CDPK4_ARATH
ID CDPK4_ARATH Reviewed; 501 AA.
AC Q38869;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Calcium-dependent protein kinase 4;
DE EC=2.7.11.1;
DE AltName: Full=Calmodulin-domain protein kinase CDPK isoform 4;
GN Name=CPK4; OrderedLocusNames=At4g09570; ORFNames=T25P22.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8756605; DOI=10.1007/bf00021802;
RA Hrabak E.M., Dickmann L.J., Satterlee J.S., Sussman M.R.;
RT "Characterization of eight new members of the calmodulin-like domain
RT protein kinase gene family from Arabidopsis thaliana.";
RL Plant Mol. Biol. 31:405-412(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RA Harmon A.C., Gribskov M., Gubrium E., Harper J.F.;
RT "The CDPK superfamily of protein kinases.";
RL New Phytol. 151:175-183(2001).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12068094; DOI=10.1104/pp.005645;
RA Cheng S.-H., Willmann M.R., Chen H.-C., Sheen J.;
RT "Calcium signaling through protein kinases. The Arabidopsis calcium-
RT dependent protein kinase gene family.";
RL Plant Physiol. 129:469-485(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12805596; DOI=10.1104/pp.102.011999;
RA Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N.,
RA Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K.,
RA Zhu J.-K., Harmon A.C.;
RT "The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
RL Plant Physiol. 132:666-680(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12913141; DOI=10.1104/pp.103.020008;
RA Dammann C., Ichida A., Hong B., Romanowsky S.M., Hrabak E.M., Harmon A.C.,
RA Pickard B.G., Harper J.F.;
RT "Subcellular targeting of nine calcium-dependent protein kinase isoforms
RT from Arabidopsis.";
RL Plant Physiol. 132:1840-1848(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH DI19.
RX PubMed=16438971; DOI=10.1016/j.febslet.2006.01.013;
RA Rodriguez Milla M.A., Uno Y., Chang I.-F., Townsend J., Maher E.A.,
RA Quilici D., Cushman J.C.;
RT "A novel yeast two-hybrid approach to identify CDPK substrates:
RT characterization of the interaction between AtCPK11 and AtDi19, a nuclear
RT zinc finger protein.";
RL FEBS Lett. 580:904-911(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17921317; DOI=10.1105/tpc.107.050666;
RA Zhu S.-Y., Yu X.-C., Wang X.-J., Zhao R., Li Y., Fan R.-C., Shang Y.,
RA Du S.-Y., Wang X.-F., Wu F.-Q., Xu Y.-H., Zhang X.-Y., Zhang D.-P.;
RT "Two calcium-dependent protein kinases, CPK4 and CPK11, regulate abscisic
RT acid signal transduction in Arabidopsis.";
RL Plant Cell 19:3019-3036(2007).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. Functions as regulator of the calcium-
CC mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA-
CC responsive transcription factors ABF1 and ABF4 in vitro. Phosphorylates
CC the nuclear zinc finger Di19 in vitro. {ECO:0000269|PubMed:16438971,
CC ECO:0000269|PubMed:17921317}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Activated by calcium. Autophosphorylation may play
CC an important role in the regulation of the kinase activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with Di19. {ECO:0000269|PubMed:16438971}.
CC -!- INTERACTION:
CC Q38869; Q9C593: At5g21940; NbExp=3; IntAct=EBI-979475, EBI-2213247;
CC Q38869; Q94BN0: BT2; NbExp=7; IntAct=EBI-979475, EBI-540986;
CC Q38869; Q39083: DI19-1; NbExp=5; IntAct=EBI-979475, EBI-979339;
CC Q38869; O23338: dl3455w; NbExp=3; IntAct=EBI-979475, EBI-2296482;
CC Q38869; Q9LIS3: GAE6; NbExp=4; IntAct=EBI-979475, EBI-2297116;
CC Q38869; O23680: TOC33; NbExp=5; IntAct=EBI-979475, EBI-639377;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12913141}. Nucleus
CC {ECO:0000269|PubMed:12913141}.
CC -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK subfamily:
CC a kinase domain, an autoinhibitory (junction) domain and a calmodulin-
CC like domain. The autoinhibitory domain (289-319) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant cpk4-1 shows reduced ABA and salt
CC responsiveness in seed germination. {ECO:0000269|PubMed:17921317}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U31752; AAB03243.1; -; mRNA.
DR EMBL; AL161515; CAB78080.1; -; Genomic_DNA.
DR EMBL; AL161831; CAB82124.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82766.1; -; Genomic_DNA.
DR PIR; G85097; G85097.
DR RefSeq; NP_192695.1; NM_117025.6.
DR AlphaFoldDB; Q38869; -.
DR SMR; Q38869; -.
DR BioGRID; 11840; 32.
DR IntAct; Q38869; 34.
DR MINT; Q38869; -.
DR STRING; 3702.AT4G09570.1; -.
DR iPTMnet; Q38869; -.
DR PaxDb; Q38869; -.
DR PRIDE; Q38869; -.
DR ProteomicsDB; 224455; -.
DR EnsemblPlants; AT4G09570.1; AT4G09570.1; AT4G09570.
DR GeneID; 826541; -.
DR Gramene; AT4G09570.1; AT4G09570.1; AT4G09570.
DR KEGG; ath:AT4G09570; -.
DR Araport; AT4G09570; -.
DR TAIR; locus:2136917; AT4G09570.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q38869; -.
DR OMA; HPWIIDE; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q38869; -.
DR PRO; PR:Q38869; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38869; baseline and differential.
DR Genevisible; Q38869; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13499; EF-hand_7; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..501
FT /note="Calcium-dependent protein kinase 4"
FT /id="PRO_0000304510"
FT DOMAIN 25..283
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 326..361
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 362..397
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 398..433
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 437..467
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 289..319
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
SQ SEQUENCE 501 AA; 56416 MW; C709C17DFAF74B70 CRC64;
MEKPNPRRPS NSVLPYETPR LRDHYLLGKK LGQGQFGTTY LCTEKSSSAN YACKSIPKRK
LVCREDYEDV WREIQIMHHL SEHPNVVRIK GTYEDSVFVH IVMEVCEGGE LFDRIVSKGC
FSEREAAKLI KTILGVVEAC HSLGVMHRDL KPENFLFDSP SDDAKLKATD FGLSVFYKPG
QYLYDVVGSP YYVAPEVLKK CYGPEIDVWS AGVILYILLS GVPPFWAETE SGIFRQILQG
KIDFKSDPWP TISEGAKDLI YKMLDRSPKK RISAHEALCH PWIVDEHAAP DKPLDPAVLS
RLKQFSQMNK IKKMALRVIA ERLSEEEIGG LKELFKMIDT DNSGTITFEE LKAGLKRVGS
ELMESEIKSL MDAADIDNSG TIDYGEFLAA TLHINKMERE ENLVVAFSYF DKDGSGYITI
DELQQACTEF GLCDTPLDDM IKEIDLDNDG KIDFSEFTAM MKKGDGVGRS RTMRNNLNFN
IAEAFGVEDT SSTAKSDDSP K
