G0YVX9 · G0YVX9_9REOV
- ProteinOuter capsid glycoprotein VP7
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids326 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
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.
Miscellaneous
In group A rotaviruses, VP7 defines the G serotype.
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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 95 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 177 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 206 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 214 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 216 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 228 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 229 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 231 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 301 | Ca2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell endoplasmic reticulum lumen | |
Cellular Component | membrane | |
Cellular Component | T=13 icosahedral viral capsid | |
Cellular Component | viral outer capsid | |
Molecular Function | metal ion binding |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameOuter capsid glycoprotein VP7
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus > Rotavirus A
Accessions
- Primary accessionG0YVX9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 6-23 | Helical | |||
Transmembrane | 35-55 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_5023226632 | 51-326 | Outer capsid glycoprotein VP7 | ||
Disulfide bond | 82↔135 | ||||
Disulfide bond | 165↔249 | ||||
Disulfide bond | 191↔244 | ||||
Disulfide bond | 196↔207 | ||||
Post-translational modification
N-glycosylated.
The N-terminus is blocked possibly by pyroglutamic acid.
Keywords
- PTM
Interaction
Subunit
Homotrimer. 2 Ca2+ ions bound at each subunit interface in the trimer hold the trimer together.
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
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 165-167 | CNP motif; interaction with ITGAV/ITGB3 | |||
Region | 237-239 | LVD motif; interaction with ITGA4/ITGB1 heterodimer | |||
Region | 253-255 | GPR motif; interaction with ITGAX/ITGB2 | |||
Sequence similarities
Belongs to the rotavirus VP7 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length326
- Mass (Da)37,253
- Last updated2011-10-19 v1
- ChecksumF9A52171232733F2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HQ834201 EMBL· GenBank· DDBJ | AEK20846.1 EMBL· GenBank· DDBJ | Genomic RNA |