Q5ICL9 · NPR4_ARATH

Function

function

Salicylic acid (SA)-binding substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of NPR1 in the absence of SA (PubMed:22699612, PubMed:32788727).
Together with NPR3, acts as receptor of salicylic acid to monitor immunity in a NPR1-dependent manner and induce systemic acquired resistance (SAR) (PubMed:22699612, PubMed:32788727).
Involved in the regulation of basal defense responses against pathogens, and may be implicated in the cross-talk between the SA- and JA-dependent signaling pathways (PubMed:15634206, PubMed:17076807, PubMed:32788727).

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site.

157450100150200250300350400450500550
TypeIDPosition(s)Description
Binding site136Zn2+ (UniProtKB | ChEBI)
Binding site141Zn2+ (UniProtKB | ChEBI)
Binding site143Zn2+ (UniProtKB | ChEBI)
Binding site146Zn2+ (UniProtKB | ChEBI)
Binding site419salicylate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionsalicylic acid binding
Biological Processdefense response to bacterium
Biological Processdefense response to fungus
Biological Processplant-type hypersensitive response
Biological Processprotein ubiquitination
Biological Processregulation of jasmonic acid mediated signaling pathway
Biological Processregulation of salicylic acid mediated signaling pathway
Biological Processregulation of systemic acquired resistance
Biological Processresponse to bacterium
Biological Processresponse to fungus
Biological Processresponse to salicylic acid
Biological Processsystemic acquired resistance
Biological Processsystemic acquired resistance, salicylic acid mediated signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Regulatory protein NPR4
  • Alternative names
    • BTB/POZ domain-containing protein NPR4

Gene names

    • Name
      NPR4
    • ORF names
      T16H5.20
    • Ordered locus names
      At4g19660

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q5ICL9
  • Secondary accessions
    • O81848

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Enhanced susceptibility to the virulent bacterial pathogen Pseudomonas syringe and to the fungal pathogen Erysiphe cichoracearum (powdery mildew) (PubMed:15634206).
The double mutant npr3 npr4 accumulates NPR1 proteins (while NPR1 transcripts level is normal) due to reduced NPR1 degradation by the proteasome; this leads to a reduced growth of the compatible pathogenic bacteria Pseudomonas syringae pv. maculicola ES4326 after inoculation, but impaired hypersensitive response (HR) and subsequent systemic acquired resistance (SAR) induction when infected by the avirulent strain Psm ES4326/avrRpt2 (PubMed:22699612, PubMed:32788727).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis321Abolishes interaction with TGA2 or with TGA7.
Mutagenesis392Normal salicylic acid (SA) binding.
Mutagenesis419Impaired salicylic acid (SA) binding.
Mutagenesis419Impaired salicylic acid (SA) binding. Interacts with NPR1 in the absence of SA, and lost ability of SA to repress this interaction.
Mutagenesis420Impaired salicylic acid (SA) binding.
Mutagenesis423Impaired salicylic acid (SA) binding.
Mutagenesis426Strongly reduced salicylic acid (SA) binding. Interacts with NPR1 in the absence of SA, and lost ability of SA to repress this interaction, thus leading to faster NPR1 degradation but reduced PR1 induction. Strongly increased salicylic acid (SA) binding leading to restored ability of SA to repress NPR1 binding and delayed NPR1 degradation resulting in increased levels of SA-induced PR1 gene expression; when associated with G-459.
Mutagenesis431Impaired salicylic acid (SA) binding.
Mutagenesis434Impaired salicylic acid (SA) binding.
Mutagenesis434Reduced salicylic acid (SA) binding.
Mutagenesis459Slightly increased salicylic acid (SA) binding.
Mutagenesis459Slightly increased salicylic acid (SA) binding. Strongly increased salicylic acid (SA) binding leading to restored ability of SA to repress NPR1 binding and delayed NPR1 degradation resulting in increased levels of SA-induced PR1 gene expression; when associated with L-426.
Mutagenesis469Normal salicylic acid (SA) binding.
Mutagenesis470Slightly increased salicylic acid (SA) binding.
Mutagenesis488Reduced salicylic acid (SA) binding.
Mutagenesis488Normal salicylic acid (SA) binding. Interacts with NPR1 in the absence of SA, but this interaction is repressed by SA.
Mutagenesis489Impaired salicylic acid (SA) binding. Interacts with NPR1 in the absence of SA, and lost ability of SA to repress this interaction.
Mutagenesis496Reduced salicylic acid (SA) binding.
Mutagenesis500Normal salicylic acid (SA) binding.
Mutagenesis503Impaired salicylic acid (SA) binding.
Mutagenesis505Slightly increased salicylic acid (SA) binding.
Mutagenesis505Slightly reduced salicylic acid (SA) binding.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 51 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004079931-574Regulatory protein NPR4
Modified residue11Phosphoserine

