Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q82029

- NSP4_ROTHS

UniProt

Q82029 - NSP4_ROTHS

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Non-structural glycoprotein 4

Gene
N/A
Organism
Rotavirus A (strain Human/Japan/S2/1980 G2-P1B[4]-I2-R2-C2-M2-Ax-Nx-T2-E2-Hx) (RV-A)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei111 – 1122CleavageSequence Analysis
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
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 Human/Japan/S2/1980 G2-P1B[4]-I2-R2-C2-M2-Ax-Nx-T2-E2-Hx) (RV-A)
Taxonomic identifieri10959 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]

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 cell endoplasmic reticulum Source: UniProtKB-KW
  2. host cell membrane Source: UniProtKB-KW
  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 – 175175Non-structural glycoprotein 4PRO_0000369483Add
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

ProteinModelPortaliQ82029.
SMRiQ82029. Positions 95-137.
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.

Q82029-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEKFTDLNYT LSVITLMNST LHTILEDPGM AYFPYIASVL TVLFTLHKAS
60 70 80 90 100
IPTMKIALKT SKCSYKVVKY CIVTILNTLL KLAGYKEQIT AKDEIEKQMD
110 120 130 140 150
RVVKEMRRQL EMIDKLTTRE IEQVELLKRI YDKLIVRSTG EIDMTKEINQ
160 170
KNVRTLEEWE SGKNPYEPKE VTAAM
Length:175
Mass (Da):20,303
Last modified:November 1, 1996 - v1
Checksum:i3C51EED704B1E693
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59104 mRNA. Translation: AAB81290.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59104 mRNA. Translation: AAB81290.1 .

3D structure databases

ProteinModelPortali Q82029.
SMRi Q82029. Positions 95-137.
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. "Genetic characterization of the rotavirus nonstructural protein, NSP4."
    Kirkwood C.D., Palombo E.A.
    Virology 236:258-265(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiNSP4_ROTHS
AccessioniPrimary (citable) accession number: Q82029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 46 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3