EP153_ASFB7
ID EP153_ASFB7 Reviewed; 153 AA.
AC Q65150;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Lectin-like protein EP153R;
DE Short=pEP153R;
GN OrderedLocusNames=Ba71V-057; ORFNames=EP153R;
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 [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 [2]
RP FUNCTION, TOPOLOGY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10639320; DOI=10.1006/viro.1999.0080;
RA Galindo I., Almazan F., Bustos M.J., Vinuela E., Carrascosa A.L.;
RT "African swine fever virus EP153R open reading frame encodes a glycoprotein
RT involved in the hemadsorption of infected cells.";
RL Virology 266:340-351(2000).
RN [3]
RP FUNCTION.
RX PubMed=15262504; DOI=10.1016/j.virol.2004.05.019;
RA Hurtado C., Granja A.G., Bustos M.J., Nogal M.L., Gonzalez de Buitrago G.,
RA de Yebenes V.G., Salas M.L., Revilla Y., Carrascosa A.L.;
RT "The C-type lectin homologue gene (EP153R) of African swine fever virus
RT inhibits apoptosis both in virus infection and in heterologous
RT expression.";
RL Virology 326:160-170(2004).
RN [4]
RP DISULFIDE BOND, SUBUNIT, FUNCTION, MUTAGENESIS OF ARG-133, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21069396; DOI=10.1007/s00705-010-0846-2;
RA Hurtado C., Bustos M.J., Granja A.G., de Leon P., Sabina P.,
RA Lopez-Vinas E., Gomez-Puertas P., Revilla Y., Carrascosa A.L.;
RT "The African swine fever virus lectin EP153R modulates the surface membrane
RT expression of MHC class I antigens.";
RL Arch. Virol. 156:219-234(2011).
CC -!- FUNCTION: Down-regulates MHC-I expression by impairing the appropriate
CC configuration or presentation into the plasma membrane of the latter
CC (PubMed:21069396). Participates in viral hemadsorption, which may help
CC viral spread (PubMed:10639320). Reduces the transactivating activity of
CC host TP53, thus inhibiting apoptosis (PubMed:15262504). Non-essential
CC for virus growth in swine macrophage cell cultures (By similarity).
CC {ECO:0000250|UniProtKB:P0CA64, ECO:0000269|PubMed:10639320,
CC ECO:0000269|PubMed:15262504, ECO:0000269|PubMed:21069396}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21069396}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10639320, ECO:0000269|PubMed:21069396}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:10639320}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:10639320}.
CC -!- SIMILARITY: Belongs to the asfivirus lectin-like protein family.
CC {ECO:0000305}.
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DR EMBL; U18466; AAA65287.1; -; Genomic_DNA.
DR RefSeq; NP_042751.1; NC_001659.2.
DR SMR; Q65150; -.
DR DNASU; 1488822; -.
DR GeneID; 22220439; -.
DR KEGG; vg:22220439; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Early protein; Glycoprotein; Host endoplasmic reticulum;
KW Host membrane; Host-virus interaction; Lectin; Membrane;
KW Modulation of host cell apoptosis by virus; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..153
FT /note="Lectin-like protein EP153R"
FT /id="PRO_0000379080"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10639320"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..153
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10639320"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
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 107
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 67..78
FT /evidence="ECO:0000269|PubMed:21069396"
FT DISULFID 97..151
FT /evidence="ECO:0000269|PubMed:21069396"
FT MUTAGEN 133
FT /note="R->D: Complete loss of down-regulation of MHC-I
FT expression."
FT /evidence="ECO:0000269|PubMed:21069396"
FT MUTAGEN 133
FT /note="R->K: No effect on down-regulation of MHC-I
FT expression."
FT /evidence="ECO:0000269|PubMed:21069396"
SQ SEQUENCE 153 AA; 18050 MW; 35353D85C07EB69D CRC64;
MYFKKKYIGL IDKNCEKKIL DDSSTIKICY ILIGILIGTN MITLIYNFIF WDNYIKCYRN
NDKMFYCPND WVGYNNICYY FSNGSFSKNY TAASNFCRQL NGTLANNDTN LLNLTKIYNN
QSMYWVNNTV ILRGDNKYSQ KVNYTDLLFI CGK
