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Q9ZSA2 (CDPKL_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Calcium-dependent protein kinase 21

EC=2.7.11.1
Gene names
Name:CPK21
Ordered Locus Names:At4g04720
ORF Names:T4B21.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in signal transduction pathways that involve calcium as a second messenger. Mediates the phosphorylation and activation of the S-type anion efflux channel SLAC1. Ref.8

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. Ref.8

Subunit structure

Interacts with SLAC1 and ABI1. Ref.8

Subcellular location

Cell membrane; Lipid-anchor Ref.7.

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 (343-373) inactivates kinase activity under calcium-free conditions By similarity.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 531530Calcium-dependent protein kinase 21
PRO_0000363343

Regions

Domain80 – 338259Protein kinase
Domain380 – 41536EF-hand 1
Domain416 – 45136EF-hand 2
Domain452 – 48736EF-hand 3
Domain488 – 52235EF-hand 4
Nucleotide binding86 – 949ATP By similarity
Calcium binding393 – 404121 By similarity
Calcium binding429 – 440122 By similarity
Calcium binding465 – 476123 By similarity
Calcium binding500 – 511124 By similarity
Region343 – 37331Autoinhibitory domain By similarity

Sites

Active site2041Proton acceptor By similarity
Binding site1091ATP By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Potential

Experimental info

Sequence conflict4681N → S in AAK92828. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9ZSA2 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: D1DCCE1F3386F9D9

FASTA53159,894
        10         20         30         40         50         60 
MGCFSSKHRK TQNDGGEKSI PINPVQTHVV PEHRKPQTPT PKPMTQPIHQ QISTPSSNPV 

        70         80         90        100        110        120 
SVRDPDTILG KPFEDIRKFY SLGKELGRGQ FGITYMCKEI GTGNTYACKS ILKRKLISKQ 

       130        140        150        160        170        180 
DKEDVKREIQ IMQYLSGQPN IVEIKGAYED RQSIHLVMEL CAGGELFDRI IAQGHYSERA 

       190        200        210        220        230        240 
AAGIIRSIVN VVQICHFMGV VHRDLKPENF LLSSKEENAM LKATDFGLSV FIEEGKVYRD 

       250        260        270        280        290        300 
IVGSAYYVAP EVLRRSYGKE IDIWSAGVIL YILLSGVPPF WAENEKGIFD EVIKGEIDFV 

       310        320        330        340        350        360 
SEPWPSISES AKDLVRKMLT KDPKRRITAA QVLEHPWIKG GEAPDKPIDS AVLSRMKQFR 

       370        380        390        400        410        420 
AMNKLKKLAL KVIAESLSEE EIKGLKTMFA NIDTDKSGTI TYEELKTGLT RLGSRLSETE 

       430        440        450        460        470        480 
VKQLMEAADV DGNGTIDYYE FISATMHRYK LDRDEHVYKA FQHFDKDNSG HITRDELESA 

       490        500        510        520        530 
MKEYGMGDEA SIKEVISEVD TDNDGRINFE EFCAMMRSGS TQPQGKLLPF H 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[4]"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.
[5]"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.
[6]"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.
[7]"Subcellular targeting of nine calcium-dependent protein kinase isoforms from Arabidopsis."
Dammann C., Ichida A., Hong B., Romanowsky S.M., Hrabak E.M., Harmon A.C., Pickard B.G., Harper J.F.
Plant Physiol. 132:1840-1848(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Guard cell anion channel SLAC1 is regulated by CDPK protein kinases with distinct Ca2+ affinities."
Geiger D., Scherzer S., Mumm P., Marten I., Ache P., Matschi S., Liese A., Wellmann C., Al-Rasheid K.A.S., Grill E., Romeis T., Hedrich R.
Proc. Natl. Acad. Sci. U.S.A. 107:8023-8028(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SLAC1 AND ABI1, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF118223 Genomic DNA. Translation: AAD03453.1.
AL161501 Genomic DNA. Translation: CAB80837.1.
CP002687 Genomic DNA. Translation: AEE82416.1.
AY050891 mRNA. Translation: AAK92828.1.
AY150502 mRNA. Translation: AAN13018.1.
PIRD85059.
RefSeqNP_192381.1. NM_116710.2.
UniGeneAt.24918.

3D structure databases

ProteinModelPortalQ9ZSA2.
SMRQ9ZSA2. Positions 42-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid11118. 1 interaction.
DIPDIP-59320N.
IntActQ9ZSA2. 1 interaction.

Proteomic databases

PaxDbQ9ZSA2.
PRIDEQ9ZSA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G04720.1; AT4G04720.1; AT4G04720.
GeneID825807.
KEGGath:AT4G04720.

Organism-specific databases

TAIRAT4G04720.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233030.
InParanoidQ9ZSA2.
KOK13412.
OMANDGRINF.
PhylomeDBQ9ZSA2.
ProtClustDBCLSN2685555.

Enzyme and pathway databases

BioCycARA:AT4G04720-MONOMER.

Gene expression databases

GenevestigatorQ9ZSA2.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF13499. EF-hand_7. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00018. 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]
ProtoNetSearch...

Entry information

Entry nameCDPKL_ARATH
AccessionPrimary (citable) accession number: Q9ZSA2
Secondary accession number(s): Q949U0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 112 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names