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P15155

- VP4_ROTGI

UniProt

P15155 - VP4_ROTGI

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus B (isolate Rat/United States/IDIR/1984) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      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 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 By similarity.By similarity
    VP8* forms the head of the spikes.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei207 – 2082CleavageSequence Analysis
    Sitei214 – 2152CleavageSequence 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 B (isolate Rat/United States/IDIR/1984) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
    Taxonomic identifieri28877 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    Rattus norvegicus (Rat) [TaxID: 10116]

    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 By similarity
    Note: Outer capsid protein.By similarity
    Chain Outer capsid protein VP5* : Virion By similarity
    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 – 751751Outer capsid protein VP4PRO_0000149539Add
    BLAST
    Chaini1 – 207207Outer capsid protein VP8*Sequence AnalysisPRO_0000369840Add
    BLAST
    Chaini215 – 751537Outer capsid protein VP5*Sequence AnalysisPRO_0000369841Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi23 – 231N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi141 – 1411N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi211 – 2111N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi276 – 2761N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi292 – 2921N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi528 – 5281N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi678 – 6781N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi699 – 6991N-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

    Glycoprotein

    Interactioni

    Subunit structurei

    VP4 is a homotrimer.Curated

    Structurei

    3D structure databases

    ProteinModelPortaliP15155.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the rotavirus VP4 family.Curated

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15155-1 [UniParc]FASTAAdd to Basket

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    MLAYLRREWQ SYGETVIAEG TFNSTSSDSS QSEKPIKTDG RYCYQAEIGR    50
    NAYSMDARGF MLGESDRHVD TTQFLPYTGY ITDGIKYCNI EPPCGTLLRM 100
    HFDVSGDVSV DMHRVASIYV EVDSVTYDGS QYTIRGYRDR NLTATETQKK 150
    LIFYGFRKLG MIGMTGNGRV MLTSTIIQKI SYKHQFTFQM HSESYVWGPC 200
    SGRIKTRVQG NDSRIIIYEQ EDGFWKILKE TLWIKLKPYF KPYGTMGGAF 250
    KNWLIDSGFE KHEYTYSYER DGQVVNATTV TYVKPTGKAG INQSWRPATD 300
    YNGQFTVLQP EDEFSVWYFE DKWQISQAIY AKNFQSDSQV EGELTNNGAL 350
    IFKMNYIPSL AGITNKGGKV KYRYISGGFA QIDTSRHTGL AIILNFKCYG 400
    KKFYADNNNY PVDNALNPYI CYIGDSYTLS GGTHYRQGAC AGFAAGYDDE 450
    ITEHDMTISY TVMKPSDPDF VTGGDNYGQT VTSDIERSIR DLQDQINSIL 500
    AEMNIQQVTS AVFTAITNLG ELPSLFSNIT KVFNRAKDNI KKLRSRSNSD 550
    ISPIGATKII DKTTLETPQL SVINRMPEEY ELGIIYNSMR TRKLIDERKH 600
    DFDTFAVATE MELPYISKVN TLTKEFKDYL KKPGLLSNDD VAVQIDPMNN 650
    RLSVLRRKYA DIIEYKIDPE LAHEVLSNMS NSATRSLFSL NVRKQIAMNN 700
    SFSEPTFSQI IDRMFDDGQL IDVLNNLNRE TATELFDEFL TRIKSMLVKM 750
    S 751
    Length:751
    Mass (Da):85,558
    Last modified:April 1, 1990 - v1
    Checksum:i756A33227C065709
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16949 Genomic RNA. Translation: CAA34823.1.
    PIRiA33093. WMXRGB.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16949 Genomic RNA. Translation: CAA34823.1 .
    PIRi A33093. WMXRGB.

    3D structure databases

    ProteinModelPortali P15155.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "The complete nucleic acid sequence of gene segment 3 of the IDIR strain of group B rotavirus."
      Sato S., Yolken R.H., Eiden J.J.
      Nucleic Acids Res. 17:10113-10113(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiVP4_ROTGI
    AccessioniPrimary (citable) accession number: P15155
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3