediated apoptosis. {ECO:0000269|PubMed:19369353}.
CC -!- SUBUNIT: Interacts with host MDM2; this interaction facilitates the
CC proteasomal degradation of TP53/p53. {ECO:0000269|PubMed:19369353}.
CC -!- INTERACTION:
CC Q2HR73; Q00987: MDM2; Xeno; NbExp=2; IntAct=EBI-9001898, EBI-389668;
CC -!- SUBCELLULAR LOCATION: Host nucleus.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF148805; ABD28910.1; -; Genomic_DNA.
DR RefSeq; YP_001129412.1; NC_009333.1.
DR PDB; 2XXN; X-ray; 1.60 A; B=202-216.
DR PDBsum; 2XXN; -.
DR SMR; Q2HR73; -.
DR BioGRID; 1776998; 33.
DR IntAct; Q2HR73; 1.
DR PRIDE; Q2HR73; -.
DR DNASU; 4961495; -.
DR GeneID; 4961495; -.
DR KEGG; vg:4961495; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Host nucleus; Host-virus interaction;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..911
FT /note="Viral IRF4-like protein"
FT /id="PRO_0000423775"
FT DNA_BIND 7..114
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 147..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:2XXN"
SQ SEQUENCE 911 AA; 97956 MW; 0F82DA473774DC2D CRC64;
MPKAGGSEWA TLWIIDALEN NKFPYFSWFD RNNLLFAAPA PLPAGSDIPP GWYSVYHAFD
EECDRVYGPS PVVGQTVYGR FGRLLRGTRR AVVRNDLRYS DTFGGSYVVW QLVRTPFKNC
TYCYGAAYGP EKLQRFIQCL LSPPMQTTAT RRSDTREQSY EEAGAAAPAP PKAPSGLRGR
PRKSNRYYNV GDITTEQKAA CSVWIPVNEG ASTSGMGSSG TRQVTQASSF TWRVPGDPPA
PSTLTGPSDP HSSGAGLPGT APPKPQHETR LAGTVSGVSG VAQTPGDTGQ LAPPMRDGSR
LPSTSPWIPA CFPWGDLPVT GWWPQGASGL PEKVHPPTTG QFDPLSPRWT YTGIPSSQLN
PAAPSWIPPH AQAGTFVGEF SQGAPLAPQG LLPQSGQCAS AWLPRRETGA EGACGASTEG
RAPQGAASER VYPFEPQPPS APAPGYAKPS CYNWSPLAEP PATRPIRAPV WHPPVGHAVV
PEVRTPLWIP WSSGGAPNQG LSHTQGGASA TPSAGAPPTP EVAERQEPSS SGIPYVCQGD
NMATGYRRVT TSSGALEVEI IDLTGDSDTP STTVASTPLP VSGPRVFQPT VLYSAPEPAV
NPEVSHLPTE LERRECVCPG SGERPRVPLV STYAGDRYAV GGYGPEQSLV PPPLGLPLTL
SNLQGEDICT WEEGLGNILS ELQEEPSSST RQATDRRRPR SRSPHGRRTP VSHSGPEKPP
SKMFFDPPDS QRVSFVVEIF VYGNLRGTLR REGDAGEAML CSWPVGDTLG HLCQSFVPEL
LRIPRLTVPS PEQMEILNRV FEGLGHGFPI FCSMSGIYSR NATQVEGWWF GNPNSRYERI
LRSFSPRVPQ QLFNTARYLA TTAAIPQTPL SVNPVTCGTV FFGASPASTE NFQNVPLTVK
IFIGSIWDSL H
