Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O81223 (CNBL4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcineurin B-like protein 4
Alternative name(s):
Protein SALT OVERLY SENSITIVE 3
Gene names
Name:CBL4
Synonyms:SOS3
Ordered Locus Names:At5g24270
ORF Names:MOP9.8
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.12 Ref.14

Cofactor

Binds 4 calcium ions per subunit.

Subunit structure

Interacts with CIPK24/SOS2, CIPK6/SIP3, CIPK10/SIP1, CIPK11/SIP4 and CIPK15/SIP2. Homodimer, mediated by calcium-binding. Ref.2 Ref.7 Ref.12 Ref.13 Ref.15 Ref.16

Subcellular location

Cell membrane; Lipid-anchor. Cytoplasm. Nucleus. Note: The cell membrane localization is S-acylation dependent. Ref.11

Domain

The calcium-binding domain (165-176) of the EF-hand 4 can also interacts with a manganese ion. The N-terminal 18 amino acids are sufficient for the cell membrane targeting of an heterologous protein. Ref.11

Post-translational modification

Both N-myristoylation and calcium-mediated conformational changes are essential for its function. S-acylated at Cys-3. Phosphorylated by CIPK6 and CIPK24. Ref.12 Ref.13

Disruption phenotype

Delayed development and flowering. Ref.12

Sequence similarities

Belongs to the calcineurin regulatory subunit family.

Contains 4 EF-hand domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CIPK1Q8RWC93EBI-537541,EBI-1748677
CIPK24Q9LDI39EBI-537541,EBI-537551

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 222221Calcineurin B-like protein 4
PRO_0000073505

Regions

Domain35 – 7036EF-hand 1
Domain71 – 10636EF-hand 2
Domain108 – 14336EF-hand 3
Domain152 – 18736EF-hand 4
Calcium binding47 – 60141; atypical
Calcium binding84 – 95122
Calcium binding121 – 132123
Calcium binding165 – 176124
Compositional bias211 – 2166Poly-Glu

Sites

Site1441Involved in dimerization

Amino acid modifications

Modified residue2051Phosphoserine By similarity
Lipidation21N-myristoyl glycine Ref.6 Ref.10

Experimental info

Mutagenesis21G → A: Abolishes function in salt tolerance and loss of activation of AKT2. Ref.6 Ref.12
Mutagenesis31C → S: Loss of activation of AKT2. Ref.12
Mutagenesis2051S → A: Loss of phosphorylation. Ref.13

Secondary structure

................................... 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O81223 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DF06C3973748AFF7

FASTA22225,693
        10         20         30         40         50         60 
MGCSVSKKKK KNAMRPPGYE DPELLASVTP FTVEEVEALY ELFKKLSSSI IDDGLIHKEE 

        70         80         90        100        110        120 
FQLALFRNRN RRNLFADRIF DVFDVKRNGV IEFGEFVRSL GVFHPSAPVH EKVKFAFKLY 

       130        140        150        160        170        180 
DLRQTGFIER EELKEMVVAL LHESELVLSE DMIEVMVDKA FVQADRKNDG KIDIDEWKDF 

