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Q9QNB2 (VP2_ROTHK) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 Human/Japan/KU/1995 G1-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) [Complete proteome]
Taxonomic identifier10952 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length892 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Domain

The N-terminus is involved in VP1 binding By similarity.

Sequence similarities

Belongs to the rotavirus VP2 family.

Ontologies

Keywords
   Cellular componentCapsid protein
Inner capsid protein
Virion
   DomainRepeat
   LigandRNA-binding
   Technical termComplete 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 – 892892Inner capsid protein VP2
PRO_0000368057

Regions

Region1 – 102102Interaction with VP1 and VP3 By similarity
Region406 – 42621Hydrophobic By similarity
Region434 – 45421Hydrophobic By similarity
Region548 – 56922Leucine-zipper 1 Potential
Region677 – 69822Leucine-zipper 2 Potential

Sequences

Sequence LengthMass (Da)Tools
Q9QNB2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 717BB8DCC285375E

FASTA892104,135
        10         20         30         40         50         60 
MAYRKRGAKR EDLSQQHERL QEKEIENNTD VTMENKNNNN NRKQRLSDKV LSQKEEIITD 

        70         80         90        100        110        120 
VQDDIKIADE VKKSSKEESK QLLEILKTKE EHQKEVQYEI LQKTIPTFEP KESILKKLED 

       130        140        150        160        170        180 
IRPEQAKKQM KLFRIFEPRQ LPIYRTNGEK ELRNRWYWKL KKDTLPDGDY DVREYFLNLY 

       190        200        210        220        230        240 
DQILIEMPDY LLLKDMAVEN KNSRDAGKVV DSETANICDA IFQDEETEGV IRRFIADMRQ 

       250        260        270        280        290        300 
QVQSDRNIVN YPSILHPIDH AFNEYFLNHQ LVEPLNNEII FNYIPERIRN DVNYILNMDM 

       310        320        330        340        350        360 
NLPSTARYIR PNLLQDRLNL HDNFESLWDT ITTSNYVLAR SVVPDLKEKE LVSTEAQIQK 

       370        380        390        400        410        420 
MSQDLQLEAL TIQSETQFLA GINSQAANDC FKTLIAAMLS QRTMSLDFVT TNYMSLISGM 

       430        440        450        460        470        480 
WLLTVIPNDM FLRESLVACE LAIINTIVYP AFGMQRMHYR NGDPQTPFQI AEQQIQNFQV 

       490        500        510        520        530        540 
ANWLHFINNN RFRQVVIDGV LNQTLNDNIR NGQVINQLME ALMQLSRQQF PTMPVDYKRS 

       550        560        570        580        590        600 
IQRGILLLSN RLGQLVDLTR LVSYNYETLM ACITMNMQHV QTLTTEKLQL TSVTSLCMLI 

       610        620        630        640        650        660 
GNTTVIPSPQ TLFHYYNVSV NFHSNYNERI NDAVAIITAA NRLNLYQKKM KSIVEDFLKR 

       670        680        690        700        710        720 
LQIFDVPRVP DDQMYRLRDR LRLLPVERRR LDIFNLILMN MEQIERASDK IAQGVLIAYR 

       730        740        750        760        770        780 
DMQLERDEMY GFVNIARNLD GYQQINLEEL MRTGDYGQIT NMLLNNQPVA LVGALPFVTD 

       790        800        810        820        830        840 
SSVISLIAKL DATVFAQIVK LRKVDTLKPI LYKINSDSND FYLVANYDWI PTSTTKVYKQ 

       850        860        870        880        890 
VPQPFDFRAS MHMLTSNLTF TVYSDLLSFV SADTVEPINA IAFDNMRIMN EL 

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References

[1]Taniguchi K.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB022766 mRNA. Translation: BAA84963.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

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_ROTHK
AccessionPrimary (citable) accession number: Q9QNB2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 1, 2000
Last modified: October 16, 2013
This is version 29 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