ID   GLYCO_LBV               Reviewed;         522 AA.
AC   Q8BDV6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   29-SEP-2021, entry version 49.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Lagos bat virus (LBV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=38766;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Nigeria/8619/1958;
RA   Bourhy H., Kassis R.;
RT   "Spatio-temporal localization of apoptosis involving caspase-8 activation
RT   governs the pathogenicity of lyssavirus infection.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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 (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   -!- SIMILARITY: Belongs to the lyssavirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AF429312; AAN63563.1; -; mRNA.
DR   SMR; Q8BDV6; -.
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   2: Evidence at transcript level;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Signal; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..522
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000299101"
FT   TOPO_DOM        26..455
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        477..522
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   LIPID           480
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   522 AA;  58667 MW;  00B97DAA5E32D4BE CRC64;
     MSQLNLIPFF CVIIVLSVED FPLYTIPEKI GPWTPIDLIH LSCPNNLQSE DEGCGTSSVF
     SYVELKTGYL THQKVSGFTC TGVVNEAVTY TNFVGYVTTT FKRKHFKPTA LACRDAYHWK
     ISGDPRYEES LHTPYPDNSW LRTVTTTKES LVIISPSIVE MDVYSRTLHS PMFPTGTCSR
     FYPSSPSCAT NHDYTLWLPD DPNLSLACDI FVTSTGKKSM NGSRMCGFTD ERGYYRTIKG
     ACKLTLCGKP GLRLFDGTWI SFPRPEVTTR CLPNQLVNIH NNRIDEVEHL IVEDLIRKRE
     ECLDTLETVL MSKSISFRRL SHFRKLVPGY GKAYTILNGS LMETNVHYLK VDNWSEILPS
     KGCLKINNQC VAHYKGVFFN GIIKGPDGHI LIPEMQSSLL KQHMDLLKAA VFPLKHPLIE
     PGSLFNKDGD ADEFVDVHMP DVHKLVSDVD LGLPDWSLYA LIGATIIAFF ILICLIRICC
     KKGGRRNSPT NRPDLPIGLS TTPQPKSKVI SSWESYKGTS NV