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B3SRR1

- VP4_ROTH7

UniProt

B3SRR1 - VP4_ROTH7

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (isolate Human/United Kingdom/A64/1987 G10-P11[14]-I2-R2-C2-M1-A3-N2-T6-E2-H3) (RV-A)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 31 (01 Oct 2014)
      Sequence version 1 (02 Sep 2008)
      Previous versions | rss
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    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.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.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.By similarity

    Sites

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

    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 Kingdom/A64/1987 G10-P11[14]-I2-R2-C2-M1-A3-N2-T6-E2-H3) (RV-A)
    Taxonomic identifieri578827 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000001456: Genome

    Subcellular locationi

    Chain Outer capsid protein VP4 : Virion By similarity. Host rough endoplasmic reticulum Curated
    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.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

    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 VP4PRO_0000368110Add
    BLAST
    Chaini1 – 230230Outer capsid protein VP8*PRO_0000368111Add
    BLAST
    Chaini247 – 775529Outer capsid protein VP5*PRO_0000368112Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi16 – 161N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi31 – 311N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi96 – 961N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi131 – 1311N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi148 – 1481N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi182 – 1821N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi197 – 1971N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi317 ↔ 379Sequence Analysis
    Glycosylationi586 – 5861N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi613 – 6131N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi629 – 6291N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi677 – 6771N-linked (GlcNAc...); by hostSequence Analysis

    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.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    VP4 is a homotrimer Potential. 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 Potential. 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.By similarityCurated

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni247 – 479233Antigen domainBy similarityAdd
    BLAST
    Regioni307 – 3093DGE motif; interaction with ITGA2/ITGB1 heterodimerBy similarity
    Regioni388 – 40821Hydrophobic; possible role in virus entry into host cellSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili483 – 51735Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi559 – 61557Ser-richAdd
    BLAST
    Compositional biasi756 – 7594Poly-Asn

    Sequence similaritiesi

    Belongs to the rotavirus VP4 family.Curated

    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.

    B3SRR1-1 [UniParc]FASTAAdd to Basket

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    MASLYRQLLS NSYVTNISDE VSEIGARKTT NVTVNPGPFA QTGHAPVNWG    50
    HGELSDSTLV QPTLDGPYQP TTFNLPIDYW MLIAPTQIGR VAEGTNTTDR 100
    WFACVLVEPS VSNTQREYVL DGQTVQLQVS NDSSTLWKFI LFIKLGKNGT 150
    YSQYSTLSTS NKLCAWMKRE GRVYWYAGTT PNASDSYYLT INNDNSNVSC 200
    DAEFYLIPRS QTDLCAQYIN NGLPPIQNTR NIVPVSISSR EIRHTRAQMN 250
    EDIVVSKTSL WKEMQYNRDI TIRFKFANSI VKSGGLGYKW SEISFKPMNY 300
    QYTYTRDGEE ITAHTTCSVN GVNDFSYNGG TLPTDFAISR FEVIKENSYV 350
    YIDYWDDSQA FRNIVYVRSL SANLNDVICS GGDYSFALPV GAYPVMSGGA 400
    VTLSPAGVTL STQFTDYVSL NSLRFRFRLA VSEPSFSISR TRLSGIYGLP 450
    AANPNNNVEY YEIAGRFSLI SLVPTNDDYQ TPIANSVTVR QDLERQLGEL 500
    REEFNSLSQE IALSQLIDLA TLPLDMFSMF SGIKSTVEAV KSMTTNIMKK 550
    FKTSNLANAI SDLTNSMSDA ASSISRSTSI RSVGSNTTMR ISTAIQTGED 600
    LKTMADASTQ ISNVSRSLRL REFTTQTDNL SFDDISAAVL KTKLDKSTQI 650
    SQNTIPDIIS ESSEKFIPMR AYRVMDNDTA FETGIDGTFY AYRVDTFDEV 700
    PFDVEKFNKL ITDSPVLSAI IDFKTLKNLN DNYGITKTQA MELLQSNPRT 750
    LKEFINNNNP IIRNRVENLI AQCRL 775
    Length:775
    Mass (Da):86,650
    Last modified:September 2, 2008 - v1
    Checksum:i2E15FDDF45922F79
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF672563 Genomic RNA. Translation: ABV53236.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF672563 Genomic RNA. Translation: ABV53236.1 .

    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_ROTH7
    AccessioniPrimary (citable) accession number: B3SRR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 31 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