ID   GLYCO_ARAV              Reviewed;         526 AA.
AC   Q6X1D5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Aravan virus (ARAV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=211977;
OH   NCBI_TaxID=109482; Myotis blythii (Lesser mouse-eared bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=14602198; DOI=10.1016/s0168-1702(03)00217-x;
RA   Kuzmin I.V., Orciari L.A., Arai Y.T., Smith J.S., Hanlon C.A., Kameoka Y.,
RA   Rupprecht C.E.;
RT   "Bat lyssaviruses (Aravan and Khujand) from Central Asia: phylogenetic
RT   relationships according to N, P and G gene sequences.";
RL   Virus Res. 97:65-79(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18514350; DOI=10.1016/j.virusres.2008.04.021;
RA   Kuzmin I.V., Wu X., Tordo N., Rupprecht C.E.;
RT   "Complete genomes of Aravan, Khujand, Irkut and West Caucasian bat viruses,
RT   with special attention to the polymerase gene and non-coding regions.";
RL   Virus Res. 136:81-90(2008).
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; EF614259; AAP86775.1; -; Genomic_RNA.
DR   RefSeq; YP_007641395.1; NC_020808.1.
DR   SMR; Q6X1D5; -.
DR   GeneID; 14857928; -.
DR   KEGG; vg:14857928; -.
DR   Proteomes; UP000007445; 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..526
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000295794"
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..526
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   LIPID           480
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  59000 MW;  9700D997CE7899F3 CRC64;
     MPLQAIPLFS LILPVLVAGK FPIYTIPDKI GPWSPIDINH LSCPNNLVVE DEGCTTLTAF
     SYMELKVGYI TTIKVSGFTC TGVVTEAETY TNFVGYVTTT FRRKHFRPTA SACREAYNWK
     ATGDPRYEES LHNPYPDSHW LRTVKTTKES LLIISPSVAD MDAYDKALYS KIFPNGKCLG
     VSLSSPFCST NHDYTLWMPE NPKPGVSCDI FTTSKGKKAT KDGKLCGFVD ERGLYKSLKG
     ACKLKLCGVM GLRLMDGSWV SLQKTEESEW CSPNQLINIH DFHSDEIEHM VVEELVKKRE
     ECLDALESIM TTKSISFRRL SHLRKLVPGF GKAYTLINKT LMEADAHYKS VREWTEVIPS
     KGCLKAGGGC YPHYNRVFFN GIILSPDGHV LIPEMQSALL QQHIELLESS VIPLRHPLAD
     PSTVFKGDDE AEEFVEVHLP DTQKQISGID LGLPEWKRYF LMGMSAIGFL ALTIILAVCC
     RRIKRRKQSK PNPVELIRKV SVTSQSGRAI PSWESYKVKT GDQPQV