ID   P14_ASFM2               Reviewed;         122 AA.
AC   Q65245;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Structural protein p14.5;
GN   OrderedLocusNames=Mal-141; ORFNames=k3R;
OS   African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10500;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA   Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA   Hammond J.M., Smith G.L.;
RT   "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT   a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL   J. Gen. Virol. 75:1655-1684(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Structural protein required for transport of intracellular
CC       particles from the assembly sites to the plasma membrane (By
CC       similarity). Binds to both ssDNA and dsDNA (By similarity). Suppressed
CC       the activation of the cGAS/STING pathway by interfering with the
CC       recruitment of IRF3 to TBK1, which in turn suppresses IRF3
CC       phosphorylation, decreasing interferon production (By similarity).
CC       {ECO:0000250|UniProtKB:Q65201}.
CC   -!- SUBUNIT: Interacts with the major capsid protein (By similarity).
CC       Interacts with host IRF3; this interaction interfers with the
CC       recruitment of IRF3 to TBK1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q65201}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:Q65201}.
CC       Note=Localizes at the surface of the intracellular virion.
CC       {ECO:0000250|UniProtKB:Q65201}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- PTM: Acetylated. {ECO:0000250|UniProtKB:Q65201}.
CC   -!- SIMILARITY: Belongs to the asfivirus structural protein p14.5 family.
CC       {ECO:0000305}.
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DR   EMBL; X71982; CAA50841.1; -; Genomic_DNA.
DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000860; 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   3: Inferred from homology;
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; Viral immunoevasion; Viral release from host cell; Virion.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..122
FT                   /note="Structural protein p14.5"
FT                   /id="PRO_0000373398"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..122
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        85..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..122
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q65201"
SQ   SEQUENCE   122 AA;  14042 MW;  DD4BAC2014DB7C99 CRC64;
     MADFNSPIQY LKEDSRDRTS IGSLEYDENA DTMIPSFAAG LEEFEPIPDY DPTRSTSLYS
     QLTHNMERIA EEDDINFQHD TREFTSLVPE ETDNKPEDDE ESGAKPKKKK HLFPKLSSHK
     SK