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P03533 (VP7_ROTS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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.

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. Ref.5

Subcellular location

Virion. 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.

Post-translational modification

The N-terminus is blocked possibly by pyroglutamic acid.

N-glycosylated. Ref.3

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: P03533-1)

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: P03533-2)

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. This isoform is thought to be the major form in the cell.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5050 Potential
Chain51 – 326276Outer capsid glycoprotein VP7 Potential
PRO_0000149621

Regions

Calcium binding127 – 15731 Potential
Motif253 – 2553GPR motif; interaction with ITGAX/ITGB2 heterodimer Probable

Amino acid modifications

Glycosylation691N-linked (GlcNAc...) (high mannose); by host Probable

Natural variations

Alternative sequence1 – 2929Missing in isoform 2.
VSP_036750

Experimental info

Sequence conflict161I → T in AAA47307. Ref.2
Sequence conflict321C → F in AAA47307. Ref.2
Sequence conflict371L → F in AAA47307. Ref.2
Sequence conflict601T → A in AAA47307. Ref.2
Sequence conflict751T → P in AAA47307. Ref.2
Sequence conflict1141G → E in AAA47307. Ref.2
Sequence conflict2191A → P in AAA47307. Ref.2
Sequence conflict2691L → H in CAA24788. Ref.1

Sequences

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

Last modified July 21, 1986. Version 1.
Checksum: C75549FD1F2A0C31

FASTA32637,120
        10         20         30         40         50         60 
MYGIEYTTVL TFLISIILLN YILKSLTRIM DCIIYRLLFI IVILSPFLRA QNYGINLPIT 

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

       130        140        150        160        170        180 
YTNIASFSVD PQLYCDYNVV LMKYDATLQL DMSELADLIL NEWLCNPMDI TLYYYQQTDE 

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

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

       310        320 
DYVDQIIQVM SKRSRSLNSA AFYYRV 

« Hide

Isoform 2 [UniParc].

Checksum: 91AE8498DCF78BF3
Show »

FASTA29733,732

References

[1]"Serotype-specific glycoprotein of simian 11 rotavirus: coding assignment and gene sequence."
Both G.W., Mattick J.S., Bellamy A.R.
Proc. Natl. Acad. Sci. U.S.A. 80:3091-3095(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Primary structure of the neutralization antigen of simian rotavirus SA11 as deduced from cDNA sequence."
Arias C.F., Lopez S., Bell J.R., Strauss J.H.
J. Virol. 50:657-661(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Processing of the rough endoplasmic reticulum membrane glycoproteins of rotavirus SA11."
Kabcenell A.K., Atkinson P.H.
J. Cell Biol. 101:1270-1280(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[4]"Processing of rotavirus glycoprotein VP7: implications for the retention of the protein in the endoplasmic reticulum."
Stirzaker S.C., Whitfeld P.L., Christie D.L., Bellamy A.R., Both G.W.
J. Cell Biol. 105:2897-2903(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: SIGNAL SEQUENCE CLEAVAGE SITE.
[5]"Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry."
Graham K.L., Halasz P., Tan Y., Hewish M.J., Takada Y., Mackow E.R., Robinson M.K., Coulson B.S.
J. Virol. 77:9969-9978(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN INTEGRIN HETERODIMER ITGAX/ITGB2, INTERACTION WITH INTEGRIN HETERODIMER ITGA5/ITGB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01190 Unassigned RNA. Translation: CAA24510.1.
V01546 Genomic RNA. Translation: CAA24788.1.
K02028 Genomic RNA. Translation: AAA47307.1.
PIRVGXR1S. A04135.

3D structure databases

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...

Entry information

Entry nameVP7_ROTS1
AccessionPrimary (citable) accession number: P03533
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 84 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