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P12476 (VP7_ROTRH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Outer capsid glycoprotein VP7
OrganismRotavirus A (strain Monkey/United States/RRV/1980 G3-P5B[3]-I2-R2-C3-M3-A9-Nx-T3-E3-H6) (RV-A)
Taxonomic identifier10969 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostMacaca mulatta (Rhesus macaque) [TaxID: 9544]

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Outer capsid protein involved in attachment and possibly entry into the host epithelial cell. It is subsequently lost, together with VP4, following virus entry into the host cell. The outer layer contains 780 copies of VP7, grouped as 260 trimers. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. In integrin-dependent strains, VP7 seems to essentially target the integrin heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 at a postbinding stage, once the initial attachment by VP4 has been achieved By similarity.

Subunit structure

Homotrimer; in the presence of calcium By similarity. Acquisition of the capsid outer layer requires a high calcium concentration inside the endoplasmic reticulum. Following cell entry, the low calcium concentration in the cytoplasm is probably responsible for the solubilization of the outer layer. Interacts with host integrin heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 By similarity. Ref.3

Subcellular location

Virion By similarity. Host endoplasmic reticulum lumen Potential. Note: Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles By similarity.

Post-translational modification

The N-terminus is blocked possibly by pyroglutamic acid By similarity.

N-glycosylated By similarity. Ref.4

Intramolecular disulfide bonds By similarity.

Miscellaneous

In group A rotaviruses, VP7 defines the G serotype.

Sequence similarities

Belongs to the rotavirus VP7 family.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P12476-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P12476-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
Note: Produced by alternative initiation at Met-30 of isoform 1. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5050 Potential
Chain51 – 326276Outer capsid glycoprotein VP7 Potential
PRO_0000149620

Amino acid modifications

Glycosylation691N-linked (GlcNAc...); by host Potential

Natural variations

Alternative sequence1 – 2929Missing in isoform 2.
VSP_038635
Natural variant321C → F in strain: Isolate MMU-18006.
Natural variant1711A → T in strain: Isolate MMU-18006.
Natural variant3241N → Y in strain: Isolate MMU-18006.

Secondary structure

......................................... 326
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 4913E7C879533A30

FASTA32636,989
        10         20         30         40         50         60 
MYGIEYTTVL TFLISLILLN YILKSLTRMM DCIIYRFLFI VVILSPLLKA QNYGINLPIT 

        70         80         90        100        110        120 
GSMDTAYANS TQEETFLTST LCLYYPTEAA TEINDNSWKD TLSQLFLTKG WPTGSVYFKE 

       130        140        150        160        170        180 
YTDIASFSVD PQLYCDYNVV LMKYDATLQL DMSELADLIL NEWLCNPMDI ALYYYQQTDE 

       190        200        210        220        230        240 
ANKWISMGSS CTIKVCPLNT QTLGIGCLTT DTATFEEVAT AEKLVITDVV DGVNHKLDVT 

       250        260        270        280        290        300 
TATCTIRNCK KLGPRENVAV IQVGGSDVLD ITADPTTAPQ TERMMRINWK KWWQVFYTVV 

       310        320 
DYVNQIIQAM SKRSRSLNSA AFYNRI 

« Hide

Isoform 2 [UniParc].

Checksum: 2B2C399A9A8A9051
Show »

FASTA29733,582

References

[1]"Comparison of the amino acid sequences of the major neutralization protein of four human rotavirus serotypes."
Green K.Y., Midthun K., Gorziglia M., Hoshino Y., Kapikian A.Z., Chanock R.M., Flores J.
Virology 161:153-159(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Isolate MMU-18006.
[2]"Characterization of homotypic and heterotypic VP7 neutralization sites of rhesus rotavirus."
Mackow E.R., Shaw R.D., Matsui S.M., Vo P.T., Benfield D.A., Greenberg H.B.
Virology 165:511-517(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers."
Dormitzer P.R., Greenberg H.B., Harrison S.C.
Virology 277:420-428(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
[4]"Intracellular manipulation of disulfide bond formation in rotavirus proteins during assembly."
Svensson L., Dormitzer P.R., von Bonsdorff C.-H., Maunula L., Greenberg H.B.
J. Virol. 68:5204-5215(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, GLYCOSYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21650 Genomic RNA. Translation: AAA47346.1.
AF295303 mRNA. No translation available.
PIRVGXRRH. A29247.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FMGX-ray3.40A51-326[»]
3GZTelectron microscopy3.80B/F/G/H/I/J/K/L/M/N/O/P/Q58-312[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001963. VP7.
[Graphical view]
PfamPF00434. VP7. 1 hit.
[Graphical view]
ProDomPD000191. VP7. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP12476.

Entry information

Entry nameVP7_ROTRH
AccessionPrimary (citable) accession number: P12476
Secondary accession number(s): P11855
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 19, 2014
This is version 75 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