Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q08010

- VP4_ROTB9

UniProt

Q08010 - VP4_ROTB9

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (isolate Cow/Germany/993/1983 G18-P[17]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    Sitei229 – 2302CleavageBy similarity
    Sitei243 – 2442CleavageBy 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 Cow/Germany/993/1983 G18-P[17]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A)
    Taxonomic identifieri45408 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiBos taurus (Bovine) [TaxID: 9913]

    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 – 770770Outer capsid protein VP4PRO_0000041015Add
    BLAST
    Chaini1 – 229229Outer capsid protein VP8*Sequence AnalysisPRO_0000041016Add
    BLAST
    Chaini244 – 770527Outer capsid protein VP5*Sequence AnalysisPRO_0000041017Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi32 – 321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi181 – 1811N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi314 ↔ 376Sequence Analysis
    Glycosylationi375 – 3751N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi482 – 4821N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi580 – 5801N-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

    ProteinModelPortaliQ08010.
    SMRiQ08010. Positions 249-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni244 – 476233Antigen domainBy similarityAdd
    BLAST
    Regioni304 – 3063DGE motif; interaction with ITGA2/ITGB1 heterodimerBy similarity
    Regioni385 – 40521Hydrophobic; possible role in virus entry into host cellSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili480 – 51435Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi556 – 60954Ser-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.

    Q08010-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASLVYRQLL ANSYTSDLQD TIDDISAQKT ENVTVNPGPF AQTGYALVEW    50
    THGDITTDET VQQTLDGPYA PSSVIIQPQY WVLMNPETAD VIAEADATNK 100
    KYACVMLAPN TEEGDKQYTI LGRQITINLG NTDQNRYKFF DLASENGETY 150
    SKIQELLTPN RLNAFMKDQG RLYVYHGTVP NISTGYYTLD DIANVQTNIK 200
    CNYYIVPKSQ TQQLEDFLKN GLPPIQESRY IMPVERSVQN IYRAKPNEDI 250
    VISKTSLWKE MQYNRDIVIR FKFGNTIIKS GGLGYKWSEI SYKPMNYEYT 300
    YERDGETVVA HTTCSVAGVN DFGYNSGSLP TDFVVSKYEV LKGNSYVYID 350
    YWDDSQAFKN MVYVRSLSAE FNAINCTGGT YDFQLPVGQW PQMRGGNVTL 400
    NSDAVTLSTQ YTDFVSLNSL RFRFKPAIGE PFFEITRTRE TRLYGLPASN 450
    PMGGNEYYET AGRFSLISLV PSNDDYQTPI QNSTTVRQDL EQQISDLREE 500
    FNQLSSEIAM SQLIDLALLP LDMFSMFSGI KSTIDAVKSV TTSVMKKMKT 550
    STLAKSVSTI TEELSDAATS VSRASSIRSN ASVWNNLVDT RTQTSVATND 600
    IATQTSRIAS KLRVKEFATQ TEGGLSFNDI SAAVLKTKID KIETVQPKIL 650
    PTIITESVDK FIPTRQYRII DKDIAYEISN SGKYFAYRVD TFEEVIFDVE 700
    KFADLVTDSP VISAIIDFKT LKNLNDNFGI TKEQAYNLLR SDPRVLKDFI 750
    NQNNPIIRNR IEQLILQCRI 770
    Length:770
    Mass (Da):86,943
    Last modified:November 1, 1995 - v1
    Checksum:i098650A26312EE3B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16352 mRNA. Translation: BAA03855.1.
    PIRiA49283.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16352 mRNA. Translation: BAA03855.1 .
    PIRi A49283.

    3D structure databases

    ProteinModelPortali Q08010.
    SMRi Q08010. Positions 249-518.
    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. "A unique VP4 gene allele carried by an unusual bovine rotavirus strain, 993/83."
      Isegawa Y., Nakagomi O., Bruessow H., Minamoto N., Nakagomi T., Ueda S.
      Virology 198:366-369(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiVP4_ROTB9
    AccessioniPrimary (citable) accession number: Q08010
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 79 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3