G9M539 · G9M539_HRSV

Function

function

Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities.

Isoform Secreted glycoprotein G

Helps the virus escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fc-gamma receptors.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Cellular Componenthost cell plasma membrane
Cellular Componentplasma membrane
Cellular Componentvirion membrane
Biological Processsymbiont entry into host cell
Biological Processvirion attachment to host cell
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Major surface glycoprotein G
  • Alternative names
    • Attachment glycoprotein G

Gene names

    • Name
      G

Organism names

  • Taxonomic identifier
  • Strain
    • RSV/YOK/07/43
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Pneumoviridae > Orthopneumovirus > Orthopneumovirus hominis

Accessions

  • Primary accession
    G9M539

Subcellular Location

Host cell membrane
; Single-pass type II membrane protein
Secreted
Virion membrane
; Single-pass type II membrane protein

Keywords

Interaction

Subunit

Homooligomer. Interacts (via N-terminus) with protein M. Part of a complex composed of F1, F2 and G glycoproteins. Interacts with protein SH. Interacts with host heparate sulfate; this interaction probably participates in the viral attachment to the host cell. Interacts with host CX3CR1; this interaction plays an important role in viral entry. Interacts with the host lectins CD209/DC-SIGN and CD209L/L-SIGN on dendritic cells; these interactions stimulate the phosphorylation of MAPK3/ERK1 and MAPK1/ERK2, which inhibits dendritic cell activation and could participate in the limited immunity against RSV reinfection.

Isoform Membrane-bound glycoprotein G

Homooligomer. Interacts (via N-terminus) with protein M. Part of a complex composed of F1, F2 and G glycoproteins. Interacts with protein SH. Interacts with host heparate sulfate; this interaction probably participates in the viral attachment to the host cell.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-78Disordered
Compositional bias12-78Polar residues

Sequence similarities

Belongs to the pneumoviruses glycoprotein G family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    78
  • Mass (Da)
    8,486
  • Last updated
    2012-02-22 v1
  • Checksum
    74769AD106DEF506
TKPKEVLTTKPTEKPTIDTTKTNIRTTLLTSNTTGNPEHTSQEETLHSTTSEGNLSPSQVYTTSEYLSQSPSSSNTTK

Features

Showing features for non-terminal residue, compositional bias.

TypeIDPosition(s)Description
Non-terminal residue1
Compositional bias12-78Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB551039
EMBL· GenBank· DDBJ
BAL42436.1
EMBL· GenBank· DDBJ
Viral cRNA

Similar Proteins

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