F6LR22 · F6LR22_9REOV

  • Protein
    Inner capsid protein VP2
  • Gene
    VP2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

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.

1880100200300400500600700800
TypeIDPosition(s)Description
Site220Interaction with the intermediate capsid protein VP6
Site224Interaction with the intermediate capsid protein VP6
Site228Interaction with the intermediate capsid protein VP6
Site839Interaction with the intermediate capsid protein VP6
Site841Interaction with the intermediate capsid protein VP6

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 ComponentT=2 icosahedral viral capsid
Cellular Componentviral inner capsid
Cellular Componentviral nucleocapsid
Molecular FunctionRNA binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Inner capsid protein VP2

Gene names

    • Name
      VP2

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KF17
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus > Rotavirus A

Accessions

  • Primary accession
    F6LR22

Proteomes

Subcellular Location

Virion
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

PTM/Processing

Post-translational modification

Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins seems to have a positive role on viral replication.

Keywords

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 region.

TypeIDPosition(s)Description
Region1-45Disordered
Region1-805-fold hub; involved in the encapsidation of VP1 and VP3
Region394-414Hydrophobic
Region422-442Hydrophobic

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    880
  • Mass (Da)
    102,469
  • Last updated
    2011-07-27 v1
  • Checksum
    82640A27B7310BC3
MAYRKRGARREANVNSNDRMQEKDDEKQDQNNKMQLSDKVLSKKEEVITDNQEEVKIADEVKKSTKEESKQLLEVLKTKEEHQKEIQYEILQKTIPTFEPKESILKKLEDIKPEQAKKQTKLFRIFEPRQLPIYRANGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQVLTEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGAVRRFIAEMRQRVQADRNVVNYPSILHPIDYAFNEYFLQHQLVEPLNNDIIFNYIPERIRNDVNYILNMDRNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLKELVSTEAQIQKMSQDLQLEALTIQSETQFLTGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVVPNDMFIRESLVACQLAIVNTIVYPAFGMQRMHYRNGDPQTPFQIAEQQIQNFQVANWLHFVNNNQFRQVVIDGVLNQVLNDNIRNGHVINQLMEALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLAYNYETLMACITMNMRHVQTLTTEKLQLTSVTSLCMLIGNATVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKAIVEDFLKRLHIFDVARVPDDQMYRLRDRLRLLPVEVRRLDIFNLILMNMDQIERASDKIAQGVIIAYRDMQLERDEMYGYVNIARNLDGFQQINLEELMRTGDYAQITNMLLNNQPVALVGALPFVTDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWVPTSTTKVYKQVPQQFDFRNSMHMLTSNLTFTVYSDLLAFVSADTVEPINAVAFDNMRIMNEL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JF421976
EMBL· GenBank· DDBJ
AEF32122.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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