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)

Q998M5

- VP4_ROTEO

UniProt

Q998M5 - VP4_ROTEO

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (isolate Equine/Japan/HO-5/1980 G3-Px[x]-I6-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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
    Sitei231 – 2322CleavageBy similarity
    Sitei247 – 2482CleavageBy 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 Equine/Japan/HO-5/1980 G3-Px[x]-I6-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A)
    Taxonomic identifieri148357 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusunclassified rotaviruses
    Virus hostiEquus caballus (Horse) [TaxID: 9796]

    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_0000368101Add
    BLAST
    Chaini1 – 231231Outer capsid protein VP8*PRO_0000368102Add
    BLAST
    Chaini248 – 776529Outer capsid protein VP5*PRO_0000368103Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi32 – 321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi111 – 1111N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi133 – 1331N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi318 ↔ 380Sequence 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

    ProteinModelPortaliQ998M5.
    SMRiQ998M5. Positions 64-224, 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.

    Q998M5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASLIYRQLL ANSYTVDLSD EIENIGYAKS KNVTINPGPF AQTGYAPVNW    50
    GPGEVNDSTT VEPVLDGPYQ PTNFNPPVNY WMLLSPLNAG VVVEGTNSID 100
    RWLATVLVEP NVTTTVRTYT LFGVQEQISV ENNSTTKWKF INLIKTTPSG 150
    NFTLYSTLLS EPKLHGIMKH GGQLWVYNGE TPNATTTGYV TSNYDSLTMT 200
    SFCDFYIIPR NQESTCTEYI NNGLPPIQNT RNVVSVSISS RNIIHNRAQV 250
    NEDIVISKTS LWKEVQYNRD ITIRFRFANA IIKSGGLGYK WSEISFKPAN 300
    YQYTYTRDGE EITAHTTCSV NGVNDFSFNG GSLPTDFVIS RYEVIKENSY 350
    VYVDYWDDSQ AFRNVVYVRS LAANLNDVLC TGGDYNFALP VGQWPVMTGG 400
    AVMLHAAGVT LSTQFTDFVS LNSLKFRFSL SAEEPYFSIT RTRVTRLYGL 450
    PAVNPNNDRD YYEIAGRFSL ISLVPSNDDY QTPIMNSVTV RQDLERQLGE 500
    LREEFNALSQ EIAISQLIDL ALLPLDMFSM FSGIKSTIDA AKSMATNVMK 550
    KFKKSKLASS VSTLTDSLSD AASSVSRSSS IRSVSSSVSA WTDVSDQLTD 600
    ISNSVNSIST QTSTISRRLR LKEIATQTEG MNFDDISAAV LKTKIDKSTQ 650
    IAANNIPDVI TEASEKFIPN RAYRVISNDN VFEASTDGRF FAYKVGTFEE 700
    IPFDVQKFAD LVTDSPVISA IIDFKTLKNL NDNYGITREQ AFNLLRSDPR 750
    VLREFINQDN PIIKNRIEQL ILQCRL 776
    Length:776
    Mass (Da):86,658
    Last modified:June 1, 2001 - v1
    Checksum:i5E92A0551F0C86ED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046471 Genomic RNA. Translation: BAB40369.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046471 Genomic RNA. Translation: BAB40369.1 .

    3D structure databases

    ProteinModelPortali Q998M5.
    SMRi Q998M5. Positions 64-224, 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. "Identification of Equine Rotavirus VP4 and VP7 Types by PCR."
      Tsunemitsu H., Imagawa H.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiVP4_ROTEO
    AccessioniPrimary (citable) accession number: Q998M5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 66 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.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3