ID   VF329_ASFP4             Reviewed;         329 AA.
AC   P0CAE5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Transmembrane protein I329L;
DE   Flags: Precursor;
GN   OrderedLocusNames=Pret-154;
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 [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: Viral TLR3 homolog that probably prevents TLR3 dimerization
CC       and subsequent induction of IFN (By similarity). Inhibits dsRNA-
CC       stimulated activation of NF-kB and IRF3 (By similarity).
CC       {ECO:0000250|UniProtKB:P27945}.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P27945}; Single-pass type I membrane protein
CC       {ECO:0000305}. Host Golgi apparatus membrane; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- DOMAIN: Contains putative leucine-rich repeats (LRR) and a C-terminus
CC       cysteine-rich capping motif similar to domain structure of host TLR3.
CC       {ECO:0000250|UniProtKB:P27945}.
CC   -!- PTM: Highly glycosylated. {ECO:0000250|UniProtKB:P27945}.
CC   -!- SIMILARITY: Belongs to the asfivirus I329L family. {ECO:0000305}.
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DR   EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000859; Genome.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Host endoplasmic reticulum;
KW   Host Golgi apparatus; Host membrane; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host TLR pathway by virus; Late protein; Leucine-rich repeat;
KW   Membrane; Signal; Transmembrane; Transmembrane helix; Viral immunoevasion.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..329
FT                   /note="Transmembrane protein I329L"
FT                   /id="PRO_0000373651"
FT   TOPO_DOM        17..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..329
FT                   /note="Cytoplasmic"
FT   REPEAT          112..133
FT                   /note="LRR"
FT                   /evidence="ECO:0000250|UniProtKB:P27945"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        195..237
FT                   /evidence="ECO:0000250|UniProtKB:P27945"
SQ   SEQUENCE   329 AA;  38424 MW;  7E19246E254DBA80 CRC64;
     MLRVFIFFVF LGSGLTGRIK PQITCKYFIS ENNTWYKYNV TILNGTIVLP AYNTIPSNAA
     GISCTCHDID YLQKNNISIH YNTSILKTFQ DIRIIRCGMK NISEIAGGFG KELKFLDLRY
     NDLQVIEYNI LRKLIRSNTP TYLYYNNLMC GKRNCPLYYF LLKQEQTYLK LLPQFFLRRI
     NFSNNNTYLY HFLSCGNKPG HEFLEYQTKY CRTKFPEINI TVNQLTAKKN TERYKSCYPL
     VFISILCSCI SFLFLFICLL RSICKKYSCT KQGKSGHNYI PLIPSYTFSL KKHRHPETAV
     VEDHTTSANS PIVYIPTTEE KKVSCSRRK