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Q8JNB4

- VP4_ROTW3

UniProt

Q8JNB4 - VP4_ROTW3

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (strain Cow/United States/WC3/1981 G6-P7[5]-I2-R2-C2-M2-A3-N2-T6-E2-H3) (RV-A) (Rotavirus (strain Wistar calf 3))
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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
    Sitei231 – 2322CleavageBy similarity
    Sitei247 – 2482CleavageSequence Analysis

    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 Cow/United States/WC3/1981 G6-P7[5]-I2-R2-C2-M2-A3-N2-T6-E2-H3) (RV-A) (Rotavirus (strain Wistar calf 3))
    Taxonomic identifieri578828 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiBos taurus (Bovine) [TaxID: 9913]
    ProteomesiUP000007181: 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 – 776776Outer capsid protein VP4PRO_0000368134Add
    BLAST
    Chaini1 – 231231Outer capsid protein VP8*PRO_0000368135Add
    BLAST
    Chaini248 – 776529Outer capsid protein VP5*PRO_0000368136Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi318 ↔ 380Sequence Analysis
    Glycosylationi507 – 5071N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi593 – 5931N-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

    ProteinModelPortaliQ8JNB4.
    SMRiQ8JNB4. Positions 65-224, 253-522.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni248 – 480233Antigen domainBy similarityAdd
    BLAST
    Regioni308 – 3103DGE motif; interaction with ITGA2/ITGB1 heterodimerBy similarity
    Regioni389 – 40921Hydrophobic; possible role in virus entry into host cellSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili484 – 51835Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi560 – 61657Ser-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.

    Q8JNB4-1 [UniParc]FASTAAdd to Basket

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    MASLIYRQLL ANSYAVDLSD EIQSVGSEKN QRVTVNPGPF AQTVYAPVNW    50
    GPGEVNDSTV VQPVLDGPYQ PASFDLPVGN WMLLAPTGPG VVVEGTDNSG 100
    RWLSVILIEP GVTSETRTYT MFGSSKQVLV SNASDTKWKF VEMMKTAIDG 150
    DYAEWGTLLS DTKLYGMMKY GKRLFIYEGE TPNATTKRYI VTNYASVEVR 200
    PYSDFYIISR SQESACTEYI NNGLPPIQNT RNVVPVAIVS RSIKPREVQA 250
    NEDIVVSKTS LWKEMQYNRD IIIRFKFDNS IIKSGGLGYK WAEISFKAAN 300
    YQYNYMRDGE DVTAHTTCSV NGVNDFSFNG GSLPTDFAIS RYEVIKENSY 350
    VYVDYWDDSQ AFRNMVYVRS LAANLNDVMC SGGHYSFALP AGQWPVMKGG 400
    AVTLHTAGVT LSTQFTDYVS LNSLRFRFRL AAEEPSFTIT RTRVSKLYGI 450
    PAANPNGGRE YYEVAGRFSL ISLVPSNDDY QTPIMNSVTV RQYLERHLNE 500
    LREEFNNLSQ EIAVSQLIDL AMLPLDMFSM FSGIESTVNA AKSMATNVMR 550
    KFKSSKLASS VSMLRDSLSD GASSIARSTS IRSIGSTASA WANISERTQD 600
    AVNEVATISS QVSQISGKLR LKEITTQTEG MNFDDVSGAV LKAKIDRSIQ 650
    VDQNALPDVI TEASEKFIRN RAYRVIDGDE AFEAGTDGRF FAYKVETLEE 700
    MPFNIEKFAD LVTNSPVISA IIDFKTLKNL NDNYGITREQ AFNLLRSNPK 750
    VLRGFIDQNN PIIKNRIEQL IMQCRL 776
    Length:776
    Mass (Da):86,571
    Last modified:October 1, 2002 - v1
    Checksum:iBE2BC5021142F121
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY050271 mRNA. Translation: AAL11027.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY050271 mRNA. Translation: AAL11027.1 .

    3D structure databases

    ProteinModelPortali Q8JNB4.
    SMRi Q8JNB4. Positions 65-224, 253-522.
    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. "Sequence analysis of the VP4, VP6, VP7, and NSP4 gene products of the bovine rotavirus WC3."
      Ciarlet M., Hyser J.M., Estes M.K.
      Virus Genes 24:107-118(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiVP4_ROTW3
    AccessioniPrimary (citable) accession number: Q8JNB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 64 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