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Q93VD3

- CIPKN_ARATH

UniProt

Q93VD3 - CIPKN_ARATH

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Protein

CBL-interacting serine/threonine-protein kinase 23

Gene
CIPK23, LKS1, PKS17, SnRK3.23, At1g30270, F12P21.6
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Manganese.1 Publication

Kineticsi

  1. KM=43.2 µM for synthetic substrate1 Publication

Vmax=147.7 pmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601ATP By similarity
Active sitei154 – 1541Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 459ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. potassium channel activity Source: UniProtKB-KW
  3. protein binding Source: IntAct
  4. protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  1. potassium ion import Source: TAIR
  2. response to nutrient Source: TAIR
  3. response to water deprivation Source: TAIR
  4. signal transduction Source: InterPro
  5. 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

Enzyme and pathway databases

BioCyciARA:AT1G30270-MONOMER.

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
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G30270.

Subcellular locationi

Cell membrane; Peripheral membrane protein
Note: Associated to the plasma membrane when associated with AKT1, CBL1 and CBL9.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: TAIR
  2. cytosol Source: TAIR
  3. nucleus Source: TAIR
  4. plasma membrane Source: TAIR
  5. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991A → V in lks1-1; enhanced sensitivity to low K(+). 1 Publication
Mutagenesisi447 – 4471L → F in lks1-2; enhanced sensitivity to low K(+). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482CBL-interacting serine/threonine-protein kinase 23PRO_0000337224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761Phosphoserine By similarity
Modified residuei190 – 1901Phosphothreonine By similarity
Modified residuei191 – 1911Phosphothreonine By similarity

Post-translational modificationi

Autophosphorylated.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ93VD3.
PRIDEiQ93VD3.

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

GenevestigatoriQ93VD3.

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 interactions.
DIPiDIP-36761N.
IntActiQ93VD3. 9 interactions.
STRINGi3702.AT1G30270.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ93VD3.
SMRiQ93VD3. Positions 24-475.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 286256Protein kinaseAdd
BLAST
Domaini328 – 35225NAFAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 20130Activation loop By similarityAdd
BLAST
Regioni359 – 38830PPI By similarityAdd
BLAST

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.

Sequence similaritiesi

Contains 1 NAF domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233016.
InParanoidiQ93VD3.
KOiK00924.
OMAiEVIENEW.
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.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
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

MASRTTPSRS TPSRSTPSGS SSGGRTRVGK YELGRTLGEG TFAKVKFARN    50
VENGDNVAIK VIDKEKVLKN KMIAQIKREI STMKLIKHPN VIRMFEVMAS 100
KTKIYFVLEF VTGGELFDKI SSNGRLKEDE ARKYFQQLIN AVDYCHSRGV 150
YHRDLKPENL LLDANGALKV SDFGLSALPQ QVREDGLLHT TCGTPNYVAP 200
EVINNKGYDG AKADLWSCGV ILFVLMAGYL PFEDSNLTSL YKKIFKAEFT 250
CPPWFSASAK KLIKRILDPN PATRITFAEV IENEWFKKGY KAPKFENADV 300
SLDDVDAIFD DSGESKNLVV ERREEGLKTP VTMNAFELIS TSQGLNLGSL 350
FEKQMGLVKR KTRFTSKSSA NEIVTKIEAA AAPMGFDVKT NNYKMKLTGE 400
KSGRKGQLAV ATEVFQVAPS LYMVEMRKSG GDTLEFHKFY KNLTTGLKDI 450
VWKTIDEEKE EGTDGGGTNG AMANRTIAKQ ST 482
Length:482
Mass (Da):53,514
Last modified:December 1, 2001 - v1
Checksum:iCAA1B526B955F5F2
GO

Sequence cautioni

The sequence AAG50566.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_102766.5.
UniGeneiAt.17201.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A86427.
RefSeqi NP_564353.1. NM_102766.5.
UniGenei At.17201.

3D structure databases

ProteinModelPortali Q93VD3.
SMRi Q93VD3. Positions 24-475.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 25142. 8 interactions.
DIPi DIP-36761N.
IntActi Q93VD3. 9 interactions.
STRINGi 3702.AT1G30270.1-P.

Proteomic databases

PaxDbi Q93VD3.
PRIDEi Q93VD3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G30270.1 ; AT1G30270.1 ; AT1G30270 .
GeneIDi 839907.
KEGGi ath:AT1G30270.

Organism-specific databases

TAIRi AT1G30270.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233016.
InParanoidi Q93VD3.
KOi K00924.
OMAi EVIENEW.
PhylomeDBi Q93VD3.

Enzyme and pathway databases

BioCyci ARA:AT1G30270-MONOMER.

Miscellaneous databases

PROi Q93VD3.

Gene expression databases

Genevestigatori Q93VD3.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR018451. NAF/FISL_domain.
IPR004041. NAF_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF03822. NAF. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50816. NAF. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the CIPK gene family from Arabidopsis thaliana."
    Weinl S., Albrecht V., Kudla J.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
    , 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.
  5. Cited for: GENE FAMILY, NOMENCLATURE.
  6. "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: INTERACTION WITH CBL9.
  7. "Calcium signaling networks channel plant K+ uptake."
    Hedrich R., Kudla J.
    Cell 125:1221-1223(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis."
    Xu J., Li H.-D., Chen L.-Q., Wang Y., Liu L.-L., He L., Wu W.-H.
    Cell 125:1347-1360(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-199 AND LEU-447, INTERACTION WITH AKT1; CBL1; CBL2; CBL3; CBL5; CBL8 AND CBL9, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION.
  9. "A Ca(2)+ signaling pathway regulates a K(+) channel for low-K response in Arabidopsis."
    Li L., Kim B.-G., Cheong Y.H., Pandey G.K., Luan S.
    Proc. Natl. Acad. Sci. U.S.A. 103:12625-12630(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AKT1, AUTOPHOSPHORYLATION.
  10. "Two calcineurin B-like calcium sensors, interacting with protein kinase CIPK23, regulate leaf transpiration and root potassium uptake in Arabidopsis."
    Cheong Y.H., Pandey G.K., Grant J.J., Batistic O., Li L., Kim B.-G., Lee S.-C., Kudla J., Luan S.
    Plant J. 52:223-239(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CBL1 AND CBL9, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  11. "A protein phosphorylation/dephosphorylation network regulates a plant potassium channel."
    Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G., Buchanan B.B., Luan S.
    Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AKT1; CBL1; CBL2; CBL3 AND CBL9.
  12. "CHL1 functions as a nitrate sensor in plants."
    Ho C.H., Lin S.H., Hu H.C., Tsay Y.F.
    Cell 138:1184-1194(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY NITRATE, INTERACTION WITH NRT1.1.
  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: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION.

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: June 11, 2014
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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