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Protein

Non-structural glycoprotein 4

Gene
N/A
Organism
Rotavirus C (isolate RVC/Human/United Kingdom/Bristol/1989) (RV-C)
Status
Reviewed-Annotation score: 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).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

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 RVC/Human/United Kingdom/Bristol/1989) (RV-C)
Taxonomic identifieri31567 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007664 Componenti: Genome

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 19LumenalBy similarityAdd BLAST19
Transmembranei20 – 40HelicalSequence analysisAdd BLAST21
Topological domaini41 – 150CytoplasmicBy similarityAdd BLAST110

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host endoplasmic reticulum, Host membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003698901 – 150Non-structural glycoprotein 4Add BLAST150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi5N-linked (GlcNAc...); by hostSequence analysis1

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili60 – 92Sequence analysisAdd BLAST33

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

« Hide

        10         20         30         40         50
MDFINQTLFS KYTESNVDTI PYLLGLILAL TNGSRILRFI NSFIIICKHI
60 70 80 90 100
VTTSKSAIDK MRKINNSEHN TKNAHEEYEE VMKQIREMRI HMTALFNSLH
110 120 130 140 150
DDNVKWRMSE SIRREKKHEM KMSDNRNEFK HSHNDTNICE KSGLETEVCL
Length:150
Mass (Da):17,705
Last modified:November 1, 1996 - v1
Checksum:iA988D32675905515
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83967 Genomic RNA. Translation: CAA58801.1.
RefSeqiYP_392515.1. NC_007573.1.

Genome annotation databases

GeneIDi3844400.
KEGGivg:3844400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83967 Genomic RNA. Translation: CAA58801.1.
RefSeqiYP_392515.1. NC_007573.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3844400.
KEGGivg:3844400.

Family and domain databases

ProtoNetiSearch...

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: November 30, 2016
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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.