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B3SRX5

- VP4_ROTWI

UniProt

B3SRX5 - VP4_ROTWI

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Protein
Outer capsid protein VP4
Gene
N/A
Organism
Rotavirus A (isolate Human/United States/WI61/1983 G9-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 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. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment By similarity.
VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei230 – 2312Cleavage By similarity
Sitei246 – 2472Cleavage By similarity

GO - Biological processi

  1. permeabilization of host organelle membrane involved in viral entry into host cell Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Viral penetration via permeabilization of host membrane, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid protein VP4
Alternative name(s):
Hemagglutinin
Cleaved into the following 2 chains:
OrganismiRotavirus A (isolate Human/United States/WI61/1983 G9-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A)
Taxonomic identifieri578830 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000006580: Genome

Subcellular locationi

Chain Outer capsid protein VP4 : Virion By similarity. Host rough endoplasmic reticulum 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.
Chain Outer capsid protein VP8* : Virion
Note: Outer capsid protein By similarity.
Chain Outer capsid protein VP5* : Virion
Note: Outer capsid protein By similarity.

GO - Cellular componenti

  1. host cell rough endoplasmic reticulum Source: UniProtKB-SubCell
  2. viral outer capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host endoplasmic reticulum, Outer capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 775775Outer capsid protein VP4
PRO_0000368113Add
BLAST
Chaini1 – 230230Outer capsid protein VP8*
PRO_0000368114Add
BLAST
Chaini247 – 775529Outer capsid protein VP5*
PRO_0000368115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi56 – 561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi97 – 971N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi132 – 1321N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi317 ↔ 379 Reviewed prediction
Glycosylationi324 – 3241N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi385 – 3851N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi583 – 5831N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi589 – 5891N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi592 – 5921N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi599 – 5991N-linked (GlcNAc...); by host Reviewed prediction

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

VP4 is a homotrimer Reviewed prediction. VP4 adopts a dimeric appearance above the capsid surface, while forming a trimeric base anchored inside the capsid layer. Only hints of the third molecule are observed above the capsid surface. It probably performs a series of molecular rearrangements during viral entry. Prior to trypsin cleavage, it is flexible. The priming trypsin cleavage triggers its rearrangement into rigid spikes with approximate two-fold symmetry of their protruding parts. After an unknown second triggering event, cleaved VP4 may undergo another rearrangement, in which two VP5* subunits fold back on themselves and join a third subunit to form a tightly associated trimer, shaped like a folded umbrella. VP5* is a homotrimer Reviewed prediction. The trimer is coiled-coil stabilized by its C-terminus, however, its N-terminus, known as antigen domain or "body", seems to be flexible allowing it to self-associate either as a dimer or a trimer. The two- to three-fold reorganization and fold-back of VP5* may be linked to membrane penetration, by exposing its hydrophobic region. Interacts with host ITGA2 (via ITAG2 I-domain); this interaction occurs when ITGA2 is part of the integrin heterodimer ITGA2/ITGB1. Interacts with host integrin heterodimer ITGA4/ITGB1 and ITGA4/ITGB7 By similarity.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni247 – 479233Antigen domain By similarity
Add
BLAST
Regioni307 – 3093DGE motif; interaction with ITGA2/ITGB1 heterodimer By similarity
Regioni388 – 40821Hydrophobic; possible role in virus entry into host cell Reviewed prediction
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili483 – 51735 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi559 – 61557Ser-rich
Add
BLAST

Sequence similaritiesi

Belongs to the rotavirus VP4 family.

Keywords - Domaini

Coiled coil

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000416. Haemagglutinin_VP4.
[Graphical view]
PfamiPF00426. VP4_haemagglut. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B3SRX5-1 [UniParc]FASTAAdd to Basket

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MASLIYRQLL TNSYSVDLHD EIEQIGSEKT QNVTVNPGPF AQTRYAPVNW    50
GHGEINDSTT VEPILDGPYQ PTTFTPPIDY WILINSNTNG VVYESTNNSD 100
FWTAVVAVEP HVNPVDRQYT VFGENKQFNV RNDSDKWKFL EMFRSSSQNE 150
FYNRRTLTSH TKLVGILKYG GRIWTFHGET PRATTDSSNT ANLNDISIIV 200
HSEFYIIPRS QESKCNEYIN NGLPPIQNTR NVVPLSLSSR SIQYKRAQVN 250
EDITISKTSL WKEMQYNSDI IIRFKFGNSI VKLGGLGYKW SEISFKAANY 300
QYNYLRDGEQ VTAHTTCSVN GVNNFSYNGG SLPTDFSVSR YEVIKENSYV 350
YVDYWDDSKA FRNMVYVRSL AANLNSVKCT GGSYNFSLPV GAWPVMNGGA 400
VSLHFAGVTL STQFTDFVSL NSLRFRFSLT VDEPSFSILR TRTVNLYGLP 450
AANPNNGNEY YEISGRFSLI SLVPTNDDYQ TPIMNSVTVR QDLERQLTDL 500
REEFNSLSQE IAMSQLIDLA LLPLDMFSMF SGIKSTIDLT KSMATSVMKK 550
FRKSKLATSI SEMTNSLSDA ASSASRSVSI RSNISTISNL TNVSNDVSNV 600
TNSLNDISTQ TSTISKKLRL REMITQTEGM SFDDISAAVL KTKIDMSTQI 650
GKNTLPDIVT EASEKFIPKR SYRILKDDEV MEINTEGKVF AYKIDTLNEV 700
PFDVNKFAEL VTNSPVISAI IDFKTLKNLN DNYGITRIEA LNLIKSNPNV 750
LRNFINQNNP IIRNRIEQLI LQCKL 775
Length:775
Mass (Da):87,376
Last modified:September 2, 2008 - v1
Checksum:i2A827F1C5C695822
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF672619 Genomic RNA. Translation: ABV53300.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF672619 Genomic RNA. Translation: ABV53300.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000416. Haemagglutinin_VP4.
[Graphical view ]
Pfami PF00426. VP4_haemagglut. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Group A human rotavirus genomics: evidence that gene constellations are influenced by viral protein interactions."
    Heiman E.M., McDonald S.M., Barro M., Taraporewala Z.F., Bar-Magen T., Patton J.T.
    J. Virol. 82:11106-11116(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiVP4_ROTWI
AccessioniPrimary (citable) accession number: B3SRX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 30 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, VP4 defines the P serotype.
This strain has been shown to be sialic acid-independent in cell culture conditions By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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