Q39016 (CDPKB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calcium-dependent protein kinase 11
EC=2.7.11.1

Alternative name(s):
Calcium-dependent protein kinase isoform CDPK2
Short name=AtCDPK2

Gene names

Name:	CPK11
Synonyms:	CDPK2
Ordered Locus Names:	At1g35670
ORF Names:	F15O4.8

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	495 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in signal transduction pathways that involve calcium as a second messenger. Functions as regulator of the calcium-mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA-responsive transcription factors ABF1 and ABF4 in vitro. Ref.1 Ref.10
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by calcium. Autophosphorylation may play an important role in the regulation of the kinase activity By similarity.
Subunit structure	Interacts with Di19. Ref.8
Subcellular location	Cytoplasm. Nucleus Ref.8.
Induction	By drought and high-slat stress, but not by low-temperature, heat stress or abscisic acid treatment. Ref.1
Domain	There is 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (290-320) inactivates kinase activity under calcium-free conditions By similarity.
Disruption phenotype	Mutant cpk11-2 shows reduced ABA and salt responsiveness in seed germination. Ref.10
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily. Contains 4 EF-hand domains. Contains 1 protein kinase domain.
Sequence caution	The sequence AAF79386.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of abscisic acid mediated signaling pathway Inferred from mutant phenotype Ref.10. Source: TAIR protein autophosphorylation Inferred from direct assay PubMed 21477822. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 17317660. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: InterPro calmodulin-dependent protein kinase activity Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADF3	Q9ZSK4	5	EBI-979321,EBI-2009725
At1g52740	Q9C944	9	EBI-979321,EBI-1537419
At3g26510	Q27GK5	5	EBI-979321,EBI-2297208
At5g52550	Q940C2	6	EBI-979321,EBI-2298422
BT2	Q94BN0	7	EBI-979321,EBI-540986
CHLP	Q9CA67	5	EBI-979321,EBI-2298544
DI19-1	Q39083	25	EBI-979321,EBI-979339
dl3455w	O23338	6	EBI-979321,EBI-2296482
F5I14.18	O04482	4	EBI-979321,EBI-2298606
MTACP2	O80800	4	EBI-979321,EBI-2298689
TOC33	O23680	4	EBI-979321,EBI-639377