       190        200        210        220 
VSLNPSLIKN MTLPYLKDIN RTFPSFVSSC EEEEMELQNV SS 

« Hide

References

« Hide 'large scale' references
[1]"A calcium sensor homolog required for plant salt tolerance."
Liu J., Zhu J.-K.
Science 280:1943-1945(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis."
Shi J., Kim K.-N., Ritz O., Albrecht V., Gupta R., Harter K., Luan S., Kudla J.
Plant Cell 11:2393-2405(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CIPK6.
Strain: cv. Columbia.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones."
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:291-300(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding."
Ishitani M., Liu J., Halfter U., Kim C.-S., Shi W., Zhu J.-K.
Plant Cell 12:1667-1677(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
[7]"The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3."
Halfter U., Ishitani M., Zhu J.-K.
Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CIPK24/SOS2; CIPK6/SIP3; CIPK10/SIP1; CIPK11/SIP4 AND CIPK15/SIP2.
[8]"Regulation of SOS1, a plasma membrane Na(+)/H(+) exchanger in Arabidopsis thaliana, by SOS2 and SOS3."
Qiu Q.-S., Guo Y., Dietrich M.A., Schumaker K.S., Zhu J.-K.
Proc. Natl. Acad. Sci. U.S.A. 99:8436-8441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Calcium sensors and their interacting protein kinases: genomics of the Arabidopsis and rice CBL-CIPK signaling networks."
Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.
Plant Physiol. 134:43-58(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.
[10]"Dual fatty acyl modification determines the localization and plasma membrane targeting of CBL/CIPK Ca2+ signaling complexes in Arabidopsis."
Batistic O., Sorek N., Schueltke S., Yalovsky S., Kudla J.
Plant Cell 20:1346-1362(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[11]"CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores."
Batistic O., Waadt R., Steinhorst L., Held K., Kudla J.
Plant J. 61:211-222(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DOMAIN.
[12]"Calcium-dependent modulation and plasma membrane targeting of the AKT2 potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase complex."
Held K., Pascaud F., Eckert C., Gajdanowicz P., Hashimoto K., Corratge-Faillie C., Offenborn J.N., Lacombe B., Dreyer I., Thibaud J.B., Kudla J.
Cell Res. 21:1116-1130(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CIPK6, DISRUPTION PHENOTYPE, PHOSPHORYLATION, MUTAGENESIS OF GLY-2 AND CYS-3.
[13]"Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins."
Hashimoto K., Eckert C., Anschuetz U., Scholz M., Held K., Waadt R., Reyer A., Hippler M., Becker D., Kudla J.
J. Biol. Chem. 287:7956-7968(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH CIPK24, MUTAGENESIS OF SER-205.
[14]"Arabidopsis SOS3 plays an important role in salt tolerance by mediating calcium-dependent microfilament reorganization."
Ye J., Zhang W., Guo Y.
Plant Cell Rep. 32:139-148(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"The structure of the Arabidopsis thaliana SOS3: molecular mechanism of sensing calcium for salt stress response."
Sanchez-Barrena M.J., Martinez-Ripoll M., Zhu J.-K., Albert A.
J. Mol. Biol. 345:1253-1264(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH CALCIUM AND MANGANESE IONS, HOMODIMERIZATION.
[16]"The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3."
Sanchez-Barrena M.J., Fujii H., Angulo I., Martinez-Ripoll M., Zhu J.-K., Albert A.
Mol. Cell 26:427-435(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-207 IN COMPLEX WITH SOS2; CALCIUM AND MANGANESE IONS, INTERACTION WITH SOS2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF060553 Genomic DNA. Translation: AAC26110.1.
Y18870 mRNA. Translation: CAB39731.1.
AF192886 mRNA. Translation: AAG28402.1.
AB006701 Genomic DNA. Translation: BAB10392.1.
CP002688 Genomic DNA. Translation: AED93277.1.
CP002688 Genomic DNA. Translation: AED93278.1.
AY063993 mRNA. Translation: AAL36349.1.
AY096693 mRNA. Translation: AAM20327.1.
RefSeqNP_001190377.1. NM_001203448.1.
NP_197815.1. NM_122333.5.
UniGeneAt.20610.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V1FX-ray3.00A1-222[»]
1V1GX-ray2.70A1-222[»]
2EHBX-ray2.10A1-207[»]
ProteinModelPortalO81223.
SMRO81223. Positions 21-202.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17769. 13 interactions.
DIPDIP-34746N.
IntActO81223. 13 interactions.
STRING3702.AT5G24270.1-P.

Proteomic databases

PaxDbO81223.
PRIDEO81223.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G24270.1; AT5G24270.1; AT5G24270.
AT5G24270.2; AT5G24270.2; AT5G24270.
GeneID832494.
KEGGath:AT5G24270.

Organism-specific databases

GeneFarm4658. 458.
TAIRAT5G24270.

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000233019.
InParanoidO81223.
KOK06268.
OMATKHASRS.
PhylomeDBO81223.

Gene expression databases

GenevestigatorO81223.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR015757. Calcineur_B.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PANTHERPTHR23056:SF37. PTHR23056:SF37. 1 hit.
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO81223.

Entry information

Entry nameCNBL4_ARATH
AccessionPrimary (citable) accession number: O81223
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names