Q07156 · VP7_ROTHU

Function

function

Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry into the host cell, low intracellular or intravesicular Ca2+ concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.

Miscellaneous

Some rotavirus strains are neuraminidase-sensitive and require sialic acid to attach to the cell surface. Some rotavirus strains are integrin-dependent. Some rotavirus strains depend on ganglioside for their entry into the host cell. Hsp70 also seems to be involved in the entry of some strains.
In group A rotaviruses, VP7 defines the G serotype.

Features

Showing features for binding site.

132650100150200250300
TypeIDPosition(s)Description
Binding site95Ca2+ 1 (UniProtKB | ChEBI)
Binding site177Ca2+ 2 (UniProtKB | ChEBI)
Binding site206Ca2+ 1 (UniProtKB | ChEBI)
Binding site214Ca2+ 1 (UniProtKB | ChEBI)
Binding site216Ca2+ 1 (UniProtKB | ChEBI)
Binding site228Ca2+ 2 (UniProtKB | ChEBI)
Binding site229Ca2+ 2 (UniProtKB | ChEBI)
Binding site231Ca2+ 2 (UniProtKB | ChEBI)
Binding site301Ca2+ 2 (UniProtKB | ChEBI)

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 Componenthost cell endoplasmic reticulum lumen
Cellular ComponentT=13 icosahedral viral capsid
Cellular Componentviral outer capsid
Molecular Functionmetal ion binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Outer capsid glycoprotein VP7

Organism names

Accessions

  • Primary accession
    Q07156

Subcellular Location

Virion
Note: The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles.

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-50
ChainPRO_000014960751-326Outer capsid glycoprotein VP7
Glycosylation69N-linked (GlcNAc...) asparagine; by host
Disulfide bond82↔135
Glycosylation145N-linked (GlcNAc...) asparagine; by host
Disulfide bond165↔249
Disulfide bond191↔244
Disulfide bond196↔207

Post-translational modification

N-glycosylated.
The N-terminus is blocked possibly by pyroglutamic acid.

Keywords

Interaction

Subunit

Homotrimer; disulfide-linked. 2 Ca2+ ions bound at each subunit interface in the trimer hold the trimer together. Interacts with the intermediate capsid protein VP6. Interacts with the outer capsid protein VP5*.

Structure

3D structure databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region165-167CNP motif; interaction with ITGAV/ITGB3
Region237-239LVD motif; interaction with ITGA4/ITGB1 heterodimer
Region253-255GPR motif; interaction with ITGAX/ITGB2

Sequence similarities

Belongs to the rotavirus VP7 family.

Keywords

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative initiation.

Q07156-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    326
  • Mass (Da)
    37,163
  • Last updated
    1994-10-01 v1
  • Checksum
    C3A78ADFAAB0AC66
MYGIEYTTVLTFLISIILLNYILKSVTSAMDFIIYRFLLIIVVVSPFVKTQNYGINVPITGSMDTAYTNSSQQETFLTSTLCLYYPIEASTQIGDTEWKGTLSQLFLTKGWPTGSVYFKEYTDIASFSIDPQFYCDYNVVLVKYNSTLELDMSELADLILNEWLCNPMDIALYYYQQTNEANKWISMGQSCTIKVCPLNTQTLGIGCTTTNTATFEEVATNEKLVITDVVDGVNHKLDVTTNTCTIRNCRKLGPRENVAKLQVGGSEVLDITADPTTTPQTERMMQINWKKWWQVFYTVVDYINQIVQVMSKRSRSFNSAAFYYRI

Q07156-2

  • Name
    2
  • Note
    Produced by alternative initiation at Met-30 of isoform 1.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0385961-29in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L14072
EMBL· GenBank· DDBJ
AAA03613.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp