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P03524

- VGLG_RABVE

UniProt

P03524 - VGLG_RABVE

Protein

Glycoprotein G

Gene

G

Organism
Rabies virus (strain ERA) (RABV)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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

    GO - Cellular componenti

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

    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 host2 Publications
    Glycosylationi266 – 2661N-linked (GlcNAc...); by host2 Publications
    Glycosylationi338 – 3381N-linked (GlcNAc...); by host2 Publications
    Lipidationi480 – 4801S-palmitoyl cysteine; by hostBy 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.By similarity

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 459440Virion surfaceSequence AnalysisAdd
    BLAST
    Topological domaini481 – 52444IntravirionSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei460 – 48021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the lyssavirus glycoprotein family.Curated

    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: October 1, 2014
    This is version 70 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