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P21284

- VP4_ROTHL

UniProt

P21284 - VP4_ROTHL

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (strain Human/Philippines/L26/1987 G12-P1B[4]-I2-R2-C2-M1/M2-A2-N1-T2-E2-H1) (RV-A)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      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 (strain Human/Philippines/L26/1987 G12-P1B[4]-I2-R2-C2-M1/M2-A2-N1-T2-E2-H1) (RV-A)
    Taxonomic identifieri10953 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000001459: 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_0000041063Add
    BLAST
    Chaini1 – 230230Outer capsid protein VP8*Sequence AnalysisPRO_0000041064Add
    BLAST
    Chaini247 – 775529Outer capsid protein VP5*Sequence AnalysisPRO_0000041065Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi32 – 321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi97 – 971N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi150 – 1501N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi195 – 1951N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi317 ↔ 379Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi583 – 5831N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi589 – 5891N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi599 – 5991N-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

    Structurei

    3D structure databases

    ProteinModelPortaliP21284.
    SMRiP21284. Positions 60-223, 252-521.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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.

    P21284-1 [UniParc]FASTAAdd to Basket

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    MASLIYRQLL TNSYSVDLHD EIEQIGSEKT QNVTINPGPF AQTRYAPVNW    50
    RHGEINDSTT VEPVLDGPYQ PTTFKPPNDY WLLISSNTDG VVYESTNNSD 100
    FWTAVIAVEP RVSQTNRQYI LFGENKQFNI ENNSDKWKFF EMFKGSSQSN 150
    FSNRRTLTSN NRLVGMLKYG GRVWTFHGET PRATTDSSNT ADLNNISIVI 200
    HSEFYIIPRS QESKCNEYIN NGLPPIQNTR NVVPLSLSSR SIQYRRAQVN 250
    EDITISKTSL WKEMQYNRDI IIRFKFGNSV IKLGGLGYKW SEISYKAANY 300
    QYSYSRDGEQ VTAHTTCSVN GVNNFSYNGG SLPTDFSISR YEVIKENSYV 350
    YIDYWDDSKA FRNMVYVRSL AANLNSVKCA GGSYNFRLPV GEWPIMNGGA 400
    VSLHFAGVTL STQFTNFVSL NSLRFRFSLT VDEPSFSIIR TRTVNLYGLP 450
    AANPNNGNEY YEMSGRFSLI SLVPTNDDYQ TPIMNSVTVR QDLERQLSDL 500
    REEFNSLSQE IAMSQLIDLA LLPLDMFSMF SGIKSTIDLT KSMATSVMKK 550
    FRKSKLATSI SEMTNSLSDA ASSASRSASV RSNLSVISNW TDASKSTSNI 600
    TDLVNDVSTQ TSTISKKLRL KEMITQTEGM SFDDISAAVL KTKIDMSTQI 650
    GKNTLPDIVT EASEKFIPKR SYRVLKDNEV MEINTEGKFF AYKVDTLNEI 700
    PFDINKFAEL VTDSPVISAI IDFKTLKNLN DNYGITRMEA LNLIKSNPNV 750
    LRNFINQNNP IIRNRIEQLI LQCKL 775
    Length:775
    Mass (Da):87,651
    Last modified:May 1, 1991 - v1
    Checksum:i40CA498305DECD63
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1501N → D in ABV53268. (PubMed:18786998)Curated
    Sequence conflicti416 – 4161N → D in ABV53268. (PubMed:18786998)Curated
    Sequence conflicti479 – 4791Y → H in ABV53268. (PubMed:18786998)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511R → G in strain: L27.
    Natural varianti392 – 3921E → K in strain: L27.
    Natural varianti405 – 4051F → C in strain: L27.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58292 Genomic RNA. Translation: AAA47335.1.
    EF672591 Genomic RNA. Translation: ABV53268.1.
    PIRiA36410. VPXRWL.
    C36410. VPXRWM.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58292 Genomic RNA. Translation: AAA47335.1 .
    EF672591 Genomic RNA. Translation: ABV53268.1 .
    PIRi A36410. VPXRWL.
    C36410. VPXRWM.

    3D structure databases

    ProteinModelPortali P21284.
    SMRi P21284. Positions 60-223, 252-521.
    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. "Nucleotide sequence of VP4 and VP7 genes of human rotaviruses with subgroup I specificity and long RNA pattern: implication for new G serotype specificity."
      Taniguchi K., Urasawa T., Kobayashi N., Gorziglia M., Urasawa S.
      J. Virol. 64:5640-5644(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: L26 and L27.
    2. "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_ROTHL
    AccessioniPrimary (citable) accession number: P21284
    Secondary accession number(s): B3SRU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 89 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