ID   GLYCO_RABVI             Reviewed;         524 AA.
AC   A3RM22; Q58FH1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   29-SEP-2021, entry version 39.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Rabies virus (strain India) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=445790;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Germany;
RA   Pfefferle S., Panning M., Drosten C.;
RT   "Virological characterization of cases of transplantation-associated Rabies
RT   in Germany.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Desai A., Nagaraja T., Muhamuda K., Madhusudana S., Ravi V.;
RT   "Complete nucleotide sequencing of an Indian isolate of Rabies virus.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; AY956319; AAX56084.1; -; Genomic_RNA.
DR   EMBL; EF437215; ABO15579.1; -; Genomic_RNA.
DR   SMR; A3RM22; -.
DR   Proteomes; UP000008620; Genome.
DR   Proteomes; UP000008996; 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_0000295801"
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:0000250"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
FT   VARIANT         5
FT                   /note="V -> A (in strain: Isolate Germany)"
FT   VARIANT         14
FT                   /note="F -> V (in strain: Isolate Germany)"
FT   VARIANT         26
FT                   /note="I -> V (in strain: Isolate Germany)"
FT   VARIANT         311
FT                   /note="A -> T (in strain: Isolate Germany)"
FT   VARIANT         446
FT                   /note="I -> V (in strain: Isolate Germany)"
FT   VARIANT         481
FT                   /note="G -> R (in strain: Isolate Germany)"
SQ   SEQUENCE   524 AA;  58365 MW;  BF1351839A799CD6 CRC64;
     MVPQVLLFVP LLVFSMCFGK FPIYTIPDKL GPWSPIDIHH LSCPNNLVVE DEGCTNLSGF
     SYMELKVGYI SAIKVNGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPTP DACRAAYNWK
     MAGDPRYEES LHNPYPDYHW LRTVKTTKES LVIISPSVAD LDPYDKSLHS RVFPSGKCSG
     ITISSTYCST NHDYTIWMPE NPRLGTSCDI FTNSRGKRAS KGGKTCGFVD ERGLYKSLKG
     ACKLKLCGVL GLRLMDGTWV AMQTSDETKW CPPDQLVNLH DFRSDEIEHL VVEELVKKRE
     ECLDALESIM ATKSVSFRRL SHLRKLVPGF GKAYTIFNKT LMEADAHYKS VRTWNEIIPS
     KGCLRVGGRC HPHVNGVFFN GIILGPDGHV LIPEMQSSLL QQHMELLESS VIPLMHPLAD
     PSTVFKDGDE AEDFVEVHLP DVHKQISGVD LGLPSWGKYV LVSAGVLVVL MLTIFIMTCC
     GRVHRPKSTQ HGLGGTGRKV SVTSQSGKVI SSWESYKSGG ETRL