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Protein

Outer capsid glycoprotein VP7

Gene
N/A
Organism
Rotavirus A (strain SA11-Both G3-P5B[2]-I2-R2-C5-M5-A5-N2-T5-E2-H5) (RV-A) (Simian Agent 11 (strain Both))
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi127 – 15731Sequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid glycoprotein VP7
OrganismiRotavirus A (strain SA11-Both G3-P5B[2]-I2-R2-C5-M5-A5-N2-T5-E2-H5) (RV-A) (Simian Agent 11 (strain Both))
Taxonomic identifieri37137 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]
ProteomesiUP000007180 Componenti: Genome

Subcellular locationi

Virion. Host endoplasmic reticulum lumen Curated
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.

GO - Cellular componenti

  1. host cell endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. T=13 icosahedral viral capsid Source: UniProtKB-KW
  3. viral outer capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host endoplasmic reticulum, Outer capsid protein, T=13 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5050Sequence AnalysisAdd
BLAST
Chaini51 – 326276Outer capsid glycoprotein VP7Sequence AnalysisPRO_0000149621Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi69 – 691N-linked (GlcNAc...) (high mannose); by host1 Publication

Post-translational modificationi

The N-terminus is blocked possibly by pyroglutamic acid.
N-glycosylated.1 Publication
Intramolecular disulfide bonds.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

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 similarity1 Publication

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi253 – 2553GPR motif; interaction with ITGAX/ITGB2 heterodimerCurated

Sequence similaritiesi

Belongs to the rotavirus VP7 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001963. VP7.
[Graphical view]
PfamiPF00434. VP7. 1 hit.
[Graphical view]
ProDomiPD000191. VP7. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P03533-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MYGIEYTTVL TFLISIILLN YILKSLTRIM DCIIYRLLFI IVILSPFLRA
60 70 80 90 100
QNYGINLPIT GSMDTAYANS TQEETFLTST LCLYYPTEAA TEINDNSWKD
110 120 130 140 150
TLSQLFLTKG WPTGSVYFKE YTNIASFSVD PQLYCDYNVV LMKYDATLQL
160 170 180 190 200
DMSELADLIL NEWLCNPMDI TLYYYQQTDE ANKWISMGSS CTIKVCPLNT
210 220 230 240 250
QTLGIGCLTT DATTFEEVAT AEKLVITDVV DGVNHKLDVT TATCTIRNCK
260 270 280 290 300
KLGPRENVAV IQVGGSDILD ITADPTTAPQ TERMMRINWK KWWQVFYTVV
310 320
DYVDQIIQVM SKRSRSLNSA AFYYRV
Length:326
Mass (Da):37,120
Last modified:July 20, 1986 - v1
Checksum:iC75549FD1F2A0C31
GO
Isoform 2 (identifier: P03533-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:297
Mass (Da):33,732
Checksum:i91AE8498DCF78BF3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161I → T in AAA47307 (PubMed:6323768).Curated
Sequence conflicti32 – 321C → F in AAA47307 (PubMed:6323768).Curated
Sequence conflicti37 – 371L → F in AAA47307 (PubMed:6323768).Curated
Sequence conflicti60 – 601T → A in AAA47307 (PubMed:6323768).Curated
Sequence conflicti75 – 751T → P in AAA47307 (PubMed:6323768).Curated
Sequence conflicti114 – 1141G → E in AAA47307 (PubMed:6323768).Curated
Sequence conflicti219 – 2191A → P in AAA47307 (PubMed:6323768).Curated
Sequence conflicti269 – 2691L → H in CAA24788 (PubMed:6304692).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. CuratedVSP_036750Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01190 Unassigned RNA. Translation: CAA24510.1.
V01546 Genomic RNA. Translation: CAA24788.1.
K02028 Genomic RNA. Translation: AAA47307.1.
PIRiA04135. VGXR1S.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01190 Unassigned RNA. Translation: CAA24510.1.
V01546 Genomic RNA. Translation: CAA24788.1.
K02028 Genomic RNA. Translation: AAA47307.1.
PIRiA04135. VGXR1S.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR001963. VP7.
[Graphical view]
PfamiPF00434. VP7. 1 hit.
[Graphical view]
ProDomiPD000191. VP7. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

  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(1982) [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(1983) [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(1984) [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(1986) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN INTEGRIN HETERODIMER ITGAX/ITGB2, INTERACTION WITH INTEGRIN HETERODIMER ITGA5/ITGB3.

Entry informationi

Entry nameiVP7_ROTS1
AccessioniPrimary (citable) accession number: P03533
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: July 20, 1986
Last modified: January 6, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

In group A rotaviruses, VP7 defines the G serotype.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.