ID   I329L_ASFPP             Reviewed;         329 AA.
AC   A9JM73;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Transmembrane protein I329L;
DE   Flags: Precursor;
GN   Name=I329L {ECO:0000312|EMBL:CAN10489.1};
OS   African swine fever virus (isolate Pig/Portugal/OURT88/1988) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=443878;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OURT 88/3 {ECO:0000312|EMBL:CAN10489.1};
RX   PubMed=18198370; DOI=10.1099/vir.0.83343-0;
RA   Chapman D.A.G., Tcherepanov V., Upton C., Dixon L.K.;
RT   "Comparison of the genome sequences of non-pathogenic and pathogenic
RT   African swine fever virus isolates.";
RL   J. Gen. Virol. 89:397-408(2008).
RN   [2]
RP   SIGNAL SEQUENCE CLEAVAGE SITE.
RX   PubMed=30279544; DOI=10.1038/s41598-018-32985-z;
RA   Kessler C., Forth J.H., Keil G.M., Mettenleiter T.C., Blome S., Karger A.;
RT   "The intracellular proteome of African swine fever virus.";
RL   Sci. Rep. 8:14714-14714(2018).
CC   -!- FUNCTION: Viral TLR3 homolog that probably prevents TLR3 dimerization
CC       and subsequent induction of IFN. Inhibits dsRNA-stimulated activation
CC       of NF-kB and IRF3. {ECO:0000250|UniProtKB:P27945}.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P27945}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P27945}. Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P27945}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P27945}.
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; AM712240; CAN10489.1; -; Genomic_DNA.
DR   Proteomes; UP000108903; 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   1: Evidence at protein level;
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; Repeat; Signal; Transmembrane; Transmembrane helix;
KW   Viral immunoevasion.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..329
FT                   /note="Transmembrane protein I329L"
FT                   /id="PRO_0000454844"
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                   /evidence="ECO:0000255"
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        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;  38542 MW;  B3B0F6CACA4273FB CRC64;
     MLRVFIFFVF LGSGLTGRIK PQVTCKYFIS ENNTWYKYNV TILNSSIILP AYNTIPSNAA
     GISCTCHDID YLQKNNISIH YNTSILKTFQ DIRIIRCGMK NISEIAGGFG KELKFLDLRY
     NDLQVIDYNI LRKLIRSNTP TYLYYNNLMC GKRNCPLYYF LLKQEQTYLK RLPQFFLRRI
     SFSNNNTYLY HFLSCGNKPG HEFLEYQTKY CRTKFPEINI TVNQLIAKKN TERYKSCYPL
     VFISILCSCI SFLFLFICLL RSICKKYSCT KQDKSSHNYI PLIPSYTFSL KKHRHPETAV
     VEDHTTSANS PIVYIPTTEE KKVSCSRRK