GLYCO_RABVE
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 25-MAY-2022, entry version 93.
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.
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. 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.
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.
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; K02858; AAA47191.1; -; Genomic_RNA.
DR EMBL; K02859; AAA47192.1; -; Genomic_RNA.
DR EMBL; K02860; AAA47193.1; -; Genomic_RNA.
DR EMBL; K02861; AAA47194.1; -; Genomic_RNA.
DR EMBL; K02862; AAA47195.1; -; Genomic_RNA.
DR EMBL; K02863; AAA47196.1; -; Genomic_RNA.
DR EMBL; K02864; AAA47197.1; -; Genomic_RNA.
DR EMBL; K02865; AAA47198.1; -; Genomic_RNA.
DR EMBL; K02866; AAA47205.1; -; Genomic_RNA.
DR EMBL; K02867; AAA47206.1; -; Genomic_RNA.
DR EMBL; K02868; AAA47207.1; -; Genomic_RNA.
DR EMBL; K02869; AAA47208.1; -; Genomic_RNA.
DR PIR; A04121; VGVNG.
DR PDB; 3NFK; X-ray; 1.43 A; C/D=512-524.
DR PDBsum; 3NFK; -.
DR SMR; P03524; -.
DR ELM; P03524; -.
DR ChEMBL; CHEMBL3856167; -.
DR iPTMnet; P03524; -.
DR PRIDE; P03524; -.
DR Proteomes; UP000008619; 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 3D-structure; Glycoprotein; Lipoprotein; Membrane; Palmitate; Signal;
KW Transmembrane; Transmembrane helix; 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 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 RV231-
FT 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
