ID   EP153_ASFK5             Reviewed;         158 AA.
AC   P0CA63;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Lectin-like protein EP153R;
DE            Short=pEP153R;
GN   OrderedLocusNames=Ken-069;
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: 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 (By similarity).
CC       {ECO:0000250|UniProtKB:P0CA64, ECO:0000250|UniProtKB:Q65150}.
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       Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000250|UniProtKB:Q65150}.
CC   -!- SIMILARITY: Belongs to the asfivirus lectin-like protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0CA63; -.
DR   PRIDE; P0CA63; -.
DR   Proteomes; UP000000861; 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; Lectin; Membrane;
KW   Modulation of host cell apoptosis by virus; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..158
FT                   /note="Lectin-like protein EP153R"
FT                   /id="PRO_0000373539"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q65150"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..158
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q65150"
FT   REGION          61..157
FT                   /note="Lectin-like"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..72
FT                   /evidence="ECO:0000250|UniProtKB:Q65150"
SQ   SEQUENCE   158 AA;  18674 MW;  138E8F326291DD53 CRC64;
     MFLNKKYPSL IEKKMDDLMT LKFCYLIITF LIITNIFSLA INIWGGGDMI DRQSCENIFY
     CPKDWVGYNN ACYYFSNNNK NYTDANNYCK NSHNSTLANN DTKLLNLTKL LNLSKLYYND
     STYWVKYSLP KNKAVTLRNS TYKYDRVKYT ETFFICSN