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Q9LDI3 (CIPKO_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CBL-interacting serine/threonine-protein kinase 24

EC=2.7.11.1
Alternative name(s):
Protein SALT OVERLY SENSITIVE 2
SNF1-related kinase 3.11
Gene names
Name:CIPK24
Synonyms:SnRK3.11, SOS2
Ordered Locus Names:At5g35410
ORF Names:F6I13.1, K21B8.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulatory pathway for the control of intracellular Na+ and K+ homeostasis and salt tolerance. Activates the vacuolar H+/Ca2+ antiporter CAX1 and operates in synergy with CBL4/SOS3 to activate the plasma membrane Na+/H+ antiporter SOS1. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Phosphorylates CBL1, CBL4 and CBL10. Ref.7 Ref.9 Ref.13 Ref.16

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.16

Cofactor

Manganese. Ref.16

Subunit structure

Interacts with CBL1, CBL2, CBL4/SOS3, CBL5, CBL9, CBL10 and with the protein phosphatase 2C ABI2. Ref.7 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17

Subcellular location

Cytoplasm. Nucleus. Note: Targeted to the cell membrane when interacting with CBL1 or CBL5 and to the tonoplast when interacting with CBL2 orCBL10. Ref.15

Induction

Up-regulated in roots by salt stress.

Domain

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. The C-terminal part (309-446) of the protein is required for the phosphorylation of CBL, but is not involved in autophosphorylation. Ref.8 Ref.16

Post-translational modification

Autophosphorylated. Ref.16

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 NAF domain.

Contains 1 protein kinase domain.

Biophysicochemical properties

Kinetic parameters:

KM=131.2 µM for synthetic substrate Ref.16

Vmax=1304 pmol/min/mg enzyme

Sequence caution

The sequence AAF67384.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446CBL-interacting serine/threonine-protein kinase 24
PRO_0000085877

Regions

Domain11 – 264254Protein kinase
Domain305 – 32925NAF
Nucleotide binding17 – 259ATP By similarity
Region152 – 17928Activation loop
Region336 – 36530PPI

Sites

Active site1341Proton acceptor By similarity
Binding site401ATP By similarity

Amino acid modifications

Modified residue1561Phosphoserine By similarity
Modified residue1681Phosphothreonine By similarity
Modified residue1691Phosphothreonine By similarity

Experimental info

Mutagenesis401K → N: Abolishes autophosphorylation. Ref.1
Mutagenesis1561S → D: Increases kinase activity. Ref.10
Mutagenesis1681T → D: Increases kinase activity. Ref.7
Mutagenesis1751Y → D: Increases kinase activity. Ref.10
Mutagenesis1971G → E: Abolishes autophosphorylation. Ref.1

Secondary structure

....................... 446
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9LDI3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 99FDF3A778E1093D

FASTA44650,635
        10         20         30         40         50         60 
MTKKMRRVGK YEVGRTIGEG TFAKVKFARN TDTGDNVAIK IMAKSTILKN RMVDQIKREI 

        70         80         90        100        110        120 
SIMKIVRHPN IVRLYEVLAS PSKIYIVLEF VTGGELFDRI VHKGRLEESE SRKYFQQLVD 

       130        140        150        160        170        180 
AVAHCHCKGV YHRDLKPENL LLDTNGNLKV SDFGLSALPQ EGVELLRTTC GTPNYVAPEV 

       190        200        210        220        230        240 
LSGQGYDGSA ADIWSCGVIL FVILAGYLPF SETDLPGLYR KINAAEFSCP PWFSAEVKFL 

       250        260        270        280        290        300 
IHRILDPNPK TRIQIQGIKK DPWFRLNYVP IRAREEEEVN LDDIRAVFDG IEGSYVAENV 

       310        320        330        340        350        360 
ERNDEGPLMM NAFEMITLSQ GLNLSALFDR RQDFVKRQTR FVSRREPSEI IANIEAVANS 

       370        380        390        400        410        420 
MGFKSHTRNF KTRLEGLSSI KAGQLAVVIE IYEVAPSLFM VDVRKAAGET LEYHKFYKKL 

