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Q82055

- NSP4_ROTHC

UniProt

Q82055 - NSP4_ROTHC

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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

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.
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.

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

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; 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919Lumenal By similarity
Add
BLAST
Transmembranei20 – 4021Helical; Reviewed prediction
Add
BLAST
Topological domaini41 – 150110Cytoplasmic By similarity
Add
BLAST

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
Complete GO annotation...

Keywords - Cellular componenti

Host endoplasmic reticulum, Host membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 150150Non-structural glycoprotein 4
PRO_0000369890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi5 – 51N-linked (GlcNAc...); by host Reviewed prediction

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili60 – 9233 Reviewed prediction
Add
BLAST

Domaini

The coiled coil region mediates oligomerization By similarity.

Sequence similaritiesi

Belongs to the rotavirus NSP4 family.

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: February 19, 2014
This is version 37 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

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