B1NKU2 · VP2_ROTWI
- ProteinInner capsid protein VP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids890 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles. May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 232 | Interaction with the intermediate capsid protein VP6 | ||||
Sequence: F | ||||||
Site | 236 | Interaction with the intermediate capsid protein VP6 | ||||
Sequence: M | ||||||
Site | 849 | Interaction with the intermediate capsid protein VP6 | ||||
Sequence: M | ||||||
Site | 851 | Interaction with the intermediate capsid protein VP6 | ||||
Sequence: M |
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 | T=2 icosahedral viral capsid | |
Cellular Component | viral inner capsid | |
Cellular Component | viral nucleocapsid | |
Molecular Function | RNA binding |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameInner capsid protein VP2
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus > Rotavirus A
- Virus hosts
Accessions
- Primary accessionB1NKU2
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000368051 | 1-890 | Inner capsid protein VP2 | |||
Sequence: MAYRKRGVKRENLLQQNERLQEKEIENNTDVTMENKNNNRKQQLSDKVLSQKEEIITDVQDDIKIVDEVKKSSKEESKQLLEILKTKEDHQKEVQYEILQKTIPTFEPKESILKKLEDIRPEQAKKQMKLFRIFEPRQLPIYRANGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQILIEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGVIRRFIADMRQQIQADRNIVNYPSILHPIDHAFNEYFLNHQLVEPLNNEIIFNYIPERIRNDVNYILNMDMNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLREKELVSTEAQIQKMSQDLQLEALTIQSETQFLAGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVIPNDMFLRESLVACELAIINTIVYPAFGMQRMHYRNGDPQTPFQIAEQQIQNFQVANWLHFINNNRFRQVVIDGVLNQTLNDNIRNGQVINQLMEALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLSYNYETLMACITMNMQHVQTLTTEKLQLTSVTSLCMLIGNTTVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKSIVEDFLKRLQIFDVPRVPDDQMYRLRDRLRLLPVERRRLDIFNLILMNMDQIERASDKIAQGVIIAYRDMQLERDEMYGFVNIARNLDGYQQINLEELMRTGDYGQITNMLLNNQPVALVGALPFVTDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWIPTSTTKVYKQIPQPFDFRASMHMLTSNLTFTVYSDLLSFVSADTVEPINAIAFDNMRIMNEL |
Post-translational modification
Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins seems to have a positive role on viral replication.
Keywords
- PTM
Interaction
Subunit
Homodecamer; each decamer is made up of two conformers of VP2, called VP2A and VP2B. Interacts with a VP1-VP3 complex. Interacts with the intermediate capsid protein VP6. Interacts with NSP5. Interacts (via N-terminus) with NSP2.
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-30 | Basic and acidic residues | ||||
Sequence: MAYRKRGVKRENLLQQNERLQEKEIENNTD | ||||||
Region | 1-45 | Disordered | ||||
Sequence: MAYRKRGVKRENLLQQNERLQEKEIENNTDVTMENKNNNRKQQLS | ||||||
Region | 1-88 | 5-fold hub; involved in the encapsidation of VP1 and VP3 | ||||
Sequence: MAYRKRGVKRENLLQQNERLQEKEIENNTDVTMENKNNNRKQQLSDKVLSQKEEIITDVQDDIKIVDEVKKSSKEESKQLLEILKTKE | ||||||
Compositional bias | 31-45 | Polar residues | ||||
Sequence: VTMENKNNNRKQQLS | ||||||
Region | 404-424 | Hydrophobic | ||||
Sequence: LDFVTTNYMSLISGMWLLTVI | ||||||
Region | 432-452 | Hydrophobic | ||||
Sequence: ESLVACELAIINTIVYPAFGM |
Domain
The N-terminus binds RNA. It is necessary for encapsidation of VP1 and VP3. The N-termini of 10 VP2 molecules form a cylindrical hub underneath each 5-fold axis of the inner capsid.
Sequence similarities
Belongs to the rotavirus VP2 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length890
- Mass (Da)103,947
- Last updated2008-04-29 v1
- ChecksumFF766662D367581A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-30 | Basic and acidic residues | ||||
Sequence: MAYRKRGVKRENLLQQNERLQEKEIENNTD | ||||||
Compositional bias | 31-45 | Polar residues | ||||
Sequence: VTMENKNNNRKQQLS |