O81223 (CNBL4_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 105.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Calcineurin B-like protein 4 Alternative name(s): Protein SALT OVERLY SENSITIVE 3 | ||||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 222 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na+/H+ antiporter SOS1. May function as positive regulator of salt stress responses. 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. Ref.6 Ref.7 Ref.8 |
| 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.10 Ref.11 |
| Subcellular location | |
| Domain | The calcium-binding domain (165-176) of the EF-hand 4 can also interacts with a manganese ion. |
| Post-translational modification | Both N-myristoylation and calcium-mediated conformational changes are essential for its function. |
| Sequence similarities | Belongs to the calcineurin regulatory subunit family. Contains 4 EF-hand domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Repeat |
| Ligand | Calcium Manganese Metal-binding |
| PTM | Lipoprotein Myristate |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cellular potassium ion homeostasis Inferred from mutant phenotype PubMed 9405721. Source: TAIR detection of calcium ionInferred from mutant phenotype PubMed 9405721. Source: TAIR hypotonic salinity responseInferred from mutant phenotype PubMed 9405721. Source: TAIR |
| Cellular_component | calcineurin complex Inferred from sequence or structural similarity Ref.1. Source: TAIR cytoplasmInferred from direct assay PubMed 19686372. Source: TAIR plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | calcium ion binding Inferred from sequence or structural similarity PubMed 11230129. Source: TAIR calcium-dependent protein serine/threonine phosphatase activityInferred from sequence or structural similarity Ref.1. Source: TAIR |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CIPK1 | Q8RWC9 | 3 | EBI-537541,EBI-1748677 | |
| CIPK24 | Q9LDI3 | 9 | EBI-537541,EBI-537551 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 222 | 221 | Calcineurin B-like protein 4 | PRO_0000073505 | |||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Domain | 35 – 70 | 36 | EF-hand 1 | ||||||||||||||||||||||||||||||||||||||||
| Domain | 71 – 106 | 36 | EF-hand 2 | ||||||||||||||||||||||||||||||||||||||||
| Domain | 108 – 143 | 36 | EF-hand 3 | ||||||||||||||||||||||||||||||||||||||||
| Domain | 152 – 187 | 36 | EF-hand 4 | ||||||||||||||||||||||||||||||||||||||||
| Calcium binding | 47 – 60 | 14 | 1; atypical | ||||||||||||||||||||||||||||||||||||||||
| Calcium binding | 84 – 95 | 12 | 2 | ||||||||||||||||||||||||||||||||||||||||
| Calcium binding | 121 – 132 | 12 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Calcium binding | 165 – 176 | 12 | 4 | ||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 211 – 216 | 6 | Poly-Glu | ||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||
| Site | 144 | 1 | Involved in dimerization | ||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||
| Lipidation | 2 | 1 | N-myristoyl glycine Ref.6 | ||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 2 | 1 | G → A: Abolishes function in salt tolerance. Ref.6 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 22 – 28 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 33 – 46 | 14 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 49 – 51 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 53 – 56 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 58 – 66 | 9 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 74 – 83 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 88 – 91 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 100 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 101 – 103 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 109 – 120 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 126 – 129 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 130 – 144 | 15 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 150 – 164 | 15 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 169 – 172 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 174 – 183 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 185 – 191 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 194 – 197 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 199 – 201 | 3 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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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. 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] | "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. |
| [11] | "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. | ||||||||||||||||||||||||
| IPI | IPI00520663. | ||||||||||||||||||||||||
| RefSeq | NP_001190377.1. NM_001203448.1. NP_197815.1. NM_122333.5. | ||||||||||||||||||||||||
| UniGene | At.20610. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||
| ProteinModelPortal | O81223. | ||||||||||||||||||||||||
| SMR | O81223. Positions 21-202. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| DIP | DIP-34746N. | ||||||||||||||||||||||||
| IntAct | O81223. 13 interactions. | ||||||||||||||||||||||||
| STRING | 3702.AT5G24270.1-P. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PaxDb | O81223. | ||||||||||||||||||||||||
| PRIDE | O81223. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| EnsemblPlants | AT5G24270.1; AT5G24270.1; AT5G24270. AT5G24270.2; AT5G24270.2; AT5G24270. | ||||||||||||||||||||||||
| GeneID | 832494. | ||||||||||||||||||||||||
| KEGG | ath:AT5G24270. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| GeneFarm | 4658. 458. | ||||||||||||||||||||||||
| TAIR | At5g24270. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| eggNOG | COG5126. | ||||||||||||||||||||||||
| HOGENOM | HOG000233019. | ||||||||||||||||||||||||
| InParanoid | O81223. | ||||||||||||||||||||||||
| OMA | IERHELK. | ||||||||||||||||||||||||
| PhylomeDB | O81223. | ||||||||||||||||||||||||
| ProtClustDB | CLSN2914875. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| Genevestigator | O81223. | ||||||||||||||||||||||||
| GermOnline | AT5G24270. Arabidopsis thaliana. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| Gene3D | 1.10.238.10. 1 hit. | ||||||||||||||||||||||||
| InterPro | IPR011992. EF-hand-like_dom. IPR002048. EF_hand_dom. IPR001125. Recoverin. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF13499. EF_hand_5. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PRINTS | PR00450. RECOVERIN. | ||||||||||||||||||||||||
| SMART | SM00054. EFh. 3 hits. [Graphical view] | ||||||||||||||||||||||||
| PROSITE | PS00018. EF_HAND_1. False negative. PS50222. EF_HAND_2. 3 hits. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| EvolutionaryTrace | O81223. | ||||||||||||||||||||||||
Entry information
| Entry name | CNBL4_ARATH | ||||||||
| Accession | Primary (citable) accession number: O81223 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
