ID   GLYCO_RABVC             Reviewed;         524 AA.
AC   O92284;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   29-SEP-2021, entry version 62.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Rabies virus (strain CVS-11) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=11294;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1588319; DOI=10.1099/0022-1317-73-5-1149;
RA   Sacramento D., Badrane H., Bourhy H., Tordo N.;
RT   "Molecular epidemiology of rabies virus in France: comparison with vaccine
RT   strains.";
RL   J. Gen. Virol. 73:1149-1158(1992).
RN   [2]
RP   PALMITOYLATION.
RX   PubMed=1871978; DOI=10.1016/0042-6822(91)90866-a;
RA   Gaudin Y., Tuffereau C., Benmansour A., Flamand A.;
RT   "Fatty acylation of rabies virus proteins.";
RL   Virology 184:441-444(1991).
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; AF085333; AAC34683.1; -; mRNA.
DR   PIR; PQ0370; PQ0370.
DR   SMR; O92284; -.
DR   ChEMBL; CHEMBL3988502; -.
DR   ABCD; O92284; 5 sequenced antibodies.
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_0000295799"
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        56
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   524 AA;  58864 MW;  6A2B93A899DB2CCC CRC64;
     MVPQVLLFVP LLGFSLCFGK FPIYTIPDKL GPWSPIDIHH LSCPNNLVVE DEGCTNLSEF
     SYMELKVGYI SAIKVNGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPTP DACRAAYNWK
     MAGDPRYEES LHNPYPDYHW LRTVRTTKES LIIISPSVTD LDPYDKSLHS RVFPGGKCSG
     ITVSSTYCST NHDYTIWMPE NPRPRTPCDI FTNSRGKRAS KGNKTCGFVD ERGLYKSLKG
     ACRLKLCGVL GLRLMDGTWV AMQTSDETKW CPPDQLVNLH DFRSDEIEHL VVEELVKKRE
     ECLDALESIM TTKSVSFRRL SHLRKLVPGF GKAYTIFNKT LMEADAHYKS VRTWNEIIPS
     KGCLKVGGRC HPHVNGVFFN GIILGPDGHV LIPEMQSSLL QQHMELLKSS VIPLMHPLAD
     PSTVFKEGDE AEDFVEVHLP DVYKQISGVD LGLPNWGKYV LMTAGAMIGL VLIFSLMTWC
     RRANRPESKQ RSFGGTGRNV SVTSQSGKVI PSWESYKSGG EIRL