Q9LDI3 (CIPKO_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.7 Ref.9 Ref.13
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Manganese.
Subunit structure	Interacts with CBL1, CBL4/SOS3, CBL9, and with the protein phosphatase 2C ABI2. Ref.7 Ref.11 Ref.14 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. Ref.8
Post-translational modification	Autophosphorylated.
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.
Sequence caution	The sequence AAF67384.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Ligand	ATP-binding Manganese Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to salt stress Inferred from mutant phenotype PubMed 9668136. Source: TAIR signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	plant-type vacuole membrane Inferred from direct assay PubMed 17825054. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Inferred from direct assay Ref.1. Source: TAIR protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-537551,EBI-537551
ABI2	O04719	4	EBI-537551,EBI-537680
CAM4	P25854	2	EBI-537551,EBI-1235664
CAM7	P59220	2	EBI-537551,EBI-1236031
CBL1	O81445	3	EBI-537551,EBI-974530
CBL10	Q7FRS8	5	EBI-537551,EBI-2026616
CBL10	Q7FRS8-2	4	EBI-537551,EBI-2026677
CBL4	O81223	9	EBI-537551,EBI-537541
CML9	Q9S744	2	EBI-537551,EBI-1236048
NDPK2	O64903	3	EBI-537551,EBI-349517

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 446

446

CBL-interacting serine/threonine-protein kinase 24

PRO_0000085877

Regions

Domain

11 – 264

254

Protein kinase

Domain

305 – 329

25

NAF

Nucleotide binding

17 – 25

9

ATP By similarity

Region

152 – 179

28

Activation loop

Region

336 – 365

30

PPI

Sites

Active site

134

1

Proton acceptor By similarity

Binding site

40

1

ATP By similarity

Experimental info

Mutagenesis

40

1

K → N: Abolishes autophosphorylation. Ref.1

Mutagenesis

156

1

S → D: Increases kinase activity. Ref.10

Mutagenesis

168

1

T → D: Increases kinase activity. Ref.7

Mutagenesis

175

1

Y → D: Increases kinase activity. Ref.10

Mutagenesis

197

1

G → E: Abolishes autophosphorylation. Ref.1

Secondary structure

1

.

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446

Helix Strand Turn

Details...

Helix

312 – 316

5

Turn

320 – 322

3

Helix

324 – 328

5

Beta strand

340 – 343

4

Helix

347 – 360

14

Beta strand

363 – 376

14

Helix

381 – 383

3

Beta strand

386 – 395

10

Beta strand

398 – 408

11

Helix

410 – 423

14

Turn

425 – 427

3

Sequences

	Sequence		Length	Mass (Da)
	Q9LDI3 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 99FDF3A778E1093D	FASTA	446	50,635
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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 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.

IPI

IPI00525790.

RefSeq

NP_198391.1. NM_122932.4.

UniGene

At.7930.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EHB	X-ray	2.10	D	304-446	[»]

ProteinModelPortal

Q9LDI3.

SMR

Q9LDI3. Positions 6-430.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34745N.

IntAct

Q9LDI3. 30 interactions.

MINT

MINT-274819.

STRING

3702.AT5G35410.1-P.

Proteomic databases

PaxDb

Q9LDI3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G35410.1; AT5G35410.1; AT5G35410.

GeneID

833502.

KEGG

ath:AT5G35410.

Organism-specific databases

TAIR

At5g35410.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233016.

InParanoid

Q9LDI3.

OMA

NAFEMIT.

PhylomeDB

Q9LDI3.

ProtClustDB

CLSN2686486.

Gene expression databases

Genevestigator

Q9LDI3.

GermOnline

AT5G35410. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR018451. NAF/FISL_domain.
IPR004041. NAF_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF03822. NAF. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50816. NAF. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9LDI3.

Entry information

Entry name

CIPKO_ARATH

Accession

Primary (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:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program