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