P14_ASFB7
ID P14_ASFB7 Reviewed; 120 AA.
AC Q65201;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Protein p14.5;
DE AltName: Full=pE120R;
GN OrderedLocusNames=Ba71V-133; ORFNames=E120R;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [2]
RP DNA-BINDING, INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=9123862; DOI=10.1006/viro.1996.8434;
RA Martinez-Pomares L., Simon-Mateo C., Lopez-Otin C., Vinuela E.;
RT "Characterization of the African swine fever virus structural protein
RT p14.5: a DNA binding protein.";
RL Virology 229:201-211(1997).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE MAJOR CAPSID
RP PROTEIN.
RX PubMed=11435554; DOI=10.1128/jvi.75.15.6758-6768.2001;
RA Andres G., Garcia-Escudero R., Vinuela E., Salas M.L., Rodriguez J.M.;
RT "African swine fever virus structural protein pE120R is essential for virus
RT transport from assembly sites to plasma membrane but not for infectivity.";
RL J. Virol. 75:6758-6768(2001).
RN [4]
RP ACETYLATION AT ALA-2.
RX PubMed=16964554; DOI=10.1007/s11262-006-0015-6;
RA Alfonso P., Quetglas J.I., Escribano J.M., Alonso C.;
RT "Protein pE120R of African swine fever virus is post-translationally
RT acetylated as revealed by post-source decay MALDI mass spectrometry.";
RL Virus Genes 35:81-85(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA Alejo A., Matamoros T., Guerra M., Andres G.;
RT "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL J. Virol. 92:0-0(2018).
RN [6]
RP REVIEW.
RX PubMed=32725217; DOI=10.1042/bst20191108;
RA Cackett G., Sykora M., Werner F.;
RT "Transcriptome view of a killer: African swine fever virus.";
RL Biochem. Soc. Trans. 48:1569-1581(2020).
RN [7]
RP INDUCTION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
RN [8]
RP FUNCTION, INTERACTION WITH HOST IRF3, MUTAGENESIS OF 70-ASP-ILE-71, AND
RP INDUCTION.
RX PubMed=34190598; DOI=10.1128/jvi.00824-21;
RA Liu H., Zhu Z., Feng T., Ma Z., Xue Q., Wu P., Li P., Li S., Yang F.,
RA Cao W., Xue Z., Chen H., Liu X., Zheng H.;
RT "African swine fever virus E120R protein inhibits interferon-beta
RT production by interacting with IRF3 to block its activation.";
RL J. Virol. 95:E0082421-E0082421(2021).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=33429879; DOI=10.3390/v13010077;
RA Aicher S.M., Monaghan P., Netherton C.L., Hawes P.C.;
RT "Unpicking the Secrets of African Swine Fever Viral Replication Sites.";
RL Viruses 13:0-0(2021).
CC -!- FUNCTION: Structural protein required for transport of intracellular
CC particles from the assembly sites to the plasma membrane
CC (PubMed:11435554). Binds to both ssDNA and dsDNA (PubMed:9123862).
CC Suppressed the activation of the cGAS/STING pathway by interfering with
CC the recruitment of IRF3 to TBK1, which in turn suppresses IRF3
CC phosphorylation, decreasing interferon production (PubMed:34190598).
CC {ECO:0000269|PubMed:11435554, ECO:0000269|PubMed:34190598,
CC ECO:0000269|PubMed:9123862}.
CC -!- SUBUNIT: Interacts with the major capsid protein (PubMed:11435554).
CC Interacts with host IRF3; this interaction interfers with the
CC recruitment of IRF3 to TBK1 (PubMed:34190598).
CC {ECO:0000269|PubMed:11435554, ECO:0000269|PubMed:34190598}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:11435554,
CC ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:9123862}.
CC Note=Localizes at the surface of the intracellular virion.
CC {ECO:0000305|PubMed:11435554}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:32075923, ECO:0000269|PubMed:34190598,
CC ECO:0000269|PubMed:9123862}.
CC -!- PTM: Acetylated. {ECO:0000269|PubMed:16964554}.
CC -!- SIMILARITY: Belongs to the asfivirus structural protein p14.5 family.
CC {ECO:0000305}.
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DR EMBL; U18466; AAA65361.1; -; Genomic_DNA.
DR RefSeq; NP_042825.1; NC_001659.2.
DR GeneID; 22220361; -.
DR KEGG; vg:22220361; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; 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 Late protein; Reference proteome; Viral immunoevasion;
KW Viral release from host cell; Virion.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..120
FT /note="Protein p14.5"
FT /id="PRO_0000373396"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine; by host"
FT /evidence="ECO:0000269|PubMed:16964554"
FT MUTAGEN 70..71
FT /note="EE->AA: Complete loss of interaction with host IRF3
FT and no unhibition of interferon production."
FT /evidence="ECO:0000269|PubMed:34190598"
SQ SEQUENCE 120 AA; 13591 MW; 50321985DF6AD701 CRC64;
MADFNSPIQY LKEDSRDRTS IGSLEYDENS DTIIPSFAAG LEDFEPIPSP TTSTSLYSQL
THNMEKIAEE EDINFLHDTR EFTSLVPDKA DNKPEDDEES GAKPKKKKHL FPKLSSHKSK