       430        440 
CSKLENIIWR ATEGIPKSEI LRTITF 

« Hide

References

« Hide 'large scale' references
[1]"The Arabidopsis thaliana SOS2 gene encodes a protein kinase that is required for salt tolerance."
Liu J., Ishitani M., Halfter U., Kim C.-S., Zhu J.-K.
Proc. Natl. Acad. Sci. U.S.A. 97:3730-3734(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, MUTAGENESIS OF LYS-40 AND GLY-197.
Strain: cv. Columbia.
[2]"Molecular characterization of the CIPK gene family from Arabidopsis thaliana."
Weinl S., Albrecht V., Kudla J.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. XI."
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"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. expand/collapse author list , 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.
[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 CBL4, MUTAGENESIS OF THR-168.
[8]"Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance."
Guo Y., Halfter U., Ishitani M., Zhu J.-K.
Plant Cell 13:1383-1400(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION DOMAINS.
[9]"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.
[10]"Biochemical characterization of the Arabidopsis protein kinase SOS2 that functions in salt tolerance."
Gong D., Guo Y., Jagendorf A.T., Zhu J.-K.
Plant Physiol. 130:256-264(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-156 AND TYR-175.
[11]"A novel domain in the protein kinase SOS2 mediates interaction with the protein phosphatase 2C ABI2."
Ohta M., Guo Y., Halfter U., Zhu J.-K.
Proc. Natl. Acad. Sci. U.S.A. 100:11771-11776(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABI2.
[12]"The Arabidopsis CDPK-SnRK superfamily of protein kinases."
Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N., Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K., Zhu J.-K., Harmon A.C.
Plant Physiol. 132:666-680(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[13]"The protein kinase SOS2 activates the Arabidopsis H(+)/Ca(2+) antiporter CAX1 to integrate calcium transport and salt tolerance."
Cheng N.-H., Pittman J.K., Zhu J.-K., Hirschi K.D.
J. Biol. Chem. 279:2922-2926(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"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 CBL1 AND CBL9.
[15]"The calcium sensor CBL10 mediates salt tolerance by regulating ion homeostasis in Arabidopsis."
Kim B.G., Waadt R., Cheong Y.H., Pandey G.K., Dominguez-Solis J.R., Schueltke S., Lee S.C., Kudla J., Luan S.
Plant J. 52:473-484(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL1; CBL2; CBL5 AND CBL10, SUBCELLULAR LOCATION.
[16]"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, INTERACTION WITH CBL1; CBL4 AND CBL10, DOMAIN.
[17]"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 304-446 IN COMPLEX WITH SOS3, INTERACTION WITH SOS3 AND ABI2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF237670 Genomic DNA. Translation: AAF62923.1.
AF395081 mRNA. Translation: AAK72257.1.
AB025611 Genomic DNA. Translation: BAA98146.1.
AF262044 Genomic DNA. Translation: AAF67384.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93966.1.
AY099621 mRNA. Translation: AAM20472.1.
BT002138 mRNA. Translation: AAN72149.1.
RefSeqNP_198391.1. NM_122932.4.
UniGeneAt.7930.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EHBX-ray2.10D304-446[»]
ProteinModelPortalQ9LDI3.
SMRQ9LDI3. Positions 6-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid18756. 20 interactions.
DIPDIP-34745N.
IntActQ9LDI3. 30 interactions.
MINTMINT-274819.
STRING3702.AT5G35410.1-P.

Proteomic databases

PaxDbQ9LDI3.
PRIDEQ9LDI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G35410.1; AT5G35410.1; AT5G35410.
GeneID833502.
KEGGath:AT5G35410.

Organism-specific databases

TAIRAT5G35410.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
InParanoidQ9LDI3.
OMANAFEMIT.
PhylomeDBQ9LDI3.
ProtClustDBCLSN2686486.

Enzyme and pathway databases

BioCycARA:AT5G35410-MONOMER.

Gene expression databases

GenevestigatorQ9LDI3.

Family and domain databases

InterProIPR011009. 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]
PfamPF03822. NAF. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50816. NAF. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9LDI3.

Entry information

Entry nameCIPKO_ARATH
AccessionPrimary (citable) accession number: Q9LDI3
Secondary accession number(s): Q9LKR2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names