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Protein

CBL-interacting serine/threonine-protein kinase 23

Gene

CIPK23

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

Functioni

CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein leads to activation of the kinase in a calcium-dependent manner. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by phosphorylation the K+ conductance and uptake of AKT1 in low K+ condition, in response to calcium signaling and during the stomatal opening regulation by monitoring the turgor pressure in guard cells. In response to low nitrate concentration, phosphorylates NRT1.1, switching it from a low-affinity nitrate transporter to a high-affinity transporter. Confers tolerance to low potassium conditions. Involved in drought sensitivity and leaf transpiration.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mn2+1 Publication

Kineticsi

  1. KM=43.2 µM for synthetic substrate1 Publication
  1. Vmax=147.7 pmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei60ATPPROSITE-ProRule annotation1
Active sitei154Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi37 – 45ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • potassium channel activity Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • intracellular signal transduction Source: GO_Central
  • potassium ion import Source: TAIR
  • response to nutrient Source: TAIR
  • response to water deprivation Source: TAIR
  • stomatal movement Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Kinase, Potassium channel, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

ATP-binding, Manganese, Nucleotide-binding, Potassium

Names & Taxonomyi

Protein namesi
Recommended name:
CBL-interacting serine/threonine-protein kinase 23 (EC:2.7.11.1)
Alternative name(s):
Protein LOW-K(+)-SENSITIVE 1
SNF1-related kinase 3.23
SOS2-like protein kinase PKS17
Gene namesi
Name:CIPK23
Synonyms:LKS1, PKS17, SnRK3.23
Ordered Locus Names:At1g30270
ORF Names:F12P21.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G30270.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • cytosol Source: TAIR
  • nucleus Source: TAIR
  • plasma membrane Source: TAIR
  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Plants exhibit an increased drought tolerance and an enhanced sensitivity to abscisic acid (ABA) during the stomatal regulation.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi199A → V in lks1-1; enhanced sensitivity to low K(+). 1 Publication1
Mutagenesisi447L → F in lks1-2; enhanced sensitivity to low K(+). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003372241 – 482CBL-interacting serine/threonine-protein kinase 23Add BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei176PhosphoserineBy similarity1
Modified residuei190PhosphothreonineBy similarity1

Post-translational modificationi

Autophosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ93VD3.
PRIDEiQ93VD3.

PTM databases

iPTMnetiQ93VD3.

Expressioni

Tissue specificityi

In seedlings, mostly in vascular bundles, and in roots, especially in cortex and endodermis cells. In adult plants, mostly expressed in flowers, and, to a lower extent, in roots, leaves, stems and siliques, particularly in vascular tissues. Also detected in guard cells and root hairs.2 Publications

Inductioni

In roots under low K+ conditions and transiently by nitrate.3 Publications

Gene expression databases

GenevisibleiQ93VD3. AT.

Interactioni

Subunit structurei

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 AKT1, CBL1, CBL2, CBL3, CBL5, CBL8, CBL9 and NRT1.1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1Q389984EBI-974277,EBI-974289
CBL1O814456EBI-974277,EBI-974530
CBL9Q9LTB86EBI-974277,EBI-637381
NPF6.3Q050853EBI-974277,EBI-2463703

Protein-protein interaction databases

BioGridi25142. 8 interactors.
DIPiDIP-36761N.
IntActiQ93VD3. 9 interactors.
STRINGi3702.AT1G30270.1.

Structurei

Secondary structure

1482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 28Combined sources4
Beta strandi31 – 39Combined sources9
Beta strandi41 – 50Combined sources10
Turni51 – 53Combined sources3
Beta strandi56 – 63Combined sources8
Helixi64 – 68Combined sources5
Helixi73 – 85Combined sources13
Beta strandi94 – 99Combined sources6
Beta strandi101 – 108Combined sources8
Helixi117 – 123Combined sources7
Helixi128 – 147Combined sources20
Helixi157 – 159Combined sources3
Beta strandi160 – 162Combined sources3
Beta strandi168 – 170Combined sources3
Helixi175 – 177Combined sources3
Helixi180 – 183Combined sources4
Beta strandi186 – 189Combined sources4
Helixi195 – 197Combined sources3
Helixi200 – 203Combined sources4
Helixi210 – 227Combined sources18
Helixi237 – 246Combined sources10
Helixi257 – 266Combined sources10
Turni271 – 273Combined sources3
Helixi277 – 281Combined sources5
Turni284 – 289Combined sources6
Helixi305 – 307Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CZTX-ray2.30A/B/C/D25-482[»]
4CZUX-ray1.90A/B/C/D25-482[»]
ProteinModelPortaliQ93VD3.
SMRiQ93VD3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 286Protein kinasePROSITE-ProRule annotationAdd BLAST256
Domaini328 – 352NAFPROSITE-ProRule annotationAdd BLAST25

