| Tag |
Content |
LipidDB ID |
LipidDB-3702-00803 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
4.89 |
Molecular Weight |
25809.38 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Calcineurin B-like protein 2 |
Protein Synonyms/Alias |
SOS3-like calcium-binding protein 1; |
Gene Name |
CBL2 |
Gene Synonyms/Alias |
SCABP1; At5g55990; MDA7.3; |
Created Date |
21-DEC-2004 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
4 | Canonical | ****MSQCVDGIKHL | [1] | S-Palmitoylation | 12 | Canonical | VDGIKHLCTSVLGCF | [1] | S-Palmitoylation | 18 | Canonical | LCTSVLGCFDLDLYK | [1] | S-Palmitoylation |
|
Organism |
Arabidopsis thaliana (Mouse-ear cress) |
NCBI Taxa ID |
3702 |
Reference |
[1] Batistič O, Rehers M, Akerman A, Schlücking K, Steinhorst L, Yalovsky S, KudlaJ. S-acylation-dependent association of the calcium sensor CBL2 with the vacuolarmembrane is essential for proper abscisic acid responses. Cell Res. 2012Jul;22(7):1155-68. doi: 10.1038/cr.2012.71. Epub 2012 May 1.[ PMID:22547024]
|
Functional Description |
Acts as a calcium sensor. 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. Binds four calcium ions per subunit. 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. Mediates the inactivation of the proton pump AHA2 by CIPK11. Probably involved in regulating signaling responses to abscisic acid. |
Sequence Annotation |
Domain: 36 81 EF-hand 1. Domain: 82 117 EF-hand 2. Domain: 119 154 EF-hand 3. Domain: 163 198 EF-hand 4. Functional site: 155 155 Involved in dimerization. Modified residue: 216 216 Phosphoserine; by CIPK11 and CIPK14.
|
Protein Length |
226 AA. |
Protein Sequence (Canonical) |
MSQCVDGIKH LCTSVLGCFD LDLYKQSGGL GDPELLARDT VFSVSEIEAL YELFKKISSA 60
VIDDGLINKE EFQLALFKTN KKESLFADRV FDLFDTKHNG ILGFEEFARA LSVFHPNAPI 120
DDKIHFSFQL YDLKQQGFIE RQEVKQMVVA TLAESGMNLK DTVIEDIIDK TFEEADTKHD 180
GKIDKEEWRS LVLRHPSLLK NMTLQYLKDI TTTFPSFVFH SQVEDT 226
|
FASTA (Canonical) |
>LipidDB-3702-00803|Q8LAS7
MSQCVDGIKHLCTSVLGCFDLDLYKQSGGLGDPELLARDTVFSVSEIEALYELFKKISSA
VIDDGLINKEEFQLALFKTNKKESLFADRVFDLFDTKHNGILGFEEFARALSVFHPNAPI
DDKIHFSFQLYDLKQQGFIERQEVKQMVVATLAESGMNLKDTVIEDIIDKTFEEADTKHD
GKIDKEEWRSLVLRHPSLLKNMTLQYLKDITTTFPSFVFHSQVEDT
|
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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