ID   GLYCO_RABVH             Reviewed;         524 AA.
AC   P19462; Q8B6J6;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   29-SEP-2021, entry version 77.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Rabies virus (strain HEP-Flury) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=11296;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2596027; DOI=10.1016/0042-6822(89)90559-x;
RA   Morimoto K., Ohkubo A., Kawai A.;
RT   "Structure and transcription of the glycoprotein gene of attenuated HEP-
RT   Flury strain of rabies virus.";
RL   Virology 173:465-477(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=HEP-Flury 2003;
RX   PubMed=12505638; DOI=10.1016/s0166-0934(02)00249-5;
RA   Inoue K., Shoji Y., Kurane I., Iijima T., Sakai T., Morimoto K.;
RT   "An improved method for recovering rabies virus from cloned cDNA.";
RL   J. Virol. Methods 107:229-236(2003).
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; M32751; AAA47213.1; -; Genomic_RNA.
DR   EMBL; AB085828; BAC53868.1; -; Genomic_RNA.
DR   PIR; A33745; VGVNRB.
DR   SMR; P19462; -.
DR   ABCD; P19462; 1 sequenced antibody.
DR   Proteomes; UP000006846; 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   CHAIN           20..524
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000040994"
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          487..506
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        56
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        177
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"
FT   VARIANT         14
FT                   /note="F -> S (in strain: HEP-Flury 2003)"
SQ   SEQUENCE   524 AA;  58583 MW;  DDFAAC610EAB9CE5 CRC64;
     MVPQVLLFAP LLVFPLCFGK FPIYTIPDKL GPWSPIDLHH LSCPNNLVVE DEGCTNLSGF
     SYMELKVGYI SAIKVNGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPTP DACRAAYNWK
     MAGDPRYEES LHNPYPDYHW LRTVKTTKES LVIISPSVTD LDPYDKSLHS RVFPGGNCSG
     ITVSSTYCST NHDYTIWMPE NLRLGTSCDI FTHSRGKRAS KGDKTCGFVD ERGLYKSLKG
     ACKLKLCGVL GLRLMDGTWV AMQTSDETKW CPPGQLVNLH DFRSDEIEHL VEEELVKKRE
     ECLDALESIM TTKSVSFRRL SHLRKLVPGF GKAYTIFNKT LMEADAHYKS VQTWNEIIPS
     KGCLRVGERC HPHVNGVFFN GIILGSDGHV LIPEMQSSLL QQHMELLESS VIPLMHPLAD
     PSTVFKDGDE VEDFVEVHLP DVHKQVSGVD LGLPKWGKYV LMIAGALIAL MLIIFLMTCC
     RRVNRPESTQ SNLGGTGRNV SVPSQSGKVI SSWESYKSGG ETRL