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P03524

- VGLG_RABVE

UniProt

P03524 - VGLG_RABVE

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Protein

Glycoprotein G

Gene
G
Organism
Rabies virus (strain ERA) (RABV)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycoprotein G
Gene namesi
Name:G
OrganismiRabies virus (strain ERA) (RABV)
Taxonomic identifieri11295 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesRhabdoviridaeLyssavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mammalia [TaxID: 40674]
ProteomesiUP000008619: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 459440Virion surface Reviewed predictionAdd
BLAST
Transmembranei460 – 48021Helical; Reviewed predictionAdd
BLAST
Topological domaini481 – 52444Intravirion Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. viral envelope Source: UniProtKB-KW
  3. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Biotechnological usei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 524505Glycoprotein GPRO_0000040993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...); by host1 Publication
Glycosylationi266 – 2661N-linked (GlcNAc...); by host1 Publication
Glycosylationi338 – 3381N-linked (GlcNAc...); by host1 Publication
Lipidationi480 – 4801S-palmitoyl cysteine; by host By similarity

Post-translational modificationi

Glycosylated and palmitoylated by host. Glycosylation is crucial for glycoprotein export at the cell surface.2 Publications

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer. Interacts with matrix protein By similarity.1 Publication

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi521 – 5233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NFKX-ray1.43C/D512-524[»]
ProteinModelPortaliP03524.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR001903. Rhabd_glycop.
[Graphical view]
PfamiPF00974. Rhabdo_glycop. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03524-1 [UniParc]FASTAAdd to Basket

« Hide

MVPQALLFVP LLVFPLCFGK FPIYTILDKL GPWSPIDIHH LSCPNNLVVE    50
DEGCTNLSGF SYMELKVGYI LAIKMNGFTC TGVVTEAETY TNFVGYVTTT 100
FKRKHFRPTP DACRAAYNWK MAGDPRYEES LHNPYPDYRW LRTVKTTKES 150
LVIISPSVAD LDPYDRSLHS RVFPSGKCSG VAVSSTYCST NHDYTIWMPE 200
NPRLGMSCDI FTNSRGKRAS KGSETCGFVD ERGLYKSLKG ACKLKLCGVL 250
GLRLMDGTWV AMQTSNETKW CPPDQLVNLH DFRSDEIEHL VVEELVRKRE 300
ECLDALESIM TTKSVSFRRL SHLRKLVPGF GKAYTIFNKT LMEADAHYKS 350
VRTWNEILPS KGCLRVGGRC HPHVNGVFFN GIILGPDGNV LIPEMQSSLL 400
QQHMELLESS VIPLVHPLAD PSTVFKDGDE AEDFVEVHLP DVHNQVSGVD 450
LGLPNWGKYV LLSAGALTAL MLIIFLMTCC RRVNRSEPTQ HNLRGTGREV 500
SVTPQSGKII SSWESHKSGG ETRL 524
Length:524
Mass (Da):58,658
Last modified:July 21, 1986 - v1
Checksum:iBBA53981C1175880
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271L → P in strain: ERA 2007.
Natural varianti55 – 551T → I in strain: CVS-11, RV194-2[F3] and RV231-22.
Natural varianti177 – 1771K → N in strain: RV194-2[F3].
Natural varianti217 – 2171K → E in strain: RV231-22.
Natural varianti221 – 2244KGSE → NGNK in strain: CVS-11, RV194-2[F3] and RV231-22.
Natural varianti352 – 3521R → Q in strain: RV194-2[F3].

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA04121. VGVNG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A04121. VGVNG.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NFK X-ray 1.43 C/D 512-524 [» ]
ProteinModelPortali P03524.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR001903. Rhabd_glycop.
[Graphical view ]
Pfami PF00974. Rhabdo_glycop. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. Cited for: INTERACTION WITH HOST CELL RECEPTORS.

Entry informationi

Entry nameiVGLG_RABVE
AccessioniPrimary (citable) accession number: P03524
Secondary accession number(s): A3F5L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Arg-352 is highly involved in rabies virus pathogenicity. Its mutation dramatically attenuates the virus.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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