ID   GLYCO_IRKV              Reviewed;         524 AA.
AC   Q5VKP3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Irkut virus (IRKV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=249583;
OH   NCBI_TaxID=187017; Murina leucogaster (Greater tube-nosed bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15896400; DOI=10.1016/j.virusres.2005.03.008;
RA   Kuzmin I.V., Hughes G.J., Botvinkin A.D., Orciari L.A., Rupprecht C.E.;
RT   "Phylogenetic relationships of Irkut and West Caucasian bat viruses within
RT   the Lyssavirus genus and suggested quantitative criteria based on the N
RT   gene sequence for lyssavirus genotype definition.";
RL   Virus Res. 111:28-43(2005).
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; EF614260; AAR03480.1; -; mRNA.
DR   RefSeq; YP_007641400.1; NC_020809.1.
DR   SMR; Q5VKP3; -.
DR   GeneID; 14857934; -.
DR   KEGG; vg:14857934; -.
DR   Proteomes; UP000008381; 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..524
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000295795"
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   REGION          504..524
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   524 AA;  58831 MW;  E458EE1E41CD0761 CRC64;
     MSLLTAVIAF LFISTFCSGK FPIYTIPDKI GPWSPIDINH LSCPNNLEVE DEGCTTLTAF
     NYMELKVGYI TSIKVDGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPNV SACRAAFSWK
     TAGDPRYEES LHNPYPDSHW LRTVTTTKES LLIISPSVVD MDAYDKTLYS KMFPNGKCFP
     PISDSPFCST NHDYTLWLPE KEKLSMSCNI FVSSKGKKAT KDGRLCGFVD ERGLYKSLKG
     ACKLKLCGMA GMRLMDGSWV SLQRADAPEW CPPGALVNVH DFHSDEIAHF VVEELIKKRE
     ECLDTLETIL TTKSISFRRL SHFRKLVPGL GKAYTLINNT LMEAEAHYKS IREWKEIIPS
     KGCLKAGGRC HPHYDGIFFN GIILGPNGDV LIPEMQSSLL QQHIELLESS MIPLRHPLAD
     SSAIFRSDNE AEDFVDVHLP DTQKQVSDID LGFPEWKRYF LIGVSAIALF SLAIIIAVCC
     RKFKRRKRPK PGPIELVRKV SVTSQSGKVV PSWESYKEGA TSQP