VF475_ASFB7
ID VF475_ASFB7 Reviewed; 475 AA.
AC Q65167;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 60.
DE RecName: Full=Uncharacterized protein B475L;
DE Short=pB475L;
GN OrderedLocusNames=Ba71V-077; ORFNames=B475L;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [2]
RP INDUCTION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:32075923}.
CC -!- SIMILARITY: Belongs to the asfivirus B475L family. {ECO:0000305}.
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DR EMBL; U18466; AAA65307.1; -; Genomic_DNA.
DR RefSeq; NP_042771.1; NC_001659.2.
DR SMR; Q65167; -.
DR GeneID; 22220307; -.
DR KEGG; vg:22220307; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Coiled coil; Glycoprotein; Host membrane; Late protein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..475
FT /note="Uncharacterized protein B475L"
FT /id="PRO_0000373695"
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 295..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 183..233
FT /evidence="ECO:0000255"
FT COMPBIAS 295..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 475 AA; 56068 MW; 682FCB97CBC13D8F CRC64;
MDQEESHVIS IFETLGAYFI NIFYNFLYKN ALYKKHSIVT EYQYQVKGYI LGVKQNKKLY
EKMLDSFYKY FCNITQINSK TLNFSNFITT IVDSFIPKEY SQSISLEKKE SILELLLCDY
ISNLGTFITT EKMLPFIIKN RKENYHKVTK EMQDYSLTFL LKKRMELYNK FLRKQAYVEP
ETELEETYAR LSSYNRSLLH QIEELTSEKK SLLADLSTLR KKYEKRQSEY RRLVQLLYQQ
IQRSSTSKSS YPLTKFIETL PSEHFSNEEY QKETPADQKE VVEMELLRKQ ELLTSQELTS
KSPNNYPVPH SRTIVSKPPD NYPVPRSRTT TKLDFDNSLQ NQELHTKNGF SEKDIVEFGQ
DKPEEENILA IDQDKPEEEN ILAIKQDIPE EENILAIDQD KPEFNQDTPE FKEAVLDTKE
NILEEENQDE PIVQNPFLEN FWKPEQKTFN QSGLFEESSN FSNDWSGGDV TLNFS