GLYCO_RABVV
ID GLYCO_RABVV Reviewed; 524 AA.
AC Q08089;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 23-FEB-2022, entry version 69.
DE RecName: Full=Glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Rabies virus (strain Vnukovo-32) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=45418;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7979981; DOI=10.1007/bf01310030;
RA Fodor I., Grabko V.I., Khozinski V.V., Selimov M.A.;
RT "Nucleotide and deduced amino acid sequences of the glycoprotein gene of
RT rabies virus vaccine strain Vnukovo-32.";
RL Arch. Virol. 135:451-459(1994).
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; X71879; CAA50713.1; -; mRNA.
DR PIR; S33419; S33419.
DR SMR; Q08089; -.
DR IntAct; Q08089; 1.
DR MINT; Q08089; -.
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_0000040998"
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 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; 58692 MW; 6DB36E50406CC16D CRC64;
MVPQALLFVP LLVFPLCFGK FPIYTIPDKL GPWSPIDIHH LSCPNNLVVE DEGCTNLSGF
SYMELKVGYI LAIKMNGFTC TGVVTEAENY TNFVGYVTTT FKRKHLRPTP DACRAAYNWK
MAGDPRYEES LHNPYPDYSW LRTVKTTKES LVIISPSVAD LDPYDRSLHS RVFPSGKCSG
VAVSSTYCST NHDYTIWMPE NPRLGKSCDI FTNSRGKRAS KGSETCGFVD ERGLYKSLKG
ACKLKLCGVL GLRLMDGTWV AMQTSNETKW CPPDQLVNLH DFRSDEIEHL VVEELVRKRE
ECLDALESIM TTKSVSFRRL SHLRKLVPGF GKAYTIFNKT LMEADAHYKS VRTWNEILPS
KGCLRVGGRC HPHVNGVFFN GIILGPDGNV LIPEMQSSLL QQHMELLESS VIPLVHPLAD
PSTVFKDGDE AEDFVEVHLP DVHNQVSGVD LGLPNWGKYV LLSAGALTAL MLIIFLMTCC
RRVNRSEPTQ HNLRGTGREV SVTPQTWKII SSWESHKSGG ETRL