Q9LTB8 · CNBL9_ARATH
- ProteinCalcineurin B-like protein 9
- GeneCBL9
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids213 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a calcium sensor involved in abscisic acid (ABA) signaling and stress-induced ABA biosynthesis pathways. Contributes to the regulation of early stress-related CBF/DREB transcription factors. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. May function as a negative regulator of stress and ABA responses. Mediates the activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in response to low potassium conditions and in the context of stomatal movement. Involved in the calcium-dependent regulation by CIPK26 of reactive oxygen species production by the NADPH oxidase RBOHF. The CBL9/CIPK3 complex acts in the regulation of abscisic acid response in seed germination.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 117 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 119 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 121 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 128 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 140 | Involved in dimerization | ||||
Sequence: S | ||||||
Binding site | 161 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 163 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 165 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 167 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 172 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | plastid | |
Molecular Function | calcium ion binding | |
Molecular Function | kinase binding | |
Biological Process | abscisic acid-activated signaling pathway | |
Biological Process | calcium-mediated signaling | |
Biological Process | pollen tube growth | |
Biological Process | response to water deprivation |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCalcineurin B-like protein 9
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9LTB8
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
Note: Plasma membrane localization abolished by 2-bromopalmitate (2-BP) treatment.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Hypersensitivity to abscisic acid in the early developmental stages.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 201 | Loss of phosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 201 | Increased interaction with CIPK23. | ||||
Sequence: S → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000073510 | 2-213 | Calcineurin B-like protein 9 | |||
Sequence: GCFHSTAAREFPDHENPVKLASETAFSVSEVEALYELFKSISSSVVDDGLINKEEFQLALFKNRKKENLFANRIFDLFDVKRKGVIDFGDFVRSLNVFHPNASLEEKTDFTFRLYDMDCTGFIERQEVKQMLIALLCESEMKLADDTIEMILDQTFEDADVDRDGKIDKTEWSNFVIKNPSLLKIMTLPYLRDITTTFPSFVFNSEVDEIAT | ||||||
Modified residue | 201 | Phosphoserine; by CIPK23 | ||||
Sequence: S |
Post-translational modification
Both N-myristoylation and calcium-mediated conformational changes are essential for its function.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous. Colocalized with CIPK23 in root tips and vascular bundles in the stem and the leaf, as well as in guard cells and root hairs.
Induction
By drought, cold, salt and abscisic acid (ABA) treatments.
Gene expression databases
Interaction
Subunit
Homodimer (By similarity).
Part of a K+-channel calcium-sensing kinase/phosphatase complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a K+-channel (AKT1). Interacts with CIPK1, CIPK3, CIPK6, CIPK8, CIPK14, CIPK16, CIPK18, CIPK21, CIPK23, CIPK24 and CIPK26.
Part of a K+-channel calcium-sensing kinase/phosphatase complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a K+-channel (AKT1). Interacts with CIPK1, CIPK3, CIPK6, CIPK8, CIPK14, CIPK16, CIPK18, CIPK21, CIPK23, CIPK24 and CIPK26.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9LTB8 | CIPK1 Q8RWC9 | 5 | EBI-637381, EBI-1748677 | |
BINARY | Q9LTB8 | CIPK10 Q9C562 | 9 | EBI-637381, EBI-537572 | |
BINARY | Q9LTB8 | CIPK11 O22932 | 5 | EBI-637381, EBI-537638 | |
BINARY | Q9LTB8 | CIPK15 P92937 | 3 | EBI-637381, EBI-537592 | |
BINARY | Q9LTB8 | CIPK16 Q9SEZ7 | 7 | EBI-637381, EBI-1573415 | |
BINARY | Q9LTB8 | CIPK20 Q9FJ54 | 5 | EBI-637381, EBI-25514480 | |
BINARY | Q9LTB8 | CIPK23 Q93VD3 | 13 | EBI-637381, EBI-974277 | |
BINARY | Q9LTB8 | CIPK24 Q9LDI3 | 8 | EBI-637381, EBI-537551 | |
BINARY | Q9LTB8 | CIPK3 Q2V452 | 5 | EBI-637381, EBI-1748724 | |
BINARY | Q9LTB8 | CIPK5 Q9LEU7 | 6 | EBI-637381, EBI-2026322 | |
BINARY | Q9LTB8 | CIPK8 Q9STV4 | 8 | EBI-637381, EBI-2026454 | |
BINARY | Q9LTB8 | CIPK9 Q9MAM1 | 4 | EBI-637381, EBI-1765282 | |
BINARY | Q9LTB8 | IBR5 Q84JU4 | 4 | EBI-637381, EBI-604555 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-66 | EF-hand 1 | ||||
Sequence: EVEALYELFKSISSSVVDDGLINKEEFQLALFKNRK | ||||||
Domain | 67-102 | EF-hand 2 | ||||
Sequence: KENLFANRIFDLFDVKRKGVIDFGDFVRSLNVFHPN | ||||||
Domain | 104-139 | EF-hand 3 | ||||
Sequence: SLEEKTDFTFRLYDMDCTGFIERQEVKQMLIALLCE | ||||||
Domain | 148-183 | EF-hand 4 | ||||
Sequence: TIEMILDQTFEDADVDRDGKIDKTEWSNFVIKNPSL |
Domain
The N-terminal 12 amino acids are sufficient for cell membrane targeting.
Sequence similarities
Belongs to the calcineurin regulatory subunit family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length213
- Mass (Da)24,532
- Last updated2007-01-23 v3
- ChecksumE848102CD14211EE
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8BBZ1 | A0A1P8BBZ1_ARATH | CBL9 | 173 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF411958 EMBL· GenBank· DDBJ | AAL10301.1 EMBL· GenBank· DDBJ | mRNA | ||
AB025609 EMBL· GenBank· DDBJ | BAA98105.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED95471.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB060590 EMBL· GenBank· DDBJ | BAB69895.1 EMBL· GenBank· DDBJ | mRNA | ||
BT002995 EMBL· GenBank· DDBJ | AAO22803.1 EMBL· GenBank· DDBJ | mRNA | ||
BT004458 EMBL· GenBank· DDBJ | AAO42452.1 EMBL· GenBank· DDBJ | mRNA |