ID   GLYCO_RABVE             Reviewed;         524 AA.
AC   P03524; A3F5L8;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2026, entry version 104.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Rabies virus (strain ERA) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus; Rabies virus.
OX   NCBI_TaxID=11295;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6272128; DOI=10.1038/294275a0;
RA   Anilionis A., Wunner W.H., Curtis P.J.;
RT   "Structure of the glycoprotein gene in rabies virus.";
RL   Nature 294:275-278(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6897030; DOI=10.1016/0147-9571(82)90011-x;
RA   Anilionis A., Wunner W.H., Curtis P.J.;
RT   "Amino acid sequence of the rabies virus glycoprotein deduced from its
RT   cloned gene.";
RL   Comp. Immunol. Microbiol. Infect. Dis. 5:27-32(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=ERA 2007;
RA   Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
RA   Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E.,
RA   Cox J.H., Mueller T.;
RT   "Complete nucleotide sequencing of SAD derivatives of attenuated rabies
RT   virus vaccine strains.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 49-59; 169-179; 209-226 AND 337-354.
RC   STRAIN=CVS-11, RV194-2[F3], and RV231-22;
RX   PubMed=3966297; DOI=10.1016/0042-6822(85)90440-4;
RA   Wunner W.H., Dietzschold B., Smith C.L., Lafon M., Golub E.;
RT   "Antigenic variants of CVS rabies virus with altered glycosylation sites.";
RL   Virology 140:1-12(1985).
RN   [5]
RP   GLYCOSYLATION AT ASN-56; ASN-266 AND ASN-338.
RX   PubMed=1587845; DOI=10.1016/s0021-9258(19)50073-4;
RA   Shakin-Eshleman S.H., Remaley A.T., Eshleman J.R., Wunner W.H.,
RA   Spitalnik S.L.;
RT   "N-linked glycosylation of rabies virus glycoprotein. Individual sequons
RT   differ in their glycosylation efficiencies and influence on cell surface
RT   expression.";
RL   J. Biol. Chem. 267:10690-10698(1992).
RN   [6]
RP   GLYCOSYLATION.
RX   PubMed=9451021; DOI=10.1093/glycob/8.2.121;
RA   Wojczyk B.S., Stwora-Wojczyk M., Shakin-Eshleman S.H., Wunner W.H.,
RA   Spitalnik S.L.;
RT   "The role of site-specific N-glycosylation in secretion of soluble forms of
RT   rabies virus glycoprotein.";
RL   Glycobiology 8:121-130(1998).
RN   [7]
RP   INTERACTION WITH HOST CELL RECEPTORS.
RX   PubMed=15804965; DOI=10.1080/13550280590900427;
RA   Lafon M.;
RT   "Rabies virus receptors.";
RL   J. Neurovirol. 11:82-87(2005).
CC   -!- FUNCTION: Attaches the virus to host cellular receptor, inducing
CC       endocytosis of the virion by using different host proteins including
CC       TFRC, GRM2 and ITGB1 (By similarity). In the endosome, the acidic pH
CC       induces conformational changes in the glycoprotein trimer, which
CC       trigger fusion between virus and cell membrane. There is convincing in
CC       vitro evidence that the muscular form of the nicotinic acetylcholine
CC       receptor (nAChR), the neuronal cell adhesion molecule (NCAM), and the
CC       p75 neurotrophin receptor (p75NTR) bind glycoprotein and thereby
CC       facilitate rabies virus entry into cells (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P08667}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Interacts with matrix protein (By
CC       similarity). Interacts with host TRFC. Interacts with host BST2; this
CC       interaction inhibits viral budding by tethering new virions to the cell
CC       surface. Interacts with ITGB1. Interacts with host GRM2 (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08667}.
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.
CC       {ECO:0000269|PubMed:1587845, ECO:0000269|PubMed:9451021}.
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.
CC   -!- SIMILARITY: Belongs to the lyssavirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; J02293; AAA47204.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; M38452; AAA47209.1; -; Genomic_RNA.
DR   EMBL; EF206707; ABN11294.1; -; Genomic_RNA.
DR   EMBL; AH002403; AAA47191.1; -; Genomic_RNA.
DR   EMBL; AH002403; AAA47192.1; -; Genomic_RNA.
DR   EMBL; AH002403; AAA47193.1; -; Genomic_RNA.
DR   EMBL; AH002403; AAA47194.1; -; Genomic_RNA.
DR   EMBL; AH002404; AAA47195.1; -; Genomic_RNA.
DR   EMBL; AH002404; AAA47196.1; -; Genomic_RNA.
DR   EMBL; AH002404; AAA47197.1; -; Genomic_RNA.