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni172 – 201Activation loopBy similarityAdd BLAST30
Regioni359 – 388PPIBy similarityAdd BLAST30

Domaini

The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases. The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases (By similarity).By similarity

Sequence similaritiesi

Contains 1 NAF domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233016.
InParanoidiQ93VD3.
OMAiNESGDQT.
OrthoDBiEOG093608WZ.
PhylomeDBiQ93VD3.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR018451. NAF/FISL_domain.
IPR004041. NAF_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF03822. NAF. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50816. NAF. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q93VD3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRTTPSRS TPSRSTPSGS SSGGRTRVGK YELGRTLGEG TFAKVKFARN
60 70 80 90 100
VENGDNVAIK VIDKEKVLKN KMIAQIKREI STMKLIKHPN VIRMFEVMAS
110 120 130 140 150
KTKIYFVLEF VTGGELFDKI SSNGRLKEDE ARKYFQQLIN AVDYCHSRGV
160 170 180 190 200
YHRDLKPENL LLDANGALKV SDFGLSALPQ QVREDGLLHT TCGTPNYVAP
210 220 230 240 250
EVINNKGYDG AKADLWSCGV ILFVLMAGYL PFEDSNLTSL YKKIFKAEFT
260 270 280 290 300
CPPWFSASAK KLIKRILDPN PATRITFAEV IENEWFKKGY KAPKFENADV
310 320 330 340 350
SLDDVDAIFD DSGESKNLVV ERREEGLKTP VTMNAFELIS TSQGLNLGSL
360 370 380 390 400
FEKQMGLVKR KTRFTSKSSA NEIVTKIEAA AAPMGFDVKT NNYKMKLTGE
410 420 430 440 450
KSGRKGQLAV ATEVFQVAPS LYMVEMRKSG GDTLEFHKFY KNLTTGLKDI
460 470 480
VWKTIDEEKE EGTDGGGTNG AMANRTIAKQ ST
Length:482
Mass (Da):53,514
Last modified:December 1, 2001 - v1
Checksum:iCAA1B526B955F5F2
GO

Sequence cautioni

The sequence AAG50566 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY035226 mRNA. Translation: AAK61494.1.
AC073506 Genomic DNA. Translation: AAG50566.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31201.1.
AY056419 mRNA. Translation: AAL08275.1.
AY090322 mRNA. Translation: AAL90983.1.
PIRiA86427.
RefSeqiNP_564353.1. NM_102766.6.
UniGeneiAt.17201.

Genome annotation databases

EnsemblPlantsiAT1G30270.1; AT1G30270.1; AT1G30270.
GeneIDi839907.
GrameneiAT1G30270.1; AT1G30270.1; AT1G30270.
KEGGiath:AT1G30270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY035226 mRNA. Translation: AAK61494.1.
AC073506 Genomic DNA. Translation: AAG50566.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31201.1.
AY056419 mRNA. Translation: AAL08275.1.
AY090322 mRNA. Translation: AAL90983.1.
PIRiA86427.
RefSeqiNP_564353.1. NM_102766.6.
UniGeneiAt.17201.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CZTX-ray2.30A/B/C/D25-482[»]
4CZUX-ray1.90A/B/C/D25-482[»]
ProteinModelPortaliQ93VD3.
SMRiQ93VD3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi25142. 8 interactors.
DIPiDIP-36761N.
IntActiQ93VD3. 9 interactors.
STRINGi3702.AT1G30270.1.

PTM databases

iPTMnetiQ93VD3.

Proteomic databases

PaxDbiQ93VD3.
PRIDEiQ93VD3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G30270.1; AT1G30270.1; AT1G30270.
GeneIDi839907.
GrameneiAT1G30270.1; AT1G30270.1; AT1G30270.
KEGGiath:AT1G30270.

Organism-specific databases

TAIRiAT1G30270.

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233016.
InParanoidiQ93VD3.
OMAiNESGDQT.
OrthoDBiEOG093608WZ.
PhylomeDBiQ93VD3.

Miscellaneous databases

PROiQ93VD3.

Gene expression databases

GenevisibleiQ93VD3. AT.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR018451. NAF/FISL_domain.
IPR004041. NAF_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF03822. NAF. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50816. NAF. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCIPKN_ARATH
AccessioniPrimary (citable) accession number: Q93VD3
Secondary accession number(s): Q9C753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.