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Protein

Outer capsid glycoprotein VP7

Gene
N/A
Organism
Rotavirus A (isolate RVA/Cow/United States/B223/1983/G10P8[11]) (RV-A)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

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 - 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/Cow/United States/B223/1983/G10P8[11]) (RV-A)
Taxonomic identifieri1835656 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiBos taurus (Bovine) [TaxID: 9913]

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_000014958251 – 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
Glycosylationi145N-linked (GlcNAc...) asparagine; by hostSequence analysis1
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

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

SMRiP17700
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

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: P17700-1) [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
MYGIEYTTFL IYLISIILLN YILKSITRMM DYIIYKFLLI VTITSIVVNA
60 70 80 90 100
QNYGINLPIT GSMDTSYVNA TKDEPFLTST LCLYYPTEAR TEINDNEWTS
110 120 130 140 150
TLSQLFLTKG WPTGSVYFKE YDDIATFSVD PQLYCDYNIV LMRYNSSLKL
160 170 180 190 200
DMSELANLIL NEWLSNPMDI TLYYYQQTDE ANKWIAMGQS CTIKVCPLNT
210 220 230 240 250
QTLGIGCQTT NTGTFEEVAT AEKLVITDVV DGVNHKLDVT TATCTIRNCK
260 270 280 290 300
KLGPRENVAV IQVGGADILD ITSDPTTNPQ TERMMRINWK KWWQVFYTIV
310 320
DYVNQIVQAM SKRSRSLNSA AFYYRV
Length:326
Mass (Da):37,310
Last modified:August 1, 1990 - v1
Checksum:iD9253D69DD2CE2EE
GO
Isoform 2 (identifier: P17700-2) [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):33,828
Checksum:i63EEDAD2A193C05D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8T → A in CAA40982 (Ref. 2) Curated1
Sequence conflicti65T → S in CAA40982 (Ref. 2) Curated1
Sequence conflicti149K → E in CAA40982 (Ref. 2) Curated1
Sequence conflicti165S → C in CAA40982 (Ref. 2) Curated1
Sequence conflicti178 – 179TD → NG in CAA40982 (Ref. 2) Curated2
Sequence conflicti213G → R in CAA40982 (Ref. 2) Curated1
Sequence conflicti222E → Q in CAA40982 (Ref. 2) Curated1
Sequence conflicti225V → P in CAA40982 (Ref. 2) Curated1
Sequence conflicti231D → V in CAA40982 (Ref. 2) Curated1
Sequence conflicti284M → I in CAA40982 (Ref. 2) Curated1
Sequence conflicti295V → A in CAA40982 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0385861 – 29Missing in isoform 2. CuratedAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52650 Genomic RNA Translation: CAA36875.1
X57852 mRNA Translation: CAA40982.1
PIRiS29562

Keywords - Coding sequence diversityi

Alternative initiation

Similar proteinsi

Entry informationi

Entry nameiVP7_ROTBB
AccessioniPrimary (citable) accession number: P17700
Secondary accession number(s): Q65702
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 23, 2018
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health