ID   GLYCO_EBLV1             Reviewed;         524 AA.
AC   A4UHQ1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   29-SEP-2021, entry version 41.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   European bat lyssavirus 1 (strain Bat/Germany/RV9/1968) (EBLV1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=453115;
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=17374776; DOI=10.1099/vir.0.82692-0;
RA   Marston D.A., McElhinney L.M., Johnson N., Muller T., Conzelmann K.K.,
RA   Tordo N., Fooks A.R.;
RT   "Comparative analysis of the full genome sequence of European bat
RT   lyssavirus type 1 and type 2 with other lyssaviruses and evidence for a
RT   conserved transcription termination and polyadenylation motif in the G-L 3'
RT   non-translated region.";
RL   J. Gen. Virol. 88:1302-1314(2007).
CC   -!- FUNCTION: Attaches the virus to host cellular receptor, inducing
CC       endocytosis of the virion. In the endosome, the acidic pH induces
CC       conformational changes in the glycoprotein trimer, which trigger fusion
CC       between virus and cell membrane (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. Interacts with matrix protein (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: Glycosylated and palmitoylated by host. Glycosylation is crucial
CC       for glycoprotein export at the cell surface (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Arg-352 is highly involved in rabies virus
CC       pathogenicity. Its mutation dramatically attenuates the virus (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lyssavirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; EF157976; ABO65246.1; -; Genomic_RNA.
DR   RefSeq; YP_001285391.1; NC_009527.1.
DR   SMR; A4UHQ1; -.
DR   GeneID; 5219909; -.
DR   KEGG; vg:5219909; -.
DR   Proteomes; UP000008926; Genome.
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   InterPro; IPR001903; Rhabd_glycop.
DR   Pfam; PF00974; Rhabdo_glycop; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..524
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000299099"
FT   TOPO_DOM        20..459
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        481..524
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   LIPID           480
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   524 AA;  58929 MW;  237795AA21550A2D CRC64;
     MLLSTAIFAF FLNCAPCLAK FPIYTIPDKI GPWSPIDINH LSCPNNLIVE DEGCTTLTPF
     SYMELKVGYI TTIKIEGFTC TGVITEAETY TNFVGYVTTT FKRKHFRPTV SACRDAYNWK
     ITGDPRYEES LHNPYPDSHW LRTVKTTKES LLIISPSVVD MDAYDKNLYS KMFPNGKCLA
     SPPSAICCPT NHDYTIWIPE NPKPGLSCDI FTTSKGKKAT KDGRLCGFVD ERGLYKSLKG
     ACKQRLCGVP GMRLMDGSWV SLQKTEAPEW CSPDQLVNVH DFHTDEIEHL VVEELVKKRE
     ECLDALETII TTKSISFRRL SHFRKLVPGF GKAYTLINKT LMEADAHYKS VREWKEVIPS
     KGCLMAGGRC HPHYSGIFFN GIILSPGGDV LIPEMQSALL QQHIELLESS MIPLRHPLAD
     PSTVFKRDDE AEDFVEVHLP DTQKLISGID LGFPEWKRYF LIGISVLALL ALAIITAACC
     KRFKRRRRPK PNPIELIRKV SVTSQSGRAI PSWESYKVGA TGES