| Tag |
Content |
LipidDB ID |
LipidDB-3702-00886 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
4.74 |
Molecular Weight |
24553.98 |
Genbank Protein ID |
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Genbank Nucleotide ID |
|
Protein Name |
Calcineurin B-like protein 1 |
Protein Synonyms/Alias |
SOS3-like calcium-binding protein 5; |
Gene Name |
CBL1 |
Gene Synonyms/Alias |
SCABP5; At4g17615; dl4845w; FCAALL.122; |
Created Date |
21-DEC-2004 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGCFHSKAA | [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 the signaling pathway during growth and development and in response to abiotic stresses. May function as a positive regulator of salt and drought responses and as a negative regulator of cold response. 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. 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 response to glucose and gibberellin during germination and seedling development and in response to cold stress. Involved in the calcium-dependent regulation by CIPK26 of reactive oxygen species production by the NADPH oxidase RBOHF. |
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) |
MGCFHSKAAK EFRGHEDPVK LASETAFSVS EVEALFELFK SISSSVVDDG LINKEEFQLA 60
LFKSRKRENI FANRIFDMFD VKRKGVIDFG DFVRSLNVFH PNASLEDKID FTFRLYDMDC 120
TGYIERQEVK QMLIALLCES EMKLADETIE IILDKTFEDA DVNQDGKIDK LEWSDFVNKN 180
PSLLKIMTLP YLRDITTTFP SFVFHSEVDE IAT 213
|
FASTA (Canonical) |
>LipidDB-3702-00886|O81445
MGCFHSKAAKEFRGHEDPVKLASETAFSVSEVEALFELFKSISSSVVDDGLINKEEFQLA
LFKSRKRENIFANRIFDMFDVKRKGVIDFGDFVRSLNVFHPNASLEDKIDFTFRLYDMDC
TGYIERQEVKQMLIALLCESEMKLADETIEIILDKTFEDADVNQDGKIDKLEWSDFVNKN
PSLLKIMTLPYLRDITTTFPSFVFHSEVDEIAT
|
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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