A9Q1L0 (VP4_ROTB2) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 25. History...
Names and origin
|Protein names||Recommended name:|
Outer capsid protein VP4
|Organism||Rotavirus (isolate Human/Bangladesh/ADRV-N B219/2002) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219)) [Complete proteome]|
|Taxonomic identifier||348136 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus › unclassified rotaviruses|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||826 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors By similarity.
Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm By similarity.
VP8* forms the head of the spikes By similarity.
VP4 is a homotrimer Potential.
Outer capsid protein VP4: Virion By similarity. Host rough endoplasmic reticulum 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.
Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion By similarity.
Belongs to the rotavirus VP4 family.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 826||826||Outer capsid protein VP4||PRO_0000369842|
|Chain||1 – 249||249||Outer capsid protein VP8* Potential||PRO_0000369843|
|Chain||263 – 826||564||Outer capsid protein VP5* Potential||PRO_0000369844|
|Compositional bias||260 – 263||4||Poly-Lys|
|Site||249 – 250||2||Cleavage Potential|
|Site||262 – 263||2||Cleavage Potential|
Amino acid modifications
|Glycosylation||143||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||153||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||198||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||333||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||487||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||494||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||514||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||561||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||804||1||N-linked (GlcNAc...); by host Potential|
|||"Whole genomic characterization of a human rotavirus strain B219 belonging to a novel group of the genus Rotavirus."|
Nagashima S., Kobayashi N., Ishino M., Alam M.M., Ahmed M.U., Paul S.K., Ganesh B., Chawla-Sarkar M., Krishnan T., Naik T.N., Wang Y.-H.
J. Med. Virol. 80:2023-2033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PUTATIVE CLEAVAGE SITES.
|EF453358 mRNA. Translation: ABR32125.1.|
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR000416. Haemagglutinin_VP4. |
|Pfam||PF00426. VP4_haemagglut. 1 hit. |
|Accession||Primary (citable) accession number: A9Q1L0|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families