P03524 (VGLG_RABVE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glycoprotein G | ||
| Gene names |
| ||
| Organism | Rabies virus (strain ERA) (RABV) [Complete proteome] | ||
| Taxonomic identifier | 11295 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Mononegavirales › Rhabdoviridae › Lyssavirus › ![]() | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] Mammalia [TaxID: 40674] |
Protein attributes
| Sequence length | 524 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane. There is convincing in vitro evidence that the muscular form of the nicotinic acetylcholine receptor (nAChR), the neuronal cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR) bind glycoprotein G and thereby facilitate rabies virus entry into cells. |
| Subunit structure | Homotrimer. Interacts with matrix protein By similarity. Ref.7 |
| Subcellular location | Virion membrane; Single-pass type I membrane protein Potential. |
| Post-translational modification | Glycosylated and palmitoylated by host. Glycosylation is crucial for glycoprotein export at the cell surface. Ref.5 Ref.6 |
| Biotechnological use | Primary surface antigen capable of inducing and reacting with virus-neutralizing antibodies. Almost all human and veterinary vaccines are based on the functional aspects of the G protein. |
| Miscellaneous | Arg-352 is highly involved in rabies virus pathogenicity. Its mutation dramatically attenuates the virus. |
| Sequence similarities | Belongs to the lyssavirus glycoprotein family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Viral envelope protein Virion |
| Domain | Signal Transmembrane Transmembrane helix |
| PTM | Glycoprotein Lipoprotein Palmitate |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelopeInferred from electronic annotation. Source: UniProtKB-KW virion membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | |||||||||
| Chain | 20 – 524 | 505 | Glycoprotein G | PRO_0000040993 | |||||||
Regions | |||||||||||
| Topological domain | 20 – 459 | 440 | Virion surface Potential | ||||||||
| Transmembrane | 460 – 480 | 21 | Helical; Potential | ||||||||
| Topological domain | 481 – 524 | 44 | Intravirion Potential | ||||||||
Amino acid modifications | |||||||||||
| Lipidation | 480 | 1 | S-palmitoyl cysteine; by host By similarity | ||||||||
| Glycosylation | 56 | 1 | N-linked (GlcNAc...); by host Ref.5 | ||||||||
| Glycosylation | 266 | 1 | N-linked (GlcNAc...); by host Ref.5 | ||||||||
| Glycosylation | 338 | 1 | N-linked (GlcNAc...); by host Ref.5 | ||||||||
Natural variations | |||||||||||
| Natural variant | 27 | 1 | L → P in strain: ERA 2007. | ||||||||
| Natural variant | 55 | 1 | T → I in strain: CVS-11, RV194-2[F3] and RV231-22. | ||||||||
| Natural variant | 177 | 1 | K → N in strain: RV194-2[F3]. | ||||||||
| Natural variant | 217 | 1 | K → E in strain: RV231-22. | ||||||||
| Natural variant | 221 – 224 | 4 | KGSE → NGNK in strain: CVS-11, RV194-2[F3] and RV231-22. | ||||||||
| Natural variant | 352 | 1 | R → Q in strain: RV194-2[F3]. | ||||||||
Secondary structure | |||||||||||
Helix Strand Turn | |||||||||||
| Beta strand | 521 – 523 | 3 | |||||||||
Sequences
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References
| [1] | "Structure of the glycoprotein gene in rabies virus." Anilionis A., Wunner W.H., Curtis P.J. Nature 294:275-278(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [2] | "Amino acid sequence of the rabies virus glycoprotein deduced from its cloned gene." Anilionis A., Wunner W.H., Curtis P.J. Comp. Immunol. Microbiol. Infect. Dis. 5:27-32(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [3] | "Complete nucleotide sequencing of SAD derivatives of attenuated rabies virus vaccine strains." Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B., Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E., Cox J.H., Mueller T. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: ERA 2007. |
| [4] | "Antigenic variants of CVS rabies virus with altered glycosylation sites." Wunner W.H., Dietzschold B., Smith C.L., Lafon M., Golub E. Virology 140:1-12(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 49-59; 169-179; 209-226 AND 337-354. Strain: CVS-11, RV194-2[F3] and RV231-22. |
| [5] | "N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression." Shakin-Eshleman S.H., Remaley A.T., Eshleman J.R., Wunner W.H., Spitalnik S.L. J. Biol. Chem. 267:10690-10698(1992) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-56; ASN-266 AND ASN-338. |
| [6] | "The role of site-specific N-glycosylation in secretion of soluble forms of rabies virus glycoprotein." Wojczyk B.S., Stwora-Wojczyk M., Shakin-Eshleman S.H., Wunner W.H., Spitalnik S.L. Glycobiology 8:121-130(1998) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION. |
| [7] | "Rabies virus receptors." Lafon M. J. Neurovirol. 11:82-87(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HOST CELL RECEPTORS. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | J02293 Genomic RNA. Translation: AAA47204.1. Sequence problems. M38452 Genomic RNA. Translation: AAA47209.1. EF206707 Genomic RNA. Translation: ABN11294.1. K02858 Genomic RNA. Translation: AAA47191.1. K02859 Genomic RNA. Translation: AAA47192.1. K02860 Genomic RNA. Translation: AAA47193.1. K02861 Genomic RNA. Translation: AAA47194.1. K02862 Genomic RNA. Translation: AAA47195.1. K02863 Genomic RNA. Translation: AAA47196.1. K02864 Genomic RNA. Translation: AAA47197.1. K02865 Genomic RNA. Translation: AAA47198.1. K02866 Genomic RNA. Translation: AAA47205.1. K02867 Genomic RNA. Translation: AAA47206.1. K02868 Genomic RNA. Translation: AAA47207.1. K02869 Genomic RNA. Translation: AAA47208.1. | ||||||||||||
| PIR | VGVNG. A04121. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P03524. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001903. Rhabd_glycop. [Graphical view] | ||||||||||||
| Pfam | PF00974. Rhabdo_glycop. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | VGLG_RABVE | ||||||||
| Accession | Primary (citable) accession number: P03524 Secondary accession number(s): A3F5L8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
