A52_VACCW
ID A52_VACCW Reviewed; 190 AA.
AC Q01220; Q76ZM6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 23-FEB-2022, entry version 71.
DE RecName: Full=Protein A52;
GN OrderedLocusNames=VACWR178; ORFNames=A52R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA Smith G.L., Chan Y.S., Howard S.T.;
RT "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT right inverted terminal repeat.";
RL J. Gen. Virol. 72:1349-1376(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=12566418; DOI=10.1084/jem.20021652;
RA Harte M.T., Haga I.R., Maloney G., Gray P., Reading P.C., Bartlett N.W.,
RA Smith G.L., Bowie A., O'Neill L.A.;
RT "The poxvirus protein A52R targets Toll-like receptor signaling complexes
RT to suppress host defense.";
RL J. Exp. Med. 197:343-351(2003).
RN [4]
RP INTERACTION WITH HOST TRAF6 AND IRAK2.
RX PubMed=15998638; DOI=10.1074/jbc.m501917200;
RA Maloney G., Schroder M., Bowie A.G.;
RT "Vaccinia virus protein A52R activates p38 mitogen-activated protein kinase
RT and potentiates lipopolysaccharide-induced interleukin-10.";
RL J. Biol. Chem. 280:30838-30844(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 37-190.
RX PubMed=18704168; DOI=10.1371/journal.ppat.1000128;
RA Graham S.C., Bahar M.W., Cooray S., Chen R.A., Whalen D.M., Abrescia N.G.,
RA Alderton D., Owens R.J., Stuart D.I., Smith G.L., Grimes J.M.;
RT "Vaccinia virus proteins A52 and B14 Share a Bcl-2-like fold but have
RT evolved to inhibit NF-kappaB rather than apoptosis.";
RL PLoS Pathog. 4:E1000128-E1000128(2008).
CC -!- FUNCTION: Bcl-2-like protein which targets host toll-like receptor
CC signaling complexes to suppress innate immune response. Interacts with
CC host TRAF6 to activate p38 and subsequently induce the expression of
CC several cytokines such as IL-10. Associates also with host IRAK2 to
CC inhibit NF-kappa-B signaling. {ECO:0000269|PubMed:12566418}.
CC -!- SUBUNIT: Interacts with host TRAF6 and IRAK2.
CC {ECO:0000269|PubMed:15998638}.
CC -!- INTERACTION:
CC Q01220; Q9Y4K3: TRAF6; Xeno; NbExp=2; IntAct=EBI-3863691, EBI-359276;
CC -!- SIMILARITY: Belongs to the orthopoxvirus A52R protein family.
CC {ECO:0000305}.
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DR EMBL; D11079; BAA01826.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89457.1; -; Genomic_DNA.
DR PIR; JQ1790; JQ1790.
DR RefSeq; YP_233060.1; NC_006998.1.
DR PDB; 2VVW; X-ray; 1.90 A; A/B=37-190.
DR PDB; 2VVX; X-ray; 2.75 A; A/B=37-190.
DR PDBsum; 2VVW; -.
DR PDBsum; 2VVX; -.
DR SMR; Q01220; -.
DR IntAct; Q01220; 21.
DR DNASU; 3707707; -.
DR GeneID; 3707707; -.
DR KEGG; vg:3707707; -.
DR EvolutionaryTrace; Q01220; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.437.20; -; 1.
DR InterPro; IPR022819; Poxvirus_Bcl-2-like.
DR InterPro; IPR043018; Poxvirus_sf.
DR Pfam; PF06227; Poxvirus; 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 NF-kappa-B by virus;
KW Inhibition of host RLR pathway by virus; Inhibition of host TRAFs by virus;
KW Reference proteome; Viral immunoevasion.
FT CHAIN 1..190
FT /note="Protein A52"
FT /id="PRO_0000099350"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:2VVW"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2VVW"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:2VVW"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:2VVW"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:2VVW"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2VVW"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:2VVW"
FT HELIX 131..150
FT /evidence="ECO:0007829|PDB:2VVW"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:2VVW"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:2VVW"
FT HELIX 170..188
FT /evidence="ECO:0007829|PDB:2VVW"
SQ SEQUENCE 190 AA; 22770 MW; 747CCF0DC8FB7926 CRC64;
MDIKIDISIS GDKFTVTTRR ENEERKKYLP LQKEKTTDVI KPDYLEYDDL LDRDEMFTIL
EEYFMYRGLL GLRIKYGRLF NEIKKFDNDA EEQFGTIEEL KQKLRLNSEE GADNFIDYIK
VQKQDIVKLT VYDCISMIGL CACVVDVWRN EKLFSRWKYC LRAIKLFIND HMLDKIKSIL
QNRLVYVEMS