Q86218 (VP2_ROTSR) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 38. History...
Names and origin
|Protein names||Recommended name:|
Inner capsid protein VP2
|Organism||Rotavirus A (strain SA11-Ramig G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Ramig))|
|Taxonomic identifier||36435 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus › Rotavirus A ›|
|Virus host||Macaca mulatta (Rhesus macaque) [TaxID: 9544]|
|Sequence length||882 AA.|
|Protein existence||Inferred from homology|
General annotation (Comments)
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. Nacent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP2 is required for the replicase activity of VP1 polymerase. It probably plays a role in the coordination of packaging and genome replication by controlling the initiation of minus-strand synthesis. Binding to the polymerase VP1 presumably activates the autoinhibited VP1-RNA complex which will start the synthesis of the complementary minus-strand By similarity.
Dimer Potential. Interacts with VP1; this interaction presumably activates VP1. Interacts with VP3. Interacts with VP6. Interacts with NSP5 By similarity.
Virion Potential. 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.
The N-terminus is involved in VP1 binding By similarity.
Belongs to the rotavirus VP2 family.
|Cellular component||Capsid protein|
Inner capsid protein
|Gene Ontology (GO)|
|Cellular_component||viral inner capsid|
Inferred from electronic annotation. Source: UniProtKB-KWviral nucleocapsid
Inferred from electronic annotation. Source: InterPro
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 882||882||Inner capsid protein VP2||PRO_0000368065|
|Region||1 – 94||94||Interaction with VP1 and VP3 By similarity|
|Region||396 – 416||21||Hydrophobic By similarity|
|Region||424 – 444||21||Hydrophobic By similarity|
|Region||538 – 559||22||Leucine-zipper 1 Potential|
|Region||667 – 688||22||Leucine-zipper 2 Potential|
|L33364 Genomic RNA. Translation: AAA47349.1.|
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR007779. Rotavirus_VP2. |
|Pfam||PF05087. Rota_VP2. 1 hit. |
|ProDom||PD008866. Rota_VP2. 1 hit. |
[Graphical view] [Entries sharing at least one domain]
|Accession||Primary (citable) accession number: Q86218|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families