ID   GLYCO_DUVV              Reviewed;         533 AA.
AC   Q91C28; Q49AV0; Q8QPE3; Q8QPE4; Q8QPE5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   29-SEP-2021, entry version 58.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Duvenhage virus (DUVV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=38767;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11238853; DOI=10.1128/jvi.75.7.3268-3276.2001;
RA   Badrane H., Bahloul C., Perrin P., Tordo N.;
RT   "Evidence of two Lyssavirus phylogroups with distinct pathogenicity and
RT   immunogenicity.";
RL   J. Virol. 75:3268-3276(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 77-214.
RC   STRAIN=Human/South Africa/Rv6, Isolate Bat/South Africa/Rv139, and
RC   Isolate Bat/Zimbabwe/Rv131;
RX   PubMed=12417947; DOI=10.1007/s00705-002-0877-4;
RA   Johnson N., McElhinney L.M., Smith J., Lowings P., Fooks A.R.;
RT   "Phylogenetic comparison of the genus Lyssavirus using distal coding
RT   sequences of the glycoprotein and nucleoprotein genes.";
RL   Arch. Virol. 147:2111-2123(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-524.
RC   STRAIN=94286.DUV;
RX   PubMed=16051841; DOI=10.1128/jvi.79.16.10487-10497.2005;
RA   Davis P.L., Holmes E.C., Larrous F., Van der Poel W.H., Tjornehoj K.,
RA   Alonso W.J., Bourhy H.;
RT   "Phylogeography, population dynamics, and molecular evolution of European
RT   bat lyssaviruses.";
RL   J. Virol. 79:10487-10497(2005).
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; AF298147; AAK97862.1; -; Genomic_RNA.
DR   EMBL; AY062055; AAL47595.1; -; Genomic_RNA.
DR   EMBL; AY062056; AAL47596.1; -; Genomic_RNA.
DR   EMBL; AY062057; AAL47597.1; -; Genomic_RNA.
DR   EMBL; AY996322; AAY53551.1; -; Genomic_RNA.
DR   SMR; Q91C28; -.
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; Signal; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..533
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000299098"
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..533
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          492..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           480
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   VARIANT         172..177
FT                   /note="IVSNGR -> MFPNGK (in strain: Isolate Bat/Zimbabwe/
FT                   Rv131)"
FT   VARIANT         172..174
FT                   /note="IVS -> MFP (in strain: Isolate Bat/South Africa/
FT                   Rv139 and Human/South Africa/Rv6)"
SQ   SEQUENCE   533 AA;  59716 MW;  B022632E566B93B2 CRC64;
     MPLNAVIFTL LLRCSICLGK FPFYTIPDKL GPWSPIDIHH LSCPNNLVVE DEGCTTLTPF
     SYMELKVGYI TSIKVSGFTC TGVVTEAETY TNFVGYVTTT FRRRHFRPSV NSCRDAYNWK
     IAGDPRYEES LHNPYPDSHW LRTVKTTKES LLIISPSVAD MDAYDKKLYS KIVSNGRCSE
     ISPGSPFCPT NHEYTIWMPE SSNPGISCDI FTRSMGKKAT KDGQLCGFVD ERGLYKSLKG
     ACRLRLCGIS GLRLMDGSWV SLPQVNNSEW CSPDQLVNIH DFHSDEIEHL VADELVKKRE
     DCLDALETIL FTKSISFRRL SHLRKLVPGF GKAYTIINRT LMEAEAHYKS VREWKEIIPS
     KGCLKAGGRC YPHHNGIFFN GIILGPGGEI LIPEMQSALL QQHIELLESS VVPLKHPLAD
     PSTVFKNDDE AESFVDVHLP DTNQKISGID LGLPEWKRYF LIGVSAVALL ALSIIIAVCC
     KRFRKRKKSK PGPVELTRKV SVISKGNGPV PSWESYKEGT TGDVRNTTPS TRE