| Tag |
Content |
LipidDB ID |
LipidDB-3702-00134 |
Entry Name |
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UniProt Accession |
|
Theoretical PI |
4.58 |
Molecular Weight |
24531.84 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Calcineurin B-like protein 9 |
Protein Synonyms/Alias |
|
Gene Name |
CBL9 |
Gene Synonyms/Alias |
At5g47100; K14A3.5; |
Created Date |
21-DEC-2004 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGCFHSTAA | [1] | N-Myristoylation |
|
Organism |
Arabidopsis thaliana (Mouse-ear cress) |
NCBI Taxa ID |
3702 |
Reference |
[1] Batistic O, Sorek N, Schültke S, Yalovsky S, Kudla J. Dual fatty acylmodification determines the localization and plasma membrane targeting ofCBL/CIPK Ca2+ signaling complexes in Arabidopsis. Plant Cell. 2008May;20(5):1346-62. doi: 10.1105/tpc.108.058123. Epub 2008 May 23.[ PMID:18502848]
|
Functional Description |
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. |
Sequence Annotation |
Domain: 31 66 EF-hand 1. Domain: 67 102 EF-hand 2. Domain: 104 139 EF-hand 3. Domain: 148 183 EF-hand 4. Functional site: 140 140 Involved in dimerization. Modified residue: 201 201 Phosphoserine; by CIPK23.
|
Protein Length |
213 AA. |
Protein Sequence (Canonical) |
MGCFHSTAAR EFPDHENPVK LASETAFSVS EVEALYELFK SISSSVVDDG LINKEEFQLA 60
LFKNRKKENL FANRIFDLFD VKRKGVIDFG DFVRSLNVFH PNASLEEKTD FTFRLYDMDC 120
TGFIERQEVK QMLIALLCES EMKLADDTIE MILDQTFEDA DVDRDGKIDK TEWSNFVIKN 180
PSLLKIMTLP YLRDITTTFP SFVFNSEVDE IAT 213
|
FASTA (Canonical) |
>LipidDB-3702-00134|Q9LTB8
MGCFHSTAAREFPDHENPVKLASETAFSVSEVEALYELFKSISSSVVDDGLINKEEFQLA
LFKNRKKENLFANRIFDLFDVKRKGVIDFGDFVRSLNVFHPNASLEEKTDFTFRLYDMDC
TGFIERQEVKQMLIALLCESEMKLADDTIEMILDQTFEDADVDRDGKIDKTEWSNFVIKN
PSLLKIMTLPYLRDITTTFPSFVFNSEVDEIAT
|
Gene Ontology |
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Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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