Q5ICL9 · NPR4_ARATH
- ProteinRegulatory protein NPR4
- GeneNPR4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids574 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | salicylic acid binding | |
Biological Process | defense response to bacterium | |
Biological Process | defense response to fungus | |
Biological Process | plant-type hypersensitive response | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of jasmonic acid mediated signaling pathway | |
Biological Process | regulation of salicylic acid mediated signaling pathway | |
Biological Process | regulation of systemic acquired resistance | |
Biological Process | response to bacterium | |
Biological Process | response to fungus | |
Biological Process | response to salicylic acid | |
Biological Process | systemic acquired resistance | |
Biological Process | systemic acquired resistance, salicylic acid mediated signaling pathway |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRegulatory protein NPR4
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ5ICL9
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 321 | Abolishes interaction with TGA2 or with TGA7. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 392 | Normal salicylic acid (SA) binding. | ||||
Sequence: P → Q | ||||||
Mutagenesis | 419 | Impaired salicylic acid (SA) binding. | ||||
Sequence: R → K or A | ||||||
Mutagenesis | 419 | Impaired salicylic acid (SA) binding. Interacts with NPR1 in the absence of SA, and lost ability of SA to repress this interaction. | ||||
Sequence: R → Q | ||||||
Mutagenesis | 420 | Impaired salicylic acid (SA) binding. | ||||
Sequence: V → A | ||||||
Mutagenesis | 423 | Impaired salicylic acid (SA) binding. | ||||
Sequence: A → F or E | ||||||
Mutagenesis | 426 | Strongly 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. | ||||
Sequence: F → L | ||||||
Mutagenesis | 431 | Impaired salicylic acid (SA) binding. | ||||
Sequence: A → L or R | ||||||
Mutagenesis | 434 | Impaired salicylic acid (SA) binding. | ||||
Sequence: A → R | ||||||
Mutagenesis | 434 | Reduced salicylic acid (SA) binding. | ||||
Sequence: A → V | ||||||
Mutagenesis | 459 | Slightly increased salicylic acid (SA) binding. | ||||
Sequence: T → A | ||||||
Mutagenesis | 459 | Slightly 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. | ||||
Sequence: T → G | ||||||
Mutagenesis | 469 | Normal salicylic acid (SA) binding. | ||||
Sequence: E → I | ||||||
Mutagenesis | 470 | Slightly increased salicylic acid (SA) binding. | ||||
Sequence: T → A | ||||||
Mutagenesis | 488 | Reduced salicylic acid (SA) binding. | ||||
Sequence: T → A | ||||||
Mutagenesis | 488 | Normal salicylic acid (SA) binding. Interacts with NPR1 in the absence of SA, but this interaction is repressed by SA. | ||||
Sequence: T → V | ||||||
Mutagenesis | 489 | Impaired salicylic acid (SA) binding. Interacts with NPR1 in the absence of SA, and lost ability of SA to repress this interaction. | ||||
Sequence: V → A | ||||||
Mutagenesis | 496 | Reduced salicylic acid (SA) binding. | ||||
Sequence: F → A | ||||||
Mutagenesis | 500 | Normal salicylic acid (SA) binding. | ||||
Sequence: Y → S | ||||||
Mutagenesis | 503 | Impaired salicylic acid (SA) binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 505 | Slightly increased salicylic acid (SA) binding. | ||||
Sequence: K → A | ||||||
Mutagenesis | 505 | Slightly reduced salicylic acid (SA) binding. | ||||
Sequence: K → Q |
