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Protein

Outer capsid glycoprotein VP7

Gene
N/A
Organism
Rotavirus A (isolate RVA/Dog/United States/K9/1981/G3P5A[3]) (RV-A)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. 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. Following entry into the host cell, low intracellular or intravesicular Ca2+ concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.UniRule annotation

Miscellaneous

Some rotavirus strains are neuraminidase-sensitive and require sialic acid to attach to the cell surface. Some rotavirus strains are integrin-dependent. Some rotavirus strains depend on ganglioside for their entry into the host cell. Hsp70 also seems to be involved in the entry of some strains.UniRule annotation
In group A rotaviruses, VP7 defines the G serotype.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi95Calcium 1UniRule annotation1
Metal bindingi177Calcium 2UniRule annotation1
Metal bindingi206Calcium 1; via carbonyl oxygenUniRule annotation1
Metal bindingi214Calcium 1; via carbonyl oxygenUniRule annotation1
Metal bindingi216Calcium 1UniRule annotation1
Metal bindingi228Calcium 2UniRule annotation1
Metal bindingi229Calcium 2; via carbonyl oxygenUniRule annotation1
Metal bindingi231Calcium 2UniRule annotation1
Metal bindingi301Calcium 2UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processHost-virus interaction
LigandCalcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid glycoprotein VP7UniRule annotation
OrganismiRotavirus A (isolate RVA/Dog/United States/K9/1981/G3P5A[3]) (RV-A)
Taxonomic identifieri557232 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiCanis lupus familiaris (Dog) (Canis familiaris) [TaxID: 9615]

Subcellular locationi

  • Virion UniRule annotation
  • Host endoplasmic reticulum lumen UniRule annotation
  • Note: The outer layer contains 780 copies of VP7, grouped as 260 trimers. 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.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 50UniRule annotationAdd BLAST50
ChainiPRO_000036909951 – 326Outer capsid glycoprotein VP7UniRule annotationAdd BLAST276

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi69N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi82 ↔ 135UniRule annotation
Disulfide bondi165 ↔ 249UniRule annotation
Disulfide bondi191 ↔ 244UniRule annotation
Disulfide bondi196 ↔ 207UniRule annotation

Post-translational modificationi

N-glycosylated.UniRule annotation
The N-terminus is blocked possibly by pyroglutamic acid.UniRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO10695

Interactioni

Subunit structurei

Homotrimer; disulfide-linked. 2 Ca2+ ions bound at each subunit interface in the trimer hold the trimer together. Interacts with the intermediate capsid protein VP6. Interacts with the outer capsid protein VP5*.UniRule annotation

Structurei

3D structure databases

SMRiO10695
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni51 – 78Disorded; interaction with the intermediate capsid protein VP6UniRule annotationAdd BLAST28
Regioni165 – 167CNP motif; interaction with ITGAV/ITGB3UniRule annotation3
Regioni237 – 239LVD motif; interaction with ITGA4/ITGB1 heterodimerUniRule annotation3
Regioni253 – 255GPR motif; interaction with ITGAX/ITGB2UniRule annotation3
Regioni312 – 326DisordedUniRule annotationAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi240 – 245Poly-Thr6

Sequence similaritiesi

Belongs to the rotavirus VP7 family.UniRule annotation

Keywords - Domaini

Signal

Family and domain databases

HAMAPiMF_04130 Rota_VP7, 1 hit
MF_04131 Rota_VP7_A, 1 hit
InterProiView protein in InterPro
IPR001963 VP7
PfamiView protein in Pfam
PF00434 VP7, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000191 VP7, 1 hit

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: O10695-1) [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
MYGIEYTTIL TFLISFIFLN YMLKSLTRMM DFIIYRFLFI IVILSPLIKA
60 70 80 90 100
QNYGINLPIT GSMDADYANS TQEETFLTST LCLYYPTEAA SEINDNSWKD
110 120 130 140 150
TLSQLFLTKG WPTGSVYFKE YTDIASFSVD PQLYCDYNIV LMKYDAALQL
160 170 180 190 200
DMSELADLIL NEWLCNPMDI TLYYYQQTDE ANKWISMGSS CTIKVCPLNT
210 220 230 240 250
QTLGIGCLTT DVSTFEEVAT TEKLVITDVV DGVNHKLDVT TTTCTIRNCK
260 270 280 290 300
KLGPRENVAV IQVGGSDILD ITADPTTAPQ TERMMRINWK KWWQVFYTVV
310 320
DYVNQIIQAM SKRSRSLNSA AFYYRV
Length:326
Mass (Da):37,284
Last modified:July 1, 1997 - v1
Checksum:iF52E254989A20000
GO
Isoform 2 (identifier: O10695-2) [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. No experimental confirmation available.
Show »
Length:297
Mass (Da):33,778
Checksum:i26BA070D622B3A77
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0385881 – 29Missing in isoform 2. CuratedAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97199 Genomic RNA Translation: AAB58063.1

Keywords - Coding sequence diversityi

Alternative initiation

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97199 Genomic RNA Translation: AAB58063.1

3D structure databases

SMRiO10695
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO10695

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

HAMAPiMF_04130 Rota_VP7, 1 hit
MF_04131 Rota_VP7_A, 1 hit
InterProiView protein in InterPro
IPR001963 VP7
PfamiView protein in Pfam
PF00434 VP7, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000191 VP7, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiVP7_ROTD9
AccessioniPrimary (citable) accession number: O10695
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 1997
Last modified: June 20, 2018
This is version 60 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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