Keywords

Proteomic databases

Expression

Induction

Up-regulated following pathogen challenge or salicylic acid (SA) treatment, and down-regulated by methyl jasmonic acid (MeJA) treatment.

Gene expression databases

Interaction

Subunit

Forms homodimers, homotetramers and heterodimers with NPR3 in the presence of salicylic acid (SA) (PubMed:22699612).
Interacts with TGA2, TGA3, TGA5, TGA6 and TGA7 (PubMed:15634206, PubMed:17076807).
Interacts with CUL3A, a core component of the cullin-RING ubiquitin ligases (CRL) (PubMed:22699612).
Binds to NPR1; this interaction is disrupted by association with SA, probably due to conformational changes (PubMed:22699612, PubMed:26269953, PubMed:32788727).

Binary interactions

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, zinc finger, repeat, compositional bias.

TypeIDPosition(s)Description
Region1-21Disordered
Domain54-130BTB
Zinc finger131-147C2HC-type
Repeat252-280ANK 1
Repeat281-311ANK 2
Repeat315-344ANK 3
Region373-516Salicylic acid-binding core (SBC)
Compositional bias521-551Basic and acidic residues
Region521-574Disordered
Compositional bias553-574Polar residues

Domain

The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    574
  • Mass (Da)
    65,115
  • Last updated
    2005-02-15 v1
  • Checksum
    11DCA45A220A7F46
MAATAIEPSSSISFTSSHLSNPSPVVTTYHSAANLEELSSNLEQLLTNPDCDYTDAEIIIEEEANPVSVHRCVLAARSKFFLDLFKKDKDSSEKKPKYQMKDLLPYGNVGREAFLHFLSYIYTGRLKPFPIEVSTCVDSVCAHDSCKPAIDFAVELMYASFVFQIPDLVSSFQRKLRNYVEKSLVENVLPILLVAFHCDLTQLLDQCIERVARSDLDRFCIEKELPLEVLEKIKQLRVKSVNIPEVEDKSIERTGKVLKALDSDDVELVKLLLTESDITLDQANGLHYAVAYSDPKVVTQVLDLDMADVNFRNSRGYTVLHIAAMRREPTIIIPLIQKGANASDFTFDGRSAVNICRRLTRPKDYHTKTSRKEPSKYRLCIDILEREIRRNPLVSGDTPTCSHSMPEDLQMRLLYLEKRVGLAQLFFPAEANVAMDVANVEGTSECTGLLTPPPSNDTTENLGKVDLNETPYVQTKRMLTRMKALMKTVETGRRYFPSCYEVLDKYMDQYMDEEIPDMSYPEKGTVKERRQKRMRYNELKNDVKKAYSKDKVARSCLSSSSPASSLREALENPT

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8B3C8A0A1P8B3C8_ARATHNPR4601

Sequence caution

The sequence CAA19683.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB78968.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias521-551Basic and acidic residues
Compositional bias553-574Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY785951
EMBL· GenBank· DDBJ
AAW31628.1
EMBL· GenBank· DDBJ
mRNA
AL024486
EMBL· GenBank· DDBJ
CAA19683.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AL161551
EMBL· GenBank· DDBJ
CAB78968.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002687
EMBL· GenBank· DDBJ
AEE84211.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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