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P26191 (VP2_ROTPC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 48. 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 C (strain Pig/United States/Cowden/1980) (RV-C) [Complete proteome]
Taxonomic identifier10916 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostSus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length872 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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
   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 – 872872Inner capsid protein VP2
PRO_0000149534

Regions

Region1 – 9696Interaction with VP1 and VP3 By similarity
Region417 – 43620Hydrophobic By similarity
Region494 – 51320Hydrophobic By similarity

Sequences

Sequence LengthMass (Da)Tools
P26191 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 1AB1EF62AB9F51AF

FASTA872101,019
        10         20         30         40         50         60 
MISRNRRRNT QQKDAEKEKQ TENVEEKEIK EAKEQVKDEK QVITEENVDS PKDVKEQSNT 

        70         80         90        100        110        120 
VNLQKNDLVK EVINIQNQTL NTIVAENKVE IEEVVKKYIP SYSTDKLIVK NYRNSRIKCQ 

       130        140        150        160        170        180 
TYNKLFRLLH VKSYLYDVNG EKKLSTRWYW KLLKDDLPAG DYSVRQFFLS LYLNVLDEMP 

       190        200        210        220        230        240 
DYVMLRDMAV DNPYSAEAGK IVDEKSKEIL VEIYQDQMTE GYIRRYMSDL RHRISGETNT 

       250        260        270        280        290        300 
AKYPAILHPV DEELNKYFLE HQLIQPLTTR NIAELIPTQL YHDPNYVFNI DAAFLTNSRF 

       310        320        330        340        350        360 
VPPYLTQDRI GLHDGFESIW DAKTHADYVS ARRFVPDLTE LVDAEKQMKE MLQCKLNHNS 

       370        380        390        400        410        420 
WQELVHGRNE AFKFIIGTVL STRTIAVEFI TSNYMSLASC MYLMTIMPSE IFLRESLVAM 

       430        440        450        460        470        480 
QLAVINTLIY PALGLAQMHY QAGEIRRLEL AEMQVANRPI RQWLHHCNTL QFGRQVTEGV 

       490        500        510        520        530        540 
THLRFTNDIM TGRIVNLFST MLVALSSQPF ATYPLDYKRS VQRALQLLSN RTAQIADLTR 

       550        560        570        580        590        600 
LIVYNYTTLS ACIVMNMHLV GTLTVERIQA TALTSLIMLI SNKTVIPEPS SLFSYFSSNI 

       610        620        630        640        650        660 
NFLTNYNEQI DNVVAEIMAA YRLDLYQQKM LMLVTRFVSR LYIFDAPKIP PDQMYRLRNR 

       670        680        690        700        710        720 
LRNIPVERRR ADVFRIIMNN RDLIEKTSER ICQGVLLSYS PMPLTYVEDV GLTNVVNDTN 

       730        740        750        760        770        780 
GFQIINIEEI EKTGDYSAIT NALLRDTPII LKGAIPYVTN SSVIDVLSKI DTTVFASIVK 

       790        800        810        820        830        840 
DRDISKLKPI KFTINSDSSE YYLVHNNKWT PTTTTAVYKA RSQQFNIQHS VSMLESNLFF 

       850        860        870 
VVYNDLFKYI KTTTVLPINA VSYDGARIMQ ET 

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References

[1]"Sequences of the four larger proteins of a porcine group C rotavirus and comparison with the equivalent group A rotavirus proteins."
Bremont M., Juste-Lesage P., Chabanne-Vautherot D., Charpilienne A., Cohen J.
Virology 186:684-692(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74217 Unassigned DNA. Translation: AAA19561.1.
PIRP2XRCW. B40822.

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_ROTPC
AccessionPrimary (citable) accession number: P26191
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: October 16, 2013
This is version 48 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