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GLYCO_DMSVA
ID   GLYCO_DMSVA             Reviewed;         561 AA.
AC   A7WNB3;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   23-FEB-2022, entry version 31.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Drosophila melanogaster sigma virus (isolate Drosophila/USA/AP30/2005)
OS   (DMelSV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Sigmavirus.
OX   NCBI_TaxID=666363;
OH   NCBI_TaxID=7227; Drosophila melanogaster (Fruit fly).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=AP30;
RX   PubMed=17725574; DOI=10.1111/j.1365-294x.2007.03460.x;
RA   Carpenter J.A., Obbard D.J., Maside X., Jiggins F.M.;
RT   "The recent spread of a vertically transmitted virus through populations of
RT   Drosophila melanogaster.";
RL   Mol. Ecol. 16:3947-3954(2007).
CC   -!- FUNCTION: Attaches the virus to host receptors, inducing clathrin-
CC       dependent endocytosis of the virion. {ECO:0000250|UniProtKB:P03522}.
CC   -!- FUNCTION: In the endosome, the acidic pH induces conformational changes
CC       in the glycoprotein trimer, which trigger fusion between virus and
CC       endosomal membrane. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P03522};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P03522}.
CC       Host membrane {ECO:0000250|UniProtKB:P03522}; Single-pass type I
CC       membrane protein {ECO:0000250|UniProtKB:P03522}.
CC   -!- PTM: Glycosylated by host. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AM689309; CAM82926.2; -; Genomic_RNA.
DR   RefSeq; YP_003126912.1; NC_013135.1.
DR   SMR; A7WNB3; -.
DR   GeneID; 8363509; -.
DR   KEGG; vg:8363509; -.
DR   Proteomes; UP000029768; 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   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR001903; Rhabd_glycop.
DR   Pfam; PF00974; Rhabdo_glycop; 1.
PE   3: Inferred from homology;
KW   Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Host membrane;
KW   Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..561
FT                   /note="Glycoprotein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432051"
FT   TOPO_DOM        31..495
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        496..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        531..561
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   DISULFID        59..327
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        104..150
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..261
FT                   /evidence="ECO:0000250"
FT   DISULFID        256..296
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   561 AA;  63553 MW;  81D1D05E7392FF9C CRC64;
     MAHYELHVLF VHSWMLALIL ITTLVWLAAS QKAFTPDLVF PEMNRNSSWS VANYGEILCP
     TSFQSYDPKK HQILTRVLVE RPSLNTDTKV EGYTCHKVKY ETICDMPWYF SPTISHSISP
     LRVKESECKD AIAEHQLGTH VPLSFPPEDC SWNSVNTKEY EDIIVKEHPV MLDPYTNNYV
     DAIFPGGISS PGMGGTIHDD MMWVSKDLAV SPECSGWQRS MGLIYSSRLY GEREPMLEVG
     SIHIEGHRDK NLTLACRISF CGEIGVRFHD GEWMKVSVNL DHPNSVTFQV TDFPPCPPGT
     TIQTAVVENI NPEIQELTVN MMYRLKCQET ISKMVSGLPT SALDLSYLIQ VQEGPGIVYK
     REKGILYQSV GMYQYIDTVT LNKEENQLGE NSRGQKVFWT EWSDSPTRPG LQEGINGIVK
     YEGQVRVPLG MSLRLEAATE LMWGHPVHTV SHPILHVISN HTEQSVTTWN RGVNSTNLIG
     LATRSISGFY DNLKLYLILA LIFVSLIALV VLDVIPFKYI LFVLCPPLLL CRFIKCSRRK
     PETRDRYHVE YNRPGQVSSA F
 
 
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