EP153_ASFP4
ID EP153_ASFP4 Reviewed; 155 AA.
AC O89335;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Lectin-like protein EP153R;
DE Short=pEP153R;
GN OrderedLocusNames=Pret-069;
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 [GENOMIC DNA].
RX PubMed=10573162; DOI=10.1099/0022-1317-80-10-2693;
RA Neilan J.G., Borca M.V., Lu Z., Kutish G.F., Kleiboeker S.B., Carrillo C.,
RA Zsak L., Rock D.L.;
RT "An African swine fever virus ORF with similarity to C-type lectins is non-
RT essential for growth in swine macrophages in vitro and for virus virulence
RT in domestic swine.";
RL J. Gen. Virol. 80:2693-2697(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Scoles G.A., Kleiboeker S.B., Lu Z., Kutish G.F., Rock D.L.;
RT "The African swine fever virus C-type lectin (8CR) or CD2 (8DR) like genes
RT are nonessential for infection and persistence in the tick host.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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: Down-regulates MHC-I expression by impairing the appropriate
CC configuration or presentation into the plasma membrane of the latter
CC (By similarity). Participates in viral hemadsorption, which may help
CC viral spread (By similarity). Reduces the transactivating activity of
CC host TP53, thus inhibiting apoptosis (By similarity). Non-essential for
CC virus growth in swine macrophage cell cultures (PubMed:10573162).
CC {ECO:0000250|UniProtKB:Q65150, ECO:0000269|PubMed:10573162}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q65150}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q65150}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q65150}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle
CC (By similarity). Expressed in the late phase of the viral replicative
CC cycle (By similarity). {ECO:0000250|UniProtKB:Q65150}.
CC -!- SIMILARITY: Belongs to the asfivirus lectin-like protein family.
CC {ECO:0000305}.
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DR EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF017036; AAC28421.1; -; Genomic_DNA.
DR EMBL; AF050111; AAF24969.1; -; Genomic_DNA.
DR SMR; O89335; -.
DR Proteomes; UP000000859; 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 3: Inferred from homology;
KW Disulfide bond; Early protein; Glycoprotein; Host endoplasmic reticulum;
KW Host membrane; Host-virus interaction; Late protein; Lectin; Membrane;
KW Modulation of host cell apoptosis by virus; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..155
FT /note="Lectin-like protein EP153R"
FT /id="PRO_0000373541"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q65150"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..155
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q65150"
FT REGION 66..154
FT /note="Lectin-like"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 66..77
FT /evidence="ECO:0000250|UniProtKB:Q65150"
FT DISULFID 94..153
FT /evidence="ECO:0000250|UniProtKB:Q65150"
SQ SEQUENCE 155 AA; 18493 MW; 142C3B09594BE0D2 CRC64;
MYFKKKYIGL IDKNCEKKIL DDCTTIKICY ILIGILIGTN MITLIYNFIF WDHYMTCNKK
DKMFYCPKDW VGYNNVCYYF NNDSKNYTTA TNSCKQLNST LANNDTNLLN LTKVYHHDKL
YWVNYSLNDN FSLSLRNSTY EKRSKYLPLL FICSK
