ID   GLYCO_WCBV              Reviewed;         525 AA.
AC   Q5VKN9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   29-SEP-2021, entry version 56.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   West Caucasian bat virus (WCBV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=249584;
OH   NCBI_TaxID=9433; Miniopterus schreibersii (Schreibers's long-fingered bat) (Vespertilio schreibersii).
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; EF614258; AAR03484.1; -; mRNA.
DR   RefSeq; YP_009094271.1; NC_025377.1.
DR   SMR; Q5VKN9; -.
DR   GeneID; 20964561; -.
DR   KEGG; vg:20964561; -.
DR   Proteomes; UP000095862; 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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..525
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000295804"
FT   TOPO_DOM        18..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   LIPID           480
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   525 AA;  59594 MW;  DB91CA3263FE210A CRC64;
     MASYFALVLN GISMVFSQGL FPLYTIPDHL GPWTPIDLSH LHCPNNLYTD ASYCTTEQSI
     TYTELKVGSS VSQKIPGFTC TGVRTESVTY TNFVGYVTTT FKKKHFPPKS RDCREAYERK
     KAGDPRYEES LAHPYPDNSW LRTVTTTKDS WVIIEPSVVE LDIYTSALYS PLFKDGTCSK
     SRTYSPYCPT NHDFTIWMPE SENIRSACNL FSTSRGKLVR NRTSTCGIID ERGLFRSVKG
     ACKISICGRQ GIRLVDGTWM SFRYSEYLPV CSPSQLINTH DIKVDELENA IVLDLIRRRE
     ECLDTLETIL MSGSVSHRRL SHFRKLVPGS GKAYSYINGT LMESDAHYIK VENWSEVIPH
     KGCLMVGGKC YEPVNDVYFN GIIRDSNNQI LIPEMQSSLL REHVDLLKAN IVPFRHPMLL
     RSFTSDTEED IVEFVNPHLQ DTQKLVSDMD LGLSDWKRYL LIGSLAVGGV VAILFIGTCC
     LRCRAGRNRR TIRSNHRSLS HDVVFHKDKD KVITSWESYK GQTAQ