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 495	495	Calcium-dependent protein kinase 11		PRO_0000304513
Regions
	Domain	26 – 284	259	Protein kinase
	Domain	327 – 362	36	EF-hand 1
	Domain	363 – 398	36	EF-hand 2
	Domain	399 – 434	36	EF-hand 3
	Domain	435 – 468	34	EF-hand 4
	Nucleotide binding	32 – 40	9	ATP By similarity
	Calcium binding	340 – 351	12	1 By similarity
	Calcium binding	376 – 387	12	2 By similarity
	Calcium binding	412 – 423	12	3 By similarity
	Calcium binding	446 – 457	12	4 By similarity
	Region	290 – 320	31	Autoinhibitory domain By similarity
Sites
	Active site	150	1	Proton acceptor By similarity
	Binding site	55	1	ATP By similarity
Amino acid modifications
	Modified residue	361	1	Phosphoserine Ref.9
Experimental info
	Mutagenesis	150	1	D → A: Loss of activity. Ref.8
	Mutagenesis	171	1	D → A: Loss of activity. Ref.8
	Mutagenesis	306	1	F → A: Constitutive activity. Ref.8
	Sequence conflict	403	1	N → I in BAA04830. Ref.1
	Sequence conflict	410	1	Y → D in BAA04830. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q39016 [UniParc]. Last modified May 3, 2011. Version 2. Checksum: 2DD0ED8C234EF2F7	FASTA	495	55,916
	10 20 30 40 50 60 METKPNPRRP SNTVLPYQTP RLRDHYLLGK KLGQGQFGTT YLCTEKSTSA NYACKSIPKR 70 80 90 100 110 120 KLVCREDYED VWREIQIMHH LSEHPNVVRI KGTYEDSVFV HIVMEVCEGG ELFDRIVSKG 130 140 150 160 170 180 HFSEREAVKL IKTILGVVEA CHSLGVMHRD LKPENFLFDS PKDDAKLKAT DFGLSVFYKP 190 200 210 220 230 240 GQYLYDVVGS PYYVAPEVLK KCYGPEIDVW SAGVILYILL SGVPPFWAET ESGIFRQILQ 250 260 270 280 290 300 GKLDFKSDPW PTISEAAKDL IYKMLERSPK KRISAHEALC HPWIVDEQAA PDKPLDPAVL 310 320 330 340 350 360 SRLKQFSQMN KIKKMALRVI AERLSEEEIG GLKELFKMID TDNSGTITFE ELKAGLKRVG 370 380 390 400 410 420 SELMESEIKS LMDAADIDNS GTIDYGEFLA ATLHMNKMER EENLVAAFSY FDKDGSGYIT 430 440 450 460 470 480 IDELQSACTE FGLCDTPLDD MIKEIDLDND GKIDFSEFTA MMRKGDGVGR SRTMMKNLNF 490 NIADAFGVDG EKSDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two genes that encode Ca(2+)-dependent protein kinases are induced by drought and high-salt stresses in Arabidopsis thaliana." Urao T., Katagiri T., Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N., Shinozaki K. Mol. Gen. Genet. 244:331-340(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION.
[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]	"The CDPK superfamily of protein kinases." Harmon A.C., Gribskov M., Gubrium E., Harper J.F. New Phytol. 151:175-183(2001) Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family." Cheng S.-H., Willmann M.R., Chen H.-C., Sheen J. Plant Physiol. 129:469-485(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[7]	"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.
[8]	"A novel yeast two-hybrid approach to identify CDPK substrates: characterization of the interaction between AtCPK11 and AtDi19, a nuclear zinc finger protein." Rodriguez Milla M.A., Uno Y., Chang I.-F., Townsend J., Maher E.A., Quilici D., Cushman J.C. FEBS Lett. 580:904-911(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DI19, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-150; ASP-171 AND PHE-306.
[9]	"A phyloproteomic characterization of in vitro autophosphorylation in calcium-dependent protein kinases." Hegeman A.D., Rodriguez M., Han B.W., Uno Y., Phillips G.N. Jr., Hrabak E.M., Cushman J.C., Harper J.F., Harmon A.C., Sussman M.R. Proteomics 6:3649-3664(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, MASS SPECTROMETRY.
[10]	"Two calcium-dependent protein kinases, CPK4 and CPK11, regulate abscisic acid signal transduction in Arabidopsis." Zhu S.-Y., Yu X.-C., Wang X.-J., Zhao R., Li Y., Fan R.-C., Shang Y., Du S.-Y., Wang X.-F., Wu F.-Q., Xu Y.-H., Zhang X.-Y., Zhang D.-P. Plant Cell 19:3019-3036(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D21806 mRNA. Translation: BAA04830.1. AC007887 Genomic DNA. Translation: AAF79386.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE31822.1. AY050981 mRNA. Translation: AAK93658.1. AY113986 mRNA. Translation: AAM45034.1.
IPI	IPI00543334.
PIR	S46284.
RefSeq	NP_174807.1. NM_103271.3.
UniGene	At.24141.
3D structure databases
HSSP	HSSP built from PDB template 1S6J based on UniProtKB P28583.
ProteinModelPortal	Q39016.
SMR	Q39016. Positions 22-488.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q39016. 24 interactions.
MINT	MINT-1788888.
Proteomic databases
PaxDb	Q39016.
PRIDE	Q39016.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G35670.1; AT1G35670.1; AT1G35670.
GeneID	840471.
KEGG	ath:AT1G35670.
Organism-specific databases
TAIR	At1g35670.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233030.
InParanoid	Q39016.
KO	K13412.
OMA	ETEAGIF.
ProtClustDB	CLSN2681779.
Gene expression databases
ArrayExpress	Q39016.
Genevestigator	Q39016.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR011009. Kinase-like_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	PF13499. EF_hand_5. 2 hits. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00054. EFh. 4 hits. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00018. EF_HAND_1. 4 hits. PS50222. EF_HAND_2. 4 hits. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDPKB_ARATH

Accession

Primary (citable) accession number: Q39016
Secondary accession number(s): Q949P0, Q9LQH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	May 3, 2011
Last modified:	May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program