DR   EMBL; AH002404; AAA47198.1; -; Genomic_RNA.
DR   EMBL; AH002405; AAA47205.1; -; Genomic_RNA.
DR   EMBL; AH002405; AAA47206.1; -; Genomic_RNA.
DR   EMBL; AH002405; AAA47207.1; -; Genomic_RNA.
DR   EMBL; AH002405; AAA47208.1; -; Genomic_RNA.
DR   PIR; A04121; VGVNG.
DR   PDB; 3NFK; X-ray; 1.43 A; C/D=512-524.
DR   SMR; P03524; -.
DR   ELM; P03524; -.
DR   ChEMBL; CHEMBL3856167; -.
DR   GlyCosmos; P03524; 3 sites, No reported glycans.
DR   iPTMnet; P03524; -.
DR   EvolutionaryTrace; P03524; -.
DR   Gene3D; 2.30.29.130; -; 1.
DR   InterPro; IPR055448; PH_Rhabdo_glycop.
DR   InterPro; IPR055447; Rhabdo_glycop_CD.
DR   InterPro; IPR001903; Rhabdo_glycop_FD.
DR   Pfam; PF24834; PH_Rhabdo_glycop; 1.
DR   Pfam; PF24833; Rhabdo_glycop_CD; 1.
DR   Pfam; PF00974; Rhabdo_glycop_FD; 1.
DR   SUPFAM; SSF161008; Viral glycoprotein ectodomain-like; 1.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0036338; C:viral membrane; ISS:UniProtKB.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; ISS:UniProtKB.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; ISS:UniProtKB.
DR   MDposit; P03524; -.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Signal; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   SIGNAL          1..19
FT   CHAIN           20..524
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000040993"
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   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:0000269|PubMed:1587845"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:1587845"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:1587845"
FT   DISULFID        43..302
FT                   /evidence="ECO:0000250|UniProtKB:P08667"
FT   DISULFID        54..226
FT                   /evidence="ECO:0000250|UniProtKB:P08667"
FT   DISULFID        80..113
FT                   /evidence="ECO:0000250|UniProtKB:P08667"
FT   DISULFID        178..188
FT                   /evidence="ECO:0000250|UniProtKB:P08667"
FT   DISULFID        208..247
FT                   /evidence="ECO:0000250|UniProtKB:P08667"
FT   DISULFID        242..271
FT                   /evidence="ECO:0000250|UniProtKB:P08667"
FT   DISULFID        363..370
FT                   /evidence="ECO:0000250|UniProtKB:P08667"
FT   VARIANT         27
FT                   /note="L -> P (in strain: ERA 2007)"
FT   VARIANT         55
FT                   /note="T -> I (in strain: CVS-11, RV194-2[F3] and
FT                   RV231-22)"
FT   VARIANT         177
FT                   /note="K -> N (in strain: RV194-2[F3])"
FT   VARIANT         217
FT                   /note="K -> E (in strain: RV231-22)"
FT   VARIANT         221..224
FT                   /note="KGSE -> NGNK (in strain: CVS-11, RV194-2[F3] and
FT                   RV231-22)"
FT   VARIANT         352
FT                   /note="R -> Q (in strain: RV194-2[F3])"
FT   STRAND          521..523
FT                   /evidence="ECO:0007829|PDB:3NFK"
SQ   SEQUENCE   524 AA;  58658 MW;  BBA53981C1175880 CRC64;
     MVPQALLFVP LLVFPLCFGK FPIYTILDKL GPWSPIDIHH LSCPNNLVVE DEGCTNLSGF
     SYMELKVGYI LAIKMNGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPTP DACRAAYNWK
     MAGDPRYEES LHNPYPDYRW LRTVKTTKES LVIISPSVAD LDPYDRSLHS RVFPSGKCSG
     VAVSSTYCST NHDYTIWMPE NPRLGMSCDI FTNSRGKRAS KGSETCGFVD ERGLYKSLKG
     ACKLKLCGVL GLRLMDGTWV AMQTSNETKW CPPDQLVNLH DFRSDEIEHL VVEELVRKRE
     ECLDALESIM TTKSVSFRRL SHLRKLVPGF GKAYTIFNKT LMEADAHYKS VRTWNEILPS
     KGCLRVGGRC HPHVNGVFFN GIILGPDGNV LIPEMQSSLL QQHMELLESS VIPLVHPLAD
     PSTVFKDGDE AEDFVEVHLP DVHNQVSGVD LGLPNWGKYV LLSAGALTAL MLIIFLMTCC
     RRVNRSEPTQ HNLRGTGREV SVTPQSGKII SSWESHKSGG ETRL
//