ID   1101L_ASFPP             Reviewed;         270 AA.
AC   A9JLI2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Protein MGF 110-1L;
DE   Flags: Precursor;
GN   Name=MGF 110-1L {ECO:0000312|EMBL:CAN10356.1};
OS   African swine fever virus (isolate Pig/Portugal/OURT88/1988) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=443878;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OURT 88/3 {ECO:0000312|EMBL:CAN10356.1};
RX   PubMed=18198370; DOI=10.1099/vir.0.83343-0;
RA   Chapman D.A.G., Tcherepanov V., Upton C., Dixon L.K.;
RT   "Comparison of the genome sequences of non-pathogenic and pathogenic
RT   African swine fever virus isolates.";
RL   J. Gen. Virol. 89:397-408(2008).
RN   [2]
RP   SIGNAL SEQUENCE CLEAVAGE SITE.
RX   PubMed=30279544; DOI=10.1038/s41598-018-32985-z;
RA   Kessler C., Forth J.H., Keil G.M., Mettenleiter T.C., Blome S., Karger A.;
RT   "The intracellular proteome of African swine fever virus.";
RL   Sci. Rep. 8:14714-14714(2018).
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: Membrane {ECO:0000250|UniProtKB:P18560}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P18560}.
CC   -!- SIMILARITY: Belongs to the asfivirus MGF 110 family. {ECO:0000305}.
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DR   EMBL; AM712240; CAN10356.1; -; Genomic_DNA.
DR   Proteomes; UP000108903; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR004848; ASFV_fam_110.
DR   Pfam; PF01639; v110; 2.
PE   1: Evidence at protein level;
KW   Early protein; Glycoprotein; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:30279544"
FT   CHAIN           27..270
FT                   /note="Protein MGF 110-1L"
FT                   /id="PRO_0000454840"
FT   TOPO_DOM        27..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..270
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REPEAT          27..146
FT                   /note="A"
FT                   /evidence="ECO:0000250|UniProtKB:P18560"
FT   REPEAT          147..270
FT                   /note="B"
FT                   /evidence="ECO:0000250|UniProtKB:P18560"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   270 AA;  32396 MW;  C174EC7EB6AB6AF2 CRC64;
     MLGLQIFTLL SIPTLLYTYE IEPLERTSTP PEKEFGYWCT YANHCRFCWD CQDGICRNKA
     FKNHSPILEN DYIANCSIYR RNDFCIYHIT SIKPHKTYRT ECPQHINHER HEADIRKWQK
     LLTYGFYLAG CILAVNYIRK RSLQTVMYLL VFLVISFLLS QLMLYGELED KKHKIGSIPP
     KRELEHWCTH GKYCNFCWDC QNGICKNKAF KNHPPIGEND FIRYDCWTTH LPNKCSYEKI
     YKHFDTHIME CSQPTHFKWY DNLMKKQDIM