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Q82055

- NSP4_ROTHC

UniProt

Q82055 - NSP4_ROTHC

Protein

Non-structural glycoprotein 4

Gene
N/A
Organism
Rotavirus C (isolate Human/United Kingdom/Bristol/1989) (RV-C)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 By similarity.By similarity

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Enterotoxin, Toxin

    Keywords - Biological processi

    Virulence

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-structural glycoprotein 4
    Short name:
    NSP4
    OrganismiRotavirus C (isolate Human/United Kingdom/Bristol/1989) (RV-C)
    Taxonomic identifieri31567 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007664: Genome

    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 – 150150Non-structural glycoprotein 4PRO_0000369890Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi5 – 51N-linked (GlcNAc...); by hostSequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919LumenalBy similarityAdd
    BLAST
    Topological domaini41 – 150110CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei20 – 4021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili60 – 9233Sequence AnalysisAdd
    BLAST

    Domaini

    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

    Sequencei

    Sequence statusi: Complete.

    Q82055-1 [UniParc]FASTAAdd to Basket

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    MDFINQTLFS KYTESNVDTI PYLLGLILAL TNGSRILRFI NSFIIICKHI    50
    VTTSKSAIDK MRKINNSEHN TKNAHEEYEE VMKQIREMRI HMTALFNSLH 100
    DDNVKWRMSE SIRREKKHEM KMSDNRNEFK HSHNDTNICE KSGLETEVCL 150
    Length:150
    Mass (Da):17,705
    Last modified:November 1, 1996 - v1
    Checksum:iA988D32675905515
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83967 Genomic RNA. Translation: CAA58801.1.
    RefSeqiYP_392515.1. NC_007573.1.

    Genome annotation databases

    GeneIDi3844400.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83967 Genomic RNA. Translation: CAA58801.1 .
    RefSeqi YP_392515.1. NC_007573.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3844400.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of the 11th RNA segment from human group C rotavirus."
      Deng Y., Fielding P.A., Lambden P.R., Caul E.O., Clarke I.N.
      Virus Genes 10:239-243(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiNSP4_ROTHC
    AccessioniPrimary (citable) accession number: Q82055
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3