位置:首页 > 蛋白库 > P14_ASFP4
P14_ASFP4
ID   P14_ASFP4               Reviewed;         121 AA.
AC   P0C9Y6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Structural protein p14.5;
GN   OrderedLocusNames=Pret-145;
OS   African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561443;
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].
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}.
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; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000859; 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..121
FT                   /note="Structural protein p14.5"
FT                   /id="PRO_0000373399"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..121
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        84..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..121
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   121 AA;  13737 MW;  0B0923951AB3A466 CRC64;
     MADFNSPIQY LKEDSRDRTS IGSLEYDENS DTIIPSFAAG LEDFEPIPSP TTTSTSLYSQ
     LTHNMEKIAE EEDINFLHDT REFTSLVPEE TDNKPEDDEE SGAKPKKKKH LFPKLSSHKS
     K
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024