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Protein

Calcineurin B-like protein 2

Gene

CBL2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei155 – 1551Involved in dimerizationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi58 – 71141; atypicalAdd
BLAST
Calcium bindingi95 – 106122Add
BLAST
Calcium bindingi132 – 143123Add
BLAST
Calcium bindingi176 – 187124Add
BLAST

GO - Molecular functioni

  • calcium ion binding Source: TAIR

GO - Biological processi

  • calcium-mediated signaling Source: TAIR
  • potassium ion homeostasis Source: TAIR
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcineurin B-like protein 2
Alternative name(s):
SOS3-like calcium-binding protein 1
Gene namesi
Name:CBL2
Synonyms:SCABP1
Ordered Locus Names:At5g55990
ORF Names:MDA7.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G55990.

Subcellular locationi

GO - Cellular componenti

  • cytosolic ribosome Source: TAIR
  • membrane Source: TAIR
  • plant-type vacuole membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Disruption phenotypei

No visible phenotype when grown under normal conditions; due to partial redundancy with CLB3. Chlorotic symptoms under low-K+ stress. Clb2 and cbl3 double mutants show stunted growth, reduced fertility and necrotic lesions at leaf tips. They have also a reduced vacuolar H+-ATPase activity, are hypersensitive to excessive metal ions and are more tolerant to low-K+ conditions.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 31Q → E: No effect on tonoplast targeting. 1 Publication
Mutagenesisi4 – 41C → S: Loss of tonoplast targeting. Loss of tonoplast targeting; when associated with S-12 and S-18. 1 Publication
Mutagenesisi12 – 121C → S: Decreased tonoplast targeting. Loss of tonoplast targeting; when associated with S-18. Loss of tonoplast targeting; when associated with S-4 and S-18. 1 Publication
Mutagenesisi18 – 181C → S: Loss of tonoplast targeting. Loss of tonoplast targeting; when associated with S-12. Loss of tonoplast targeting; when associated with S-4 and S-12. 1 Publication
Mutagenesisi71 – 711E → A: No effect on binding to CIPK14. 1 Publication
Mutagenesisi106 – 1061E → A: No effect on binding to CIPK14. 1 Publication
Mutagenesisi143 – 1431E → A: No effect on binding to CIPK14. 1 Publication
Mutagenesisi187 – 1871E → A: No effect on binding to CIPK14. 1 Publication
Mutagenesisi216 – 2161S → A: Loss of phosphorylaton. 1 Publication
Mutagenesisi216 – 2161S → D: Increased interaction with CIPK11. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226Calcineurin B-like protein 2PRO_0000073503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi4 – 41S-palmitoyl cysteine1 Publication
Lipidationi12 – 121S-palmitoyl cysteine1 Publication
Lipidationi18 – 181S-palmitoyl cysteine1 Publication
Modified residuei216 – 2161Phosphoserine; by CIPK11 and CIPK141 Publication

Post-translational modificationi

S-acylated in vivo by PAT10. The ratio of acylation by either palmitate or stearate between Cys-4, Cys-12 and Cys-18 is unknown.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ8LAS7.
PRIDEiQ8LAS7.

PTM databases

iPTMnetiQ8LAS7.
SwissPalmiQ8LAS7.

Expressioni

Tissue specificityi

Ubiquitous. Stronger expression in aerial parts. Expressed in guard cells, meristems and elongation zones of roots, mesophyll cells of leaves, cortex and pith of inflorescence stems and anthers and stamen filaments in flowers.4 Publications

Developmental stagei

Expressed early during germination and increases to a peak level when seedlings are established.1 Publication

Inductioni

By light.1 Publication

Gene expression databases

GenevisibleiQ8LAS7. AT.

Interactioni

Subunit structurei

Homodimer (By similarity). Part of a K+-channel calcium-sensing kinase/phosphatase complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a K+-channel (AKT1). Interacts with PP2CA, CIPK1, CIPK2, CIPK4, CIPK6, CIPK7, CIPK9, CIPK11, CIPK12, CIPK13, CIPK14/SR1, CIPK16, CIPK23, and CIPK24.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CIPK1Q8RWC94EBI-485991,EBI-1748677
CIPK11O229325EBI-485991,EBI-537638
CIPK12Q9SN434EBI-485991,EBI-637523
CIPK13O229714EBI-485991,EBI-637402
CIPK14Q9LZW49EBI-485991,EBI-307576
CIPK6O655543EBI-485991,EBI-537615

