ID   I329L_ASFK5             Reviewed;         329 AA.
AC   P0CAE3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Transmembrane protein I329L;
DE   Flags: Precursor;
GN   OrderedLocusNames=Ken-153;
OS   African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561445;
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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000861; 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   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
PE   3: Inferred from homology;
KW   Glycoprotein; Host endoplasmic reticulum; Host Golgi apparatus;
KW   Host membrane; Late protein; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000250|UniProtKB:A9JM73"
FT   CHAIN           32..329
FT                   /note="Transmembrane protein I329L"
FT                   /id="PRO_0000373649"
FT   TOPO_DOM        32..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   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        58
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        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"
SQ   SEQUENCE   329 AA;  38463 MW;  CC6826FD08AC7E44 CRC64;
     MLRVFIFFVF LGSGLAGKVK SPITCKYFIS KNNTWYKYNV TILNDTIILP AYNTIPTNAT
     GISCTCHDID YLQKNNISIR YNTSILKTFQ DIRIIRCGMK NISEIAAGFS KELKFLDLRY
     NDLQFIEYNI LRKLIRSNTP TYLYYNNLMC GKRNCPLYYF LLKQEQTYLK LLPQFFLRRI
     SFSNNHTYLY HFLSCGNKPG HEFLEYQTKF CRTKFPEINI TVNQLIAKKN TERYKNCYPF
     VLVSIICSCI SSLFLLICLL RTICKKYSCT KQGKTTHSYI PLIPSYTFSL KKHRHPETAV
     VEDHASTANS PIVYIPTTEE KKVSCSRRK