ID   EP153_ASFM2             Reviewed;         161 AA.
AC   P0CA64;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Lectin-like protein EP153R;
DE            Short=pEP153R;
GN   OrderedLocusNames=Mal-065;
OS   African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10500;
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.
RN   [2]
RP   INDUCTION, AND FUNCTION.
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).
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       (Probable). Expressed in the late phase of the viral replicative cycle
CC       (PubMed:10573162). {ECO:0000269|PubMed:10573162, ECO:0000305}.
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; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0CA64; -.
DR   Proteomes; UP000000860; 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: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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Host endoplasmic reticulum; Host membrane;
KW   Host-virus interaction; Late protein; Membrane;
KW   Modulation of host cell apoptosis by virus; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..161
FT                   /note="Lectin-like protein EP153R"
FT                   /id="PRO_0000373540"
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..161
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q65150"
FT   REGION          66..160
FT                   /note="Lectin-like"
FT   CARBOHYD        89
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        116
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        136
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..159
FT                   /evidence="ECO:0000250|UniProtKB:Q65150"
SQ   SEQUENCE   161 AA;  19052 MW;  C2C57C4E692B2C58 CRC64;
     MFSNKKYIGL IDKYCEKKIL DDSSTIKICY ILIGILIGTN MITLIYNFIF WENYITCNQK
     DKTFYCPKDW VGYNNVCYYF GNDEKNYNNA SNYCKQLNST LTNNNTNLVN LTKTLNLTKT
     YNHESNYWVN YSLIKNESVL LRNSGYYKKQ KHVSLLYICS K