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.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000407993 | 1-574 | Regulatory protein NPR4 | |||
Sequence: MAATAIEPSSSISFTSSHLSNPSPVVTTYHSAANLEELSSNLEQLLTNPDCDYTDAEIIIEEEANPVSVHRCVLAARSKFFLDLFKKDKDSSEKKPKYQMKDLLPYGNVGREAFLHFLSYIYTGRLKPFPIEVSTCVDSVCAHDSCKPAIDFAVELMYASFVFQIPDLVSSFQRKLRNYVEKSLVENVLPILLVAFHCDLTQLLDQCIERVARSDLDRFCIEKELPLEVLEKIKQLRVKSVNIPEVEDKSIERTGKVLKALDSDDVELVKLLLTESDITLDQANGLHYAVAYSDPKVVTQVLDLDMADVNFRNSRGYTVLHIAAMRREPTIIIPLIQKGANASDFTFDGRSAVNICRRLTRPKDYHTKTSRKEPSKYRLCIDILEREIRRNPLVSGDTPTCSHSMPEDLQMRLLYLEKRVGLAQLFFPAEANVAMDVANVEGTSECTGLLTPPPSNDTTENLGKVDLNETPYVQTKRMLTRMKALMKTVETGRRYFPSCYEVLDKYMDQYMDEEIPDMSYPEKGTVKERRQKRMRYNELKNDVKKAYSKDKVARSCLSSSSPASSLREALENPT | ||||||
Modified residue | 11 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5ICL9 | At1g05410 Q8VZE5 | 3 | EBI-1392093, EBI-4425726 | |
BINARY | Q5ICL9 | At1g12810 F4IDX2 | 3 | EBI-1392093, EBI-25529516 | |
BINARY | Q5ICL9 | CHC2 Q0WLB5 | 3 | EBI-1392093, EBI-4412194 | |
BINARY | Q5ICL9 | COG2 F4JRR1 | 3 | EBI-1392093, EBI-4429018 | |
BINARY | Q5ICL9 | LSU1 Q9SCK1 | 3 | EBI-1392093, EBI-4424157 | |
BINARY | Q5ICL9 | LSU2 Q9FIR9 | 3 | EBI-1392093, EBI-4424076 | |
BINARY | Q5ICL9 | MTX1 O64471 | 3 | EBI-1392093, EBI-2123898 | |
BINARY | Q5ICL9 | NHL3 Q9FNH6 | 3 | EBI-1392093, EBI-4461284 | |
BINARY | Q5ICL9 | NPR1 P93002 | 3 | EBI-1392093, EBI-1392127 | |
BINARY | Q5ICL9 | NPR3 Q8L746 | 5 | EBI-1392093, EBI-4441365 | |
BINARY | Q5ICL9 | NPR4 Q5ICL9 | 2 | EBI-1392093, EBI-1392093 | |
BINARY | Q5ICL9 | SIED1 Q9FMS4 | 3 | EBI-1392093, EBI-25529548 | |
BINARY | Q5ICL9 | TSB2 P25269 | 3 | EBI-1392093, EBI-25529585 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, zinc finger, repeat, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MAATAIEPSSSISFTSSHLSN | ||||||
Domain | 54-130 | BTB | ||||
Sequence: TDAEIIIEEEANPVSVHRCVLAARSKFFLDLFKKDKDSSEKKPKYQMKDLLPYGNVGREAFLHFLSYIYTGRLKPFP | ||||||
Zinc finger | 131-147 | C2HC-type | ||||
Sequence: IEVSTCVDSVCAHDSCK | ||||||
Repeat | 252-280 | ANK 1 | ||||
Sequence: ERTGKVLKALDSDDVELVKLLLTESDITL | ||||||
Repeat | 281-311 | ANK 2 | ||||
Sequence: DQANGLHYAVAYSDPKVVTQVLDLDMADVNF | ||||||
Repeat | 315-344 | ANK 3 | ||||
Sequence: RGYTVLHIAAMRREPTIIIPLIQKGANASD | ||||||
Region | 373-516 | Salicylic acid-binding core (SBC) | ||||
Sequence: EPSKYRLCIDILEREIRRNPLVSGDTPTCSHSMPEDLQMRLLYLEKRVGLAQLFFPAEANVAMDVANVEGTSECTGLLTPPPSNDTTENLGKVDLNETPYVQTKRMLTRMKALMKTVETGRRYFPSCYEVLDKYMDQYMDEEIP | ||||||
Compositional bias | 521-551 | Basic and acidic residues | ||||
Sequence: PEKGTVKERRQKRMRYNELKNDVKKAYSKDK | ||||||
Region | 521-574 | Disordered | ||||
Sequence: PEKGTVKERRQKRMRYNELKNDVKKAYSKDKVARSCLSSSSPASSLREALENPT | ||||||
Compositional bias | 553-574 | Polar residues | ||||
Sequence: ARSCLSSSSPASSLREALENPT |
Domain
The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.
Sequence similarities
Belongs to the plant 'ANKYRIN-BTB/POZ' family. 'NPR1-like' subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length574
- Mass (Da)65,115
- Last updated2005-02-15 v1
- Checksum11DCA45A220A7F46
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8B3C8 | A0A1P8B3C8_ARATH | NPR4 | 601 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 521-551 | Basic and acidic residues | ||||
Sequence: PEKGTVKERRQKRMRYNELKNDVKKAYSKDK | ||||||
Compositional bias | 553-574 | Polar residues | ||||
Sequence: ARSCLSSSSPASSLREALENPT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |