| Tag |
Content |
LipidDB ID |
LipidDB-3702-01272 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
4.84 |
Molecular Weight |
23518.03 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Calcineurin B-like protein 5 |
Protein Synonyms/Alias |
SOS3-like calcium-binding protein 4; |
Gene Name |
CBL5 |
Gene Synonyms/Alias |
SCABP4; At4g01420; F3D13.2; |
Created Date |
21-DEC-2004 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGCVCSKQL | [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. 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 positive regulator of salt or drought responses. |
Sequence Annotation |
Domain: 30 65 EF-hand 1. Domain: 66 101 EF-hand 2. Domain: 103 138 EF-hand 3. Domain: 147 182 EF-hand 4. Functional site: 139 139 Involved in dimerization.
|
Protein Length |
203 AA. |
Protein Sequence (Canonical) |
MGCVCSKQLE GRRQEDISLL ASQTFFSEAE VEVLHGLFIK LTSCLSNDNL LTKEKFQFIL 60
IKNTKKRSLS AERIFGLFDM RNDGAIDFGE FVHTLNIFHP NSSPRDKAIF AFRLYDTRET 120
GFIEPEEVKE MIIDVLEESE LMLSESIIDS IVSKTFEEAD WKKDGIIDLE EWENFVATYP 180
LTLKNMTIPF LKDIPRIFPT FLR 203
|
FASTA (Canonical) |
>LipidDB-3702-01272|Q7FZF1
MGCVCSKQLEGRRQEDISLLASQTFFSEAEVEVLHGLFIKLTSCLSNDNLLTKEKFQFIL
IKNTKKRSLSAERIFGLFDMRNDGAIDFGEFVHTLNIFHPNSSPRDKAIFAFRLYDTRET
GFIEPEEVKEMIIDVLEESELMLSESIIDSIVSKTFEEADWKKDGIIDLEEWENFVATYP
LTLKNMTIPFLKDIPRIFPTFLR
|
Gene Ontology |
|
Interpro |
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Pfam |
|
SMART |
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PROSITE |
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PRINTS |
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