Protein-protein interaction databases

BioGridi20941. 20 interactions.
DIPiDIP-32474N.
IntActiQ8LAS7. 19 interactions.
STRINGi3702.AT5G55990.1.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 396Combined sources
Helixi44 – 5815Combined sources
Beta strandi60 – 623Combined sources
Beta strandi64 – 674Combined sources
Helixi69 – 779Combined sources
Turni81 – 833Combined sources
Helixi85 – 9410Combined sources
Beta strandi99 – 1024Combined sources
Helixi104 – 11310Combined sources
Helixi120 – 13112Combined sources
Beta strandi135 – 1406Combined sources
Helixi141 – 15414Combined sources
Helixi161 – 17515Combined sources
Beta strandi180 – 1834Combined sources
Helixi185 – 19410Combined sources
Helixi196 – 2027Combined sources
Helixi205 – 2095Combined sources
Helixi210 – 2134Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UHNX-ray2.10A32-220[»]
2ZFDX-ray1.20A1-226[»]
ProteinModelPortaliQ8LAS7.
SMRiQ8LAS7. Positions 32-220.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8LAS7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 8146EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini82 – 11736EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini119 – 15436EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini163 – 19836EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Domaini

EF-hands 1 and 4 have been shown to bind calcium. It is not known if EF-hands 2 and 3 are capable of calcium-binding. The N-terminal 22 amino acids are necessary and sufficient for vacuolar membrane targeting.1 Publication

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
HOGENOMiHOG000233019.
InParanoidiQ8LAS7.
OMAiLEHNSHT.
OrthoDBiEOG09360LEW.
PhylomeDBiQ8LAS7.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13202. EF-hand_5. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8LAS7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQCVDGIKH LCTSVLGCFD LDLYKQSGGL GDPELLARDT VFSVSEIEAL
60 70 80 90 100
YELFKKISSA VIDDGLINKE EFQLALFKTN KKESLFADRV FDLFDTKHNG
110 120 130 140 150
ILGFEEFARA LSVFHPNAPI DDKIHFSFQL YDLKQQGFIE RQEVKQMVVA
160 170 180 190 200
TLAESGMNLK DTVIEDIIDK TFEEADTKHD GKIDKEEWRS LVLRHPSLLK
210 220
NMTLQYLKDI TTTFPSFVFH SQVEDT
Length:226
Mass (Da):25,809
Last modified:December 21, 2004 - v2
Checksum:i342A013FC28D1445
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021M → V in AAM65177 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076252 mRNA. Translation: AAC26009.1.
AB011476 Genomic DNA. Translation: BAB09281.1.
CP002688 Genomic DNA. Translation: AED96707.1.
AY052304 mRNA. Translation: AAK96497.1.
AY139808 mRNA. Translation: AAM98114.1.
AY087638 mRNA. Translation: AAM65177.1.
PIRiT51357.
RefSeqiNP_200410.1. NM_124981.3.
UniGeneiAt.25275.
At.8049.

Genome annotation databases

EnsemblPlantsiAT5G55990.1; AT5G55990.1; AT5G55990.
GeneIDi835697.
GrameneiAT5G55990.1; AT5G55990.1; AT5G55990.
KEGGiath:AT5G55990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076252 mRNA. Translation: AAC26009.1.
AB011476 Genomic DNA. Translation: BAB09281.1.
CP002688 Genomic DNA. Translation: AED96707.1.
AY052304 mRNA. Translation: AAK96497.1.
AY139808 mRNA. Translation: AAM98114.1.
AY087638 mRNA. Translation: AAM65177.1.
PIRiT51357.
RefSeqiNP_200410.1. NM_124981.3.
UniGeneiAt.25275.
At.8049.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UHNX-ray2.10A32-220[»]
2ZFDX-ray1.20A1-226[»]
ProteinModelPortaliQ8LAS7.
SMRiQ8LAS7. Positions 32-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20941. 20 interactions.
DIPiDIP-32474N.
IntActiQ8LAS7. 19 interactions.
STRINGi3702.AT5G55990.1.

PTM databases

iPTMnetiQ8LAS7.
SwissPalmiQ8LAS7.

Proteomic databases

PaxDbiQ8LAS7.
PRIDEiQ8LAS7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G55990.1; AT5G55990.1; AT5G55990.
GeneIDi835697.
GrameneiAT5G55990.1; AT5G55990.1; AT5G55990.
KEGGiath:AT5G55990.

Organism-specific databases

TAIRiAT5G55990.

Phylogenomic databases

eggNOGiKOG0034. Eukaryota.
COG5126. LUCA.
HOGENOMiHOG000233019.
InParanoidiQ8LAS7.
OMAiLEHNSHT.
OrthoDBiEOG09360LEW.
PhylomeDBiQ8LAS7.

Miscellaneous databases

EvolutionaryTraceiQ8LAS7.
PROiQ8LAS7.

Gene expression databases

GenevisibleiQ8LAS7. AT.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13202. EF-hand_5. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCNBL2_ARATH
AccessioniPrimary (citable) accession number: Q8LAS7
Secondary accession number(s): O81446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: September 7, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Blockage of vesicle trafficking by Brefeldin-A does not affect S-acylation and vacuolar membrane targeting of CBL2.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.