Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00833
Entry Name
UniProt Accession
Theoretical PI
5.13
Molecular Weight
25693.48
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calcineurin B-like protein 4
Protein Synonyms/Alias
Protein SALT OVERLY SENSITIVE 3;
Gene Name
CBL4
Gene Synonyms/Alias
SOS3; At5g24270; MOP9.8;
Created Date
21-DEC-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGCSVSKKK
[1][2]
N-Myristoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Ishitani M, Liu J, Halfter U, Kim CS, Shi W, Zhu JK. SOS3 function in plantsalt tolerance requires N-myristoylation and calcium binding. Plant Cell. 2000Sep;12(9):1667-78.[PMID:11006339]
[2] 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 regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Binding of a CBL protein to the regulatory NAF domain of a CIPK serine-threonine protein kinase lead to the activation of the kinase in a calcium-dependent manner. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. Involved in salt stress responses by mediating calcium-dependent microfilament reorganization. The CBL4/CIPK6 complex mediates translocation of AKT2 from the endoplasmic reticulum to the plasma membrane. Both myristoylation and S-acylation are required for AKT2 activation.
Sequence Annotation
Domain: 35 70 EF-hand 1.
Domain: 71 106 EF-hand 2.
Domain: 108 143 EF-hand 3.
Domain: 152 187 EF-hand 4.
Functional site: 144 144 Involved in dimerization.
Modified residue: 205 205 Phosphoserine.
Protein Length
222 AA.
Protein Sequence
(Canonical)
MGCSVSKKKK KNAMRPPGYE DPELLASVTP FTVEEVEALY ELFKKLSSSI IDDGLIHKEE  60
FQLALFRNRN RRNLFADRIF DVFDVKRNGV IEFGEFVRSL GVFHPSAPVH EKVKFAFKLY  120
DLRQTGFIER EELKEMVVAL LHESELVLSE DMIEVMVDKA FVQADRKNDG KIDIDEWKDF  180
VSLNPSLIKN MTLPYLKDIN RTFPSFVSSC EEEEMELQNV SS                     222
FASTA
(Canonical)
>LipidDB-3702-00833|O81223
MGCSVSKKKKKNAMRPPGYEDPELLASVTPFTVEEVEALYELFKKLSSSIIDDGLIHKEE
FQLALFRNRNRRNLFADRIFDVFDVKRNGVIEFGEFVRSLGVFHPSAPVHEKVKFAFKLY
DLRQTGFIEREELKEMVVALLHESELVLSEDMIEVMVDKAFVQADRKNDGKIDIDEWKDF
VSLNPSLIKNMTLPYLKDINRTFPSFVSSCEEEEMELQNVSS
Gene Ontology
GO:0005955; C:calcineurin complex; ISS:TAIR
GO:0005737; C:cytoplasm; IDA:TAIR
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0005509; F:calcium ion binding; ISS:TAIR
GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; ISS:TAIR
GO:0030007; P:cellular potassium ion homeostasis; IMP:TAIR
GO:0016311; P:dephosphorylation; ISS:GOC
GO:0005513; P:detection of calcium ion; IMP:TAIR
GO:0042539; P:hypotonic salinity response; IMP:TAIR
Interpro
InterPro; IPR015757; Calcineur_B
InterPro; IPR011992; EF-hand-dom_pair
InterPro; IPR002048; EF_hand_dom
Pfam
Pfam; PF13499; EF-hand_7;
SMART
SMART; SM00054; EFh;
PROSITE
PROSITE; PS50222; EF_HAND_2;
PRINTS