P17700 (VP7_ROTBB) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 72. History...
Names and origin
|Protein names||Recommended name:|
Outer capsid glycoprotein VP7
|Organism||Rotavirus A (isolate Cow/United States/B223/1983 G10-P8-I2-Rx-Cx-Mx-A13-Nx-Tx-E2-Hx) (RV-A)|
|Taxonomic identifier||10930 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus › Rotavirus A ›|
|Virus host||Bos taurus (Bovine) [TaxID: 9913]|
|Sequence length||326 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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.
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.
Virion By similarity. 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 By similarity.
The N-terminus is blocked possibly by pyroglutamic acid By similarity.
N-glycosylated By similarity.
Intramolecular disulfide bonds By similarity.
In group A rotaviruses, VP7 defines the G serotype.
Belongs to the rotavirus VP7 family.
|Biological process||Host-virus interaction|
|Cellular component||Host endoplasmic reticulum|
|Coding sequence diversity||Alternative initiation|
|Molecular function||Capsid protein|
Outer capsid protein
T=13 icosahedral capsid protein
|Gene Ontology (GO)|
|Biological_process||modulation by virus of host morphology or physiology|
Inferred from electronic annotation. Source: UniProtKB-KW
|Cellular_component||T=13 icosahedral viral capsid|
Inferred from electronic annotation. Source: UniProtKB-KWhost cell endoplasmic reticulum lumen
Inferred from electronic annotation. Source: UniProtKB-SubCellviral outer capsid
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
|This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]|
|Isoform 1 (identifier: P17700-1) |
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: P17700-2) |
The sequence of this isoform differs from the canonical sequence as follows:
|Note: Produced by alternative initiation at Met-30 of isoform 1. No experimental confirmation available.|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Signal peptide||1 – 50||50||Potential|
|Chain||51 – 326||276||Outer capsid glycoprotein VP7 Potential||PRO_0000149582|
Amino acid modifications
|Glycosylation||69||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||145||1||N-linked (GlcNAc...); by host Potential|
|Alternative sequence||1 – 29||29||Missing in isoform 2.||VSP_038586|
|Sequence conflict||8||1||T → A in CAA40982. Ref.2|
|Sequence conflict||65||1||T → S in CAA40982. Ref.2|
|Sequence conflict||149||1||K → E in CAA40982. Ref.2|
|Sequence conflict||165||1||S → C in CAA40982. Ref.2|
|Sequence conflict||178 – 179||2||TD → NG in CAA40982. Ref.2|
|Sequence conflict||213||1||G → R in CAA40982. Ref.2|
|Sequence conflict||222||1||E → Q in CAA40982. Ref.2|
|Sequence conflict||225||1||V → P in CAA40982. Ref.2|
|Sequence conflict||231||1||D → V in CAA40982. Ref.2|
|Sequence conflict||284||1||M → I in CAA40982. Ref.2|
|Sequence conflict||295||1||V → A in CAA40982. Ref.2|
|||"Sequence of the gene encoding the major neutralization antigen (VP7) of serotype 10 rotavirus."|
Xu L.I., Harbour D.A., McCrae M.A.
J. Gen. Virol. 72:177-180(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Nucleotide sequence of the VP7 gene of serotype 10 bovine rotavirus strain B223."|
Hardy M.E., Woode G.N.
Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
|X52650 Genomic RNA. Translation: CAA36875.1.|
X57852 mRNA. Translation: CAA40982.1.
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR001963. VP7. |
|Pfam||PF00434. VP7. 1 hit. |
|ProDom||PD000191. VP7. 1 hit. |
[Graphical view] [Entries sharing at least one domain]
|Accession||Primary (citable) accession number: P17700|
Secondary accession number(s): Q65702
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families