I329L_ASFB7
ID I329L_ASFB7 Reviewed; 329 AA.
AC P27945;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Transmembrane protein I329L;
DE Flags: Precursor;
GN OrderedLocusNames=BA71V-142; ORFNames=I329L;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1309282; DOI=10.1016/0042-6822(92)90059-x;
RA Rodriguez J.M., Salas M.L., Vinuela E.;
RT "Genes homologous to ubiquitin-conjugating proteins and eukaryotic
RT transcription factor SII in African swine fever virus.";
RL Virology 186:40-52(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [3]
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21203785; DOI=10.1007/s00705-010-0894-7;
RA de Oliveira V.L., Almeida S.C., Soares H.R., Crespo A., Marshall-Clarke S.,
RA Parkhouse R.M.;
RT "A novel TLR3 inhibitor encoded by African swine fever virus (ASFV).";
RL Arch. Virol. 156:597-609(2011).
RN [4]
RP FUNCTION, AND DOMAIN.
RX PubMed=21280117; DOI=10.1002/pro.554;
RA Henriques E.S., Brito R.M., Soares H., Ventura S., de Oliveira V.L.,
RA Parkhouse R.M.;
RT "Modeling of the Toll-like receptor 3 and a putative Toll-like receptor 3
RT antagonist encoded by the African swine fever virus.";
RL Protein Sci. 20:247-255(2011).
RN [5]
RP REVIEW.
RX PubMed=23041356; DOI=10.1016/j.virusres.2012.09.014;
RA Rodriguez J.M., Salas M.L.;
RT "African swine fever virus transcription.";
RL Virus Res. 173:15-28(2013).
CC -!- FUNCTION: Viral TLR3 homolog that probably prevents TLR3 dimerization
CC and subsequent induction of IFN (PubMed:21280117, PubMed:21203785).
CC Inhibits dsRNA-stimulated activation of NF-kB and IRF3
CC (PubMed:21203785). {ECO:0000269|PubMed:21203785,
CC ECO:0000269|PubMed:21280117}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21203785}; 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:0000303|PubMed:23041356}.
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:0000269|PubMed:21280117}.
CC -!- PTM: Highly glycosylated. {ECO:0000269|PubMed:21203785}.
CC -!- SIMILARITY: Belongs to the asfivirus I329L family. {ECO:0000305}.
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DR EMBL; M77121; AAA42702.1; -; Genomic_DNA.
DR EMBL; U18466; AAA65369.1; -; Genomic_DNA.
DR PIR; D39448; WMXFB4.
DR RefSeq; NP_042833.1; NC_001659.2.
DR GeneID; 22220369; -.
DR KEGG; vg:22220369; -.
DR Proteomes; UP000000624; 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; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral immunoevasion.
FT SIGNAL 1..31
FT /evidence="ECO:0000250|UniProtKB:A9JM73"
FT CHAIN 32..329
FT /note="Transmembrane protein I329L"
FT /id="PRO_0000036743"
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 REPEAT 112..133
FT /note="LRR"
FT /evidence="ECO:0000305|PubMed:21280117"
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:0000269|PubMed:21280117"
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
