Q98031 · VP7_ROTKU
- ProteinOuter capsid glycoprotein VP7
- StatusUniProtKB reviewed (Swiss-Prot)
- 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.
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 95 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 177 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 206 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 214 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 216 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 228 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 229 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 301 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell endoplasmic reticulum lumen | |
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
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus > Rotavirus A
- Virus hosts
Accessions
- Primary accessionQ98031
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.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-50 | |||||
Sequence: MYGIGNTTILTILISIILLNYILKTITNTMDYIIFRFLLLIALISPFVRT | ||||||
Chain | PRO_0000369114 | 51-326 | Outer capsid glycoprotein VP7 | |||
Sequence: PNYGMYLPITGSLDAVYTNSTSGESFLTSTLCLYYPTEAKNEISDDEWENTLSQLFLTKGWPTGSVYFKDYNDITTFSMNPQLYCDYNVVLMRYDNTSELDASELADLILNEWLCNPMDISLHYYQQSSESNKWISMGTDCTVKVCPLNTQTLGIGCKTTDVNTFEIVASSEKLVITDVVNGVNHKINISMSTCTIRNCNKLGPRENVAIIQVGGPNALDITADPTTVPQVQRIMRINWKKWWQVFYTVVDYINQIIQVMSKRSRSLDTAAFYYRI | ||||||
Glycosylation | 69 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 82↔135 | |||||
Sequence: CLYYPTEAKNEISDDEWENTLSQLFLTKGWPTGSVYFKDYNDITTFSMNPQLYC | ||||||
Glycosylation | 146 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 165↔249 | |||||
Sequence: CNPMDISLHYYQQSSESNKWISMGTDCTVKVCPLNTQTLGIGCKTTDVNTFEIVASSEKLVITDVVNGVNHKINISMSTCTIRNC | ||||||
Disulfide bond | 191↔244 | |||||
Sequence: CTVKVCPLNTQTLGIGCKTTDVNTFEIVASSEKLVITDVVNGVNHKINISMSTC | ||||||
Disulfide bond | 196↔207 | |||||
Sequence: CPLNTQTLGIGC | ||||||
Glycosylation | 238 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
The N-terminus is blocked possibly by pyroglutamic acid.
Keywords
- PTM
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*.
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 165-167 | CNP motif; interaction with ITGAV/ITGB3 | ||||
Sequence: CNP | ||||||
Region | 253-255 | GPR motif; interaction with ITGAX/ITGB2 | ||||
Sequence: GPR |
Sequence similarities
Belongs to the rotavirus VP7 family.
Keywords
- Domain
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative initiation.
Q98031-1
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.
- Name1
- Length326
- Mass (Da)37,101
- Last updated1997-02-01 v1
- Checksum706B7C20BD7F2BD6
Q98031-2
- Name2
- NoteProduced by alternative initiation at Met-30 of isoform 1.
- Differences from canonical
- 1-29: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_038622 | 1-29 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity