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P17462 (VP2_ROTBU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inner capsid protein VP2
OrganismRotavirus A (strain Cow/United Kingdom/UK/1975 G6-P7[5]-I2-R2-C2-M2-A3-N2-T7-E2-H3) (RV-A) [Complete proteome]
Taxonomic identifier10934 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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.

Subunit structure

Dimer Potential. Interacts with VP1; this interaction presumably activates VP1. Interacts with VP3. Interacts with VP6. Interacts with NSP5 By similarity.

Subcellular location

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 By similarity.

Domain

The N-terminus is involved in VP1 binding.

Sequence similarities

Belongs to the rotavirus VP2 family.

Ontologies

Keywords
   Cellular componentCapsid protein
Inner capsid protein
Virion
   DomainRepeat
   LigandRNA-binding
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Cellular_componentviral inner capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral nucleocapsid

Inferred from electronic annotation. Source: InterPro

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Inner capsid protein VP2
PRO_0000149532

Regions

Region1 – 9292Interaction with VP1 and VP3 By similarity
Region394 – 41421Hydrophobic
Region422 – 44221Hydrophobic
Region537 – 55822Leucine-zipper 1
Region664 – 68724Leucine-zipper 2

Sequences

Sequence LengthMass (Da)Tools
P17462 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 7CFCDF653E4CF2CC

FASTA881102,488
        10         20         30         40         50         60 
MAYRKRGATV EADINNNDRM QEKDDEKQDQ NNRMQLSDKV LSKKEEVVTD SQEEIKIRDE 

        70         80         90        100        110        120 
VKKSTKEESK QLLEVLKTKE EHQKEIQYEI LQKTIPTFEP KESILKKLED IKPEQAKKQT 

       130        140        150        160        170        180 
KLFRIFEPRQ LPIYRANGEK ELRNRWYWKL KKDTLPDGDY DVREYFLNLY DQVLTEMPDY 

       190        200        210        220        230        240 
LLLKDMAVEN KNSRDAGKVV DSETASICDA IFQDEETEGA VRRFIAEMRQ RVQADRNVVN 

       250        260        270        280        290        300 
YPSILHPIDY AFNEYFLQHQ LVEPLNNDII FNYIPERIRN DVNYILNMDR NLPSTARYIR 

       310        320        330        340        350        360 
PNLLQDRLNL HDNFESLWDT ITTSNYILAR SVVPDLKELV STEAQIQKMS QDLQLEALTI 

       370        380        390        400        410        420 
QSETQFLTGI NSQAANDCFK TLIAAMLSQR TMSLDFVTTN YMSLISGMWL LTVVPNDMFI 

       430        440        450        460        470        480 
RESLVACQLA IVNTIIYPAF GMQRMHYRNG DPQTPFQIAE QQIRKFSGSG IGWHFVNNNQ 

       490        500        510        520        530        540 
FRQVVIDGVL NQVLNDNIRN VHVIKQLMQA LMQLSRQQFP TMPVDYKRSI QRGILLLSNR 

       550        560        570        580        590        600 
LGQLVDLTRL LAYNYETLMA CVTMNMQHVQ TLTTEKLQLT SVTSLCMLIG NATVIPSPQT 

       610        620        630        640        650        660 
LFHYYNVNVN FHSNYNERIN DAVAIITAAN RLNLYQKKMK AIVEDFLKRL HIFDVARVPD 

       670        680        690        700        710        720 
DQMYRLRDRL RLLPVEVRRL DIFNLILMNM DQIERASDKI AQGVIIAYRD MQLERDEMYG 

       730        740        750        760        770        780 
YVNIARNLDG FQQINLEELM RTGDYAQITN MLLNNQPVAL VGALPFVTDS SVISLIAKLD 

       790        800        810        820        830        840 
ATVFAQIVKL RKVDTLKPIL YKINSDSNDF YLVANYDWVP TSTTKVYKQV PQQFDFRNSM 

       850        860        870        880 
HMLTSNLTFT VYSDLLAFVS ADTVEPINAV AFDNMRIMNE L 

« Hide

References

[1]"Nucleotide sequence of gene 2 of the UK tissue culture adapted strain of bovine rotavirus."
Tian Y., Tarlow O., McCrae M.A.
Nucleic Acids Res. 18:4015-4015(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52589 Genomic RNA. Translation: CAA36825.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KZ4X-ray3.80A/B1-881[»]
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP17462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR007779. Rotavirus_VP2.
[Graphical view]
PfamPF05087. Rota_VP2. 1 hit.
[Graphical view]
ProDomPD008866. Rota_VP2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameVP2_ROTBU
AccessionPrimary (citable) accession number: P17462
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 16, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references