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Protein

Non-structural glycoprotein 4

Gene
N/A
Organism
Rotavirus A (strain RVA/Human/Japan/KU/1995/G1P1A[8]) (RV-A)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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)DescriptionActionsGraphical viewLength
Metal bindingi120Calcium; shared with all tetrameric partners; partialBy similarity1
Metal bindingi123Calcium; shared with all tetrameric partnersBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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 (strain RVA/Human/Japan/KU/1995/G1P1A[8]) (RV-A)
Taxonomic identifieri10952 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000001458 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 – 28LumenalBy similarityAdd BLAST28
Transmembranei29 – 51HelicalSequence analysisAdd BLAST23
Topological domaini52 – 175CytoplasmicBy similarityAdd BLAST124

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_00003694801 – 175Non-structural glycoprotein 4Add BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi8N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi18N-linked (GlcNAc...); by hostSequence analysis1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei111 – 112CleavageSequence analysis2

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

ProteinModelPortaliQ9QNA6.
SMRiQ9QNA6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 21HydrophobicBy similarityAdd BLAST15
Regioni67 – 85HydrophobicBy similarityAdd BLAST19
Regioni85 – 123Endoplasmic reticulum retention signalSequence analysisAdd BLAST39
Regioni114 – 135Interaction with CAV1By similarityAdd BLAST22
Regioni122 – 175Required for interaction with microtubulesBy similarityAdd BLAST54
Regioni159 – 175ICP binding domainBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili85 – 117Sequence analysisAdd BLAST33

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.

Q9QNA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKLADLNYT LSVITLMNDT LHSIIQDPGM AYFTYIASVL TVLFTLHKAS
60 70 80 90 100
IPTMKIALKT SKCSYKVIKY CIVTIINTLL RLAGYKEQVT TKDEIEQQMD
110 120 130 140 150
RIVKEMRRQL EMIDKLTTRE IEQVELLKSI HDNLITRSVD VIDMSKEFNQ
160 170
KNIKTLDEWE SGRNPYEPSE VTASM
Length:175
Mass (Da):20,228
Last modified:May 1, 2000 - v1
Checksum:iE54EE497BA9FFF6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022772 mRNA. Translation: BAA84969.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022772 mRNA. Translation: BAA84969.1.

3D structure databases

ProteinModelPortaliQ9QNA6.
SMRiQ9QNA6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

Entry informationi

Entry nameiNSP4_ROTHK
AccessioniPrimary (citable) accession number: Q9QNA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 44 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

Caution

A candidate enterotoxigenic cleaved form of the protein has been suggested, but it remains unclear whether this truncated form constitutes an active enterotoxin in vivo.Curated

Keywords - Technical termi

Complete 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.