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P12476

- VP7_ROTRH

UniProt

P12476 - VP7_ROTRH

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Protein

Outer capsid glycoprotein VP7

Gene
N/A
Organism
Rotavirus A (strain Monkey/United States/RRV/1980 G3-P5B[3]-I2-R2-C3-M3-A9-Nx-T3-E3-H6) (RV-A)
Status
Reviewed - Annotation score: 3 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 By similarity.

GO - Biological processi

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

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid glycoprotein VP7
OrganismiRotavirus A (strain Monkey/United States/RRV/1980 G3-P5B[3]-I2-R2-C3-M3-A9-Nx-T3-E3-H6) (RV-A)
Taxonomic identifieri10969 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]

Subcellular locationi

Virion By similarity. Host endoplasmic reticulum lumen Reviewed prediction
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.

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 – 5050 Reviewed predictionAdd
BLAST
Chaini51 – 326276Outer capsid glycoprotein VP7 Reviewed predictionPRO_0000149620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi69 – 691N-linked (GlcNAc...); by host Reviewed prediction

Post-translational modificationi

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

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi81 – 866
Helixi87 – 937
Helixi98 – 10811
Beta strandi116 – 1227
Helixi124 – 1296
Beta strandi135 – 1439
Helixi146 – 1483
Helixi152 – 1598
Beta strandi160 – 1678
Turni170 – 1723
Beta strandi182 – 19817
Beta strandi204 – 2074
Helixi212 – 2143
Beta strandi215 – 22713
Beta strandi234 – 2385
Turni241 – 2433
Beta strandi244 – 25411
Beta strandi258 – 2647
Beta strandi273 – 2764
Beta strandi284 – 2874
Helixi292 – 30110
Helixi303 – 3086

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP12476.

Family & Domainsi

Sequence similaritiesi

Belongs to the rotavirus VP7 family.

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. Align

Isoform 1 (identifier: P12476-1) [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

MYGIEYTTVL TFLISLILLN YILKSLTRMM DCIIYRFLFI VVILSPLLKA    50
QNYGINLPIT GSMDTAYANS TQEETFLTST LCLYYPTEAA TEINDNSWKD 100
TLSQLFLTKG WPTGSVYFKE YTDIASFSVD PQLYCDYNVV LMKYDATLQL 150
DMSELADLIL NEWLCNPMDI ALYYYQQTDE ANKWISMGSS CTIKVCPLNT 200
QTLGIGCLTT DTATFEEVAT AEKLVITDVV DGVNHKLDVT TATCTIRNCK 250
KLGPRENVAV IQVGGSDVLD ITADPTTAPQ TERMMRINWK KWWQVFYTVV 300
DYVNQIIQAM SKRSRSLNSA AFYNRI 326
Length:326
Mass (Da):36,989
Last modified:October 1, 1989 - v1
Checksum:i4913E7C879533A30
GO
Isoform 2 (identifier: P12476-2) [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):33,582
Checksum:i2B2C399A9A8A9051
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321C → F in strain: Isolate MMU-18006.
Natural varianti171 – 1711A → T in strain: Isolate MMU-18006.
Natural varianti324 – 3241N → Y in strain: Isolate MMU-18006.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. VSP_038635Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21650 Genomic RNA. Translation: AAA47346.1.
AF295303 mRNA. No translation available.
PIRiA29247. VGXRRH.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21650 Genomic RNA. Translation: AAA47346.1 .
AF295303 mRNA. No translation available.
PIRi A29247. VGXRRH.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FMG X-ray 3.40 A 51-326 [» ]
3GZT electron microscopy 3.80 B/F/G/H/I/J/K/L/M/N/O/P/Q 58-312 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P12476.

Family and domain databases

InterProi IPR001963. VP7.
[Graphical view ]
Pfami PF00434. VP7. 1 hit.
[Graphical view ]
ProDomi PD000191. VP7. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiVP7_ROTRH
AccessioniPrimary (citable) accession number: P12476
Secondary accession number(s): P11855
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

In group A rotaviruses, VP7 defines the G serotype.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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