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O11982

- NSP4_ROTME

UniProt

O11982 - NSP4_ROTME

Protein

Non-structural glycoprotein 4

Gene
N/A
Organism
Rotavirus A (isolate Mouse/Brazil/EHP/1981 G16-Px[20]-Ix-Rx-Cx-Mx-A7-Nx-Tx-E7-Hx) (RV-A)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Involved in virus morphogenesis. Functions as a receptor for the immature double-layered inner capsid particle (ICP) which transiently buds into the lumen of the rough endoplasmic reticulum during viral maturation By similarity.By similarity
    Enterotoxin that causes a phospholipase C-dependent elevation of the intracellular calcium concentration in host intestinal mucosa cells. Increased concentration of intracellular calcium disrupts the cytoskeleton and the tight junctions, raising the paracellular permeability. Potentiates chloride ion secretion through a calcium ion-dependent signaling pathway, inducing age-dependent diarrhea. To perform this enterotoxigenic role in vivo, NSP4 is probably released from infected enterocytes in a soluble form capable of diffusing within the intestinal lumen and interacting with the plasma membrane receptors on neighboring epithelial cells. Possible receptors for NSP4 are alpha-1/beta-1 and alpha-2/beta-1 integrin heterodimers By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi120 – 1201Calcium; shared with all tetrameric partners; partialBy similarity
    Metal bindingi123 – 1231Calcium; shared with all tetrameric partnersBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW
    2. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Enterotoxin, Toxin

    Keywords - Biological processi

    Host-virus interaction, Virulence

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-structural glycoprotein 4
    Short name:
    NSP4
    Alternative name(s):
    NCVP5
    NS28
    OrganismiRotavirus A (isolate Mouse/Brazil/EHP/1981 G16-Px[20]-Ix-Rx-Cx-Mx-A7-Nx-Tx-E7-Hx) (RV-A)
    Taxonomic identifieri578840 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiMus musculus musculus (eastern European house mouse) [TaxID: 39442]

    Subcellular locationi

    Chain Non-structural glycoprotein 4 : Host rough endoplasmic reticulum membrane By similarity; Single-pass type III membrane protein By similarity. Host membranehost caveola; Single-pass type III membrane protein. Secreted By similarity
    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. NSP4 also localizes in vesicular structures, which contain an autophagosomal marker and associate with viroplasms in virus-infected cells By similarity.By similarity

    GO - Cellular componenti

    1. host caveola Source: UniProtKB-SubCell
    2. host cell rough endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host endoplasmic reticulum, Host membrane, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 175175Non-structural glycoprotein 4PRO_0000369471Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi8 – 81N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi18 – 181N-linked (GlcNAc...); by hostSequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer. Forms a complex with the ICP. Interacts, via the active enterotoxic peptide region, with host CAV1, early and late in infection. Interacts with host integrin ITGA1/ITGB1 heterodimer. Interacts with host integrin ITGA2/ITGB1 heterodimer. Interaction with microtubules blocks trafficking to the Golgi apparatus By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO11982.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2828LumenalBy similarityAdd
    BLAST
    Topological domaini52 – 175124CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei29 – 5123HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 2115HydrophobicBy similarityAdd
    BLAST
    Regioni67 – 8519HydrophobicBy similarityAdd
    BLAST
    Regioni85 – 12339Endoplasmic reticulum retention signalSequence AnalysisAdd
    BLAST
    Regioni114 – 13522Interaction with CAV1By similarityAdd
    BLAST
    Regioni122 – 17554Required for interaction with microtubulesBy similarityAdd
    BLAST
    Regioni159 – 17517ICP binding domainBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili85 – 11733Sequence AnalysisAdd
    BLAST

    Domaini

    A disordered 28 AA C-terminal domain is presented to the cytoplasm by each subunit of the tetrameric receptor.By similarity
    The coiled coil region mediates oligomerization.By similarity

    Sequence similaritiesi

    Belongs to the rotavirus NSP4 family.Curated

    Keywords - Domaini

    Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

    Family and domain databases

    InterProiIPR002107. Rotavirus_NSP4.
    [Graphical view]
    PfamiPF01452. Rota_NSP4. 1 hit.
    [Graphical view]
    ProDomiPD002202. NSP4_rotavirus. 1 hit.
    [Graphical view] [Entries sharing at least one domain]

    Sequencei

    Sequence statusi: Complete.

    O11982-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKLADLNYT LGVITLLNDT LHNILEEPGM VYFPYVASAL TVLFTMHKAS    50
    LPAMKLAMRT SQCSYRIIKR VVVTLINTLL RLGGYNDYLT DKDETEKQIN 100
    RVVKELRQQL TMIEKLTTRE IEQVELLKRI YDMMVVRHDR EIDMSKETNQ 150
    KAFNTLHDWG NDRNYDDNTD VIAPL 175
    Length:175
    Mass (Da):20,413
    Last modified:July 1, 1997 - v1
    Checksum:i1FD43E74409C6508
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96336 mRNA. Translation: AAB58699.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96336 mRNA. Translation: AAB58699.1 .

    3D structure databases

    ProteinModelPortali O11982.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002107. Rotavirus_NSP4.
    [Graphical view ]
    Pfami PF01452. Rota_NSP4. 1 hit.
    [Graphical view ]
    ProDomi PD002202. NSP4_rotavirus. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    ProtoNeti Search...

    Publicationsi

    1. "Studies of the role for NSP4 in the pathogenesis of homologous murine rotavirus diarrhea."
      Angel J., Tang B., Feng N., Greenberg H.B., Bass D.
      J. Infect. Dis. 177:455-458(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiNSP4_ROTME
    AccessioniPrimary (citable) accession number: O11982
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 43 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds 1 calcium ion per tetramer. The calcium ion is bound by a glutamine from each tetrameric partner and by a glutamic acid from two of the tetrameric partners, while the glutamic acid from the other two partners do not participate in binding the ion By similarity.By similarity

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3