ID   GLYCO_ABLVB             Reviewed;         525 AA.
AC   Q9QSP1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-SEP-2021, entry version 58.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Australian bat lyssavirus (isolate Bat/AUS/1996) (ABLV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=446561;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH   NCBI_TaxID=328804; Pteropus conspicillatus (Spectacled flying fox).
OH   NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH   NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
OH   NCBI_TaxID=446909; Saccolaimus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12367747; DOI=10.1016/s0168-1702(02)00056-4;
RA   Gould A.R., Kattenbelt J.A., Gumley S.G., Lunt R.A.;
RT   "Characterisation of an Australian bat lyssavirus variant isolated from an
RT   insectivorous bat.";
RL   Virus Res. 89:1-28(2002).
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; AF081020; AAD47899.1; -; Genomic_RNA.
DR   RefSeq; NP_478342.1; NC_003243.1.
DR   SMR; Q9QSP1; -.
DR   GeneID; 926730; -.
DR   KEGG; vg:926730; -.
DR   Proteomes; UP000006934; 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                   /evidence="ECO:0000255"
FT   CHAIN           20..525
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000295792"
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..525
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          505..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   525 AA;  59131 MW;  19B7EA6FD8A628EF CRC64;
     MLLQVILLVS LTAILPCTGQ FPLYAIPDKL GPWSPIDIHH LSCPNNLIVE DEGCTSLSGF
     SYMELKVGFI TTIKVSGFTC TGVVTESETY TNFFGYVTTT FKRKHFRPTP ESCRKAYNWK
     IAGDPRYEES LHNPYPDYHW LRTVTTTKES LLIISPSVVD MDPYDKSLHS RMFPKGSCSG
     ASIPSVFCST NHDYTLWMPE DSNSGMSCDI FTMSKGKKAS KGGKVCGFVD ERGLYKSLKG
     ACKLKLCGIS GLRLLDGSWV SIQNHEEVKW CSPNQLVNIH DFNADEIEHL IVEELIKERE
     ECLDALESII TTKSVSFRRL SHLRKLVPGF GKAYTIINKT LMEADAHYKS VRTWDEIIPS
     KGCLKVREKC HPPYNGVFFN GIILGPDGQV LIPEMQSSLL HQHTELLESS VIPLIHPLAD
     PSTIFRGDDE AEGFIEVHLP DIQKQVSGID LGLSEWERYL IIGISAIILF ILAIIFTICC
     RRCKRRKKIR TDHIELDRKV SVTSQSGKSI PSWESYKSRQ GHSRS