ID   1101L_ASFWA             Reviewed;         269 AA.
AC   P0C9G1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Protein MGF 110-1L;
DE   Flags: Precursor;
GN   OrderedLocusNames=War-006;
OS   African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561444;
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: Plays a role in virus cell tropism, and may be required for
CC       efficient virus replication in macrophages. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Expressed in the immediate early phase of the viral
CC       replicative cycle. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the asfivirus MGF 110 family. {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; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000858; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR004848; ASFV_fam_110.
DR   Pfam; PF01639; v110; 2.
PE   3: Inferred from homology;
KW   Early protein; Glycoprotein; Host membrane; Membrane; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250|UniProtKB:A9JLI2"
FT   CHAIN           27..269
FT                   /note="Protein MGF 110-1L"
FT                   /id="PRO_0000373183"
FT   TOPO_DOM        27..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..269
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1..145
FT                   /note="A"
FT   REPEAT          147..269
FT                   /note="B"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   269 AA;  32605 MW;  B6B7F1662686999E CRC64;
     MLGLQIFTLL SIPTLLYTYE LELLDLTRTP PEKELEYWCT YANHCRFCWD CQDGICRNKV
     FENHSPILEN DYIANCSVFR RNEFCTYYVT SIKPHEVYRT ECPQQSHEWH EAVIRKWQKL
     LTYGFYLVGC VLVANYVRKR SLQTVMYLLV LLVIFFLLSQ LMLYRELEDK KHKIGSIPPK
     RELEHWCTHG KYCDFCWDCQ NGICRNKVFK NHPPIGENDF IRHDCWTIHL SNKCYYQKIY
     KYPDYHMMEC SQPTPYKWYD NLMKKQDIM