ID   GLYCO_RABVB             Reviewed;         524 AA.
AC   Q66T62;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Rabies virus (strain silver-haired bat-associated) (RABV) (SHBRV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=445793;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15520387; DOI=10.1073/pnas.0407289101;
RA   Faber M., Pulmanausahakul R., Nagao K., Prosniak M., Rice A.B.,
RA   Koprowski H., Schnell M.J., Dietzschold B.;
RT   "Identification of viral genomic elements responsible for rabies virus
RT   neuroinvasiveness.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16328-16332(2004).
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. There is convincing in vitro evidence
CC       that the muscular form of the nicotinic acetylcholine receptor (nAChR),
CC       the neuronal cell adhesion molecule (NCAM), and the p75 neurotrophin
CC       receptor (p75NTR) bind glycoprotein and thereby facilitate rabies virus
CC       entry into cells (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   -!- BIOTECHNOLOGY: Primary surface antigen capable of inducing and reacting
CC       with virus-neutralizing antibodies. Almost all human and veterinary
CC       vaccines are based on the functional aspects of the G protein.
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; AY705373; AAU11518.1; -; Genomic_RNA.
DR   SMR; Q66T62; -.
DR   PRIDE; Q66T62; -.
DR   Proteomes; UP000006845; 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   1: Evidence at protein level;
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..524
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000295798"
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"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   524 AA;  58203 MW;  147D160F30CEDB4A CRC64;
     MIPQALLFVP LLIPSLCLGK FPIYTIPDKL GPWSPIDIHH LSCPNNLVVE DEGCTSLSGF
     SYMELKVGYI SAMKVNGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPMP DACRAAHDWK
     IAGDPRYEDS LQNPYPDYHW LRTVKTTKES LVIISPSVAD LDPYDKSLHS RVFPSGKCLG
     ITVSSTYCPT NHDYTIWMPV EARLGTSCDI FTNSRGKKAS KGGRTCGFVD ERGLYKSLKG
     ACKLKLCGVP GLRLMNGTWV SIQTSDDIKW CPPDQLVNLH DFHSDEIEHL VVEELIKKRE
     GCLDALESIM TTKSVSFRRL SHLRKLVPGF GKAYTIFNNT LMEADAHYKS VRTWNEVIPS
     KGCLKVGGRC HPPVNGVFFN GIILGPDGNV LIPEMQSSLL QQHMELLESS VIPLMHPLAD
     PSTVFKDGDE AEDFVEVHLP DVHKQVSDVD LGLPSWGKYL LMSAGALATL ILAIFLITCC
     RRANRTKSTQ RGHRESGGKV SVAPQNGKII SSWELYKSES ETGM