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Q93VD3

- CIPKN_ARATH

UniProt

Q93VD3 - CIPKN_ARATH

Protein

CBL-interacting serine/threonine-protein kinase 23

Gene

CIPK23

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei60 – 601ATPPROSITE-ProRule annotation
    Active sitei154 – 1541Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi37 – 459ATPPROSITE-ProRule annotation

    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

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

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. cytosol Source: TAIR
    3. nucleus Source: TAIR
    4. plasma membrane Source: TAIR
    5. plastid Source: TAIR

    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 – 1761PhosphoserineBy similarity
    Modified residuei190 – 1901PhosphothreonineBy similarity
    Modified residuei191 – 1911PhosphothreonineBy similarity

    Post-translational modificationi

    Autophosphorylated.1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 286256Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini328 – 35225NAFPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni172 – 20130Activation loopBy similarityAdd
    BLAST
    Regioni359 – 38830PPIBy 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.By similarity

    Sequence similaritiesi

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

    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

    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: October 1, 2014
    This is version 96 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