ID   GLYCO_RABVP             Reviewed;         524 AA.
AC   P08667;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Rabies virus (strain Pasteur vaccins / PV) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=103929;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3459163; DOI=10.1073/pnas.83.11.3914;
RA   Tordo N., Poch O., Ermine A., Keith G., Rougeon F.;
RT   "Walking along the rabies genome: is the large G-L intergenic region a
RT   remnant gene?";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3914-3918(1986).
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; M13215; AAA47218.1; -; Genomic_RNA.
DR   PIR; C26275; VGVNRV.
DR   RefSeq; NP_056796.1; NC_001542.1.
DR   SMR; P08667; -.
DR   DrugBank; DB11603; Rabies immune globulin, human.
DR   ABCD; P08667; 147 sequenced antibodies.
DR   DNASU; 1489856; -.
DR   GeneID; 1489856; -.
DR   KEGG; vg:1489856; -.
DR   Proteomes; UP000008649; 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; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT   SIGNAL          1..19
FT   CHAIN           20..524
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000040995"
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           479
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:0000250"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   524 AA;  58535 MW;  EACF34361F2AEFE3 CRC64;
     MVPQALLFVP LLVFPLCFGK FPIYTIPDKL GPWSPIDIHH LSCPNNLVVE DEGCTNLSGF
     SYMELKVGYI SAIKMNGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPTP DACRAAYNWK
     MAGDPRYEES LHNPYPDYHW LRTVKTTKES LVIISPSVAD LDPYDRSLHS RVFPGGNCSG
     VAVSSTYCST NHDYTIWMPE NPRLGMSCDI FTNSRGKRAS KGSETCGFVD ERGLYKSLKG
     ACKLKLCGVL GLRLMDGTWV AMQTSNETKW CPPGQLVNLH DFRSDEIEHL VVEELVKKRE
     ECLDALESIM TTKSVSFRRL SHLRKLVPGF GKAYTIFNKT LMEADAHYKS VRTWNEIIPS
     KGCLRVGGRC HPHVNGVFFN GIILGPDGNV LIPEMQSSLL QQHMELLVSS VIPLMHPLAD
     PSTVFKNGDE AEDFVEVHLP DVHERISGVD LGLPNWGKYV LLSAGALTAL MLIIFLMTCW
     RRVNRSEPTQ HNLRGTGREV SVTPQSGKII SSWESYKSGG ETGL