CDPK2_ARATH
ID CDPK2_ARATH Reviewed; 646 AA.
AC Q38870;
DT 10-FEB-2009, 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 2;
DE EC=2.7.11.1;
DE AltName: Full=Calmodulin-domain protein kinase CDPK isoform 2;
GN Name=CPK2; OrderedLocusNames=At3g10660; ORFNames=F13M14.5, F18K10.28;
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 [GENOMIC DNA], MYRISTOYLATION AT GLY-2, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLY-2.
RX PubMed=11891256; DOI=10.1104/pp.010770;
RA Lu S.X., Hrabak E.M.;
RT "An Arabidopsis calcium-dependent protein kinase is associated with the
RT endoplasmic reticulum.";
RL Plant Physiol. 128:1008-1021(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH 14-3-3 PROTEINS.
RA Moorhead G., Douglas P., Cotelle V., Harthill J., Morrice N., Meek S.,
RA Deiting U., Stitt M., Scarabel M., Aitken A., MacKintosh C.;
RT "Phosphorylation-dependent interactions between enzymes of plant metabolism
RT and 14-3-3 proteins.";
RL Plant J. 18:1-12(1999).
RN [7]
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 [8]
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 [9]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=12912986; DOI=10.1074/jbc.m307321200;
RA Boisson B., Giglione C., Meinnel T.;
RT "Unexpected protein families including cell defense components feature in
RT the N-myristoylome of a higher eukaryote.";
RL J. Biol. Chem. 278:43418-43429(2003).
RN [10]
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 [11]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=19029837; DOI=10.4161/cc.7.23.7176;
RA Benetka W., Mehlmer N., Maurer-Stroh S., Sammer M., Koranda M.,
RA Neumueller R., Betschinger J., Knoblich J.A., Teige M., Eisenhaber F.;
RT "Experimental testing of predicted myristoylation targets involved in
RT asymmetric cell division and calcium-dependent signalling.";
RL Cell Cycle 7:3709-3719(2008).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger.
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 14-3-3 proteins. {ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11891256}; Lipid-anchor
CC {ECO:0000269|PubMed:11891256}.
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 (450-480) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
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; U31833; AAB03244.1; -; mRNA.
DR EMBL; AF286222; AAG00535.1; -; Genomic_DNA.
DR EMBL; AC011560; AAG51400.1; -; Genomic_DNA.
DR EMBL; AC013428; AAF76372.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74940.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63990.1; -; Genomic_DNA.
DR EMBL; BT046185; ACI49784.1; -; mRNA.
DR RefSeq; NP_001326044.1; NM_001337889.1.
DR RefSeq; NP_187677.1; NM_111902.2.
DR AlphaFoldDB; Q38870; -.
DR SMR; Q38870; -.
DR BioGRID; 5569; 1.
DR STRING; 3702.AT3G10660.1; -.
DR iPTMnet; Q38870; -.
DR PaxDb; Q38870; -.
DR PRIDE; Q38870; -.
DR ProteomicsDB; 241222; -.
DR EnsemblPlants; AT3G10660.1; AT3G10660.1; AT3G10660.
DR EnsemblPlants; AT3G10660.2; AT3G10660.2; AT3G10660.
DR GeneID; 820235; -.
DR Gramene; AT3G10660.1; AT3G10660.1; AT3G10660.
DR Gramene; AT3G10660.2; AT3G10660.2; AT3G10660.
DR KEGG; ath:AT3G10660; -.
DR Araport; AT3G10660; -.
DR TAIR; locus:2075885; AT3G10660.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_1_1; -.
DR InParanoid; Q38870; -.
DR OMA; SHGNAQQ; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q38870; -.
DR PRO; PR:Q38870; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38870; baseline and differential.
DR Genevisible; Q38870; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
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: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:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR CDD; cd00051; EFh; 2.
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; Endoplasmic reticulum; Kinase; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..646
FT /note="Calcium-dependent protein kinase 2"
FT /id="PRO_0000363329"
FT DOMAIN 186..444
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 487..522
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 523..558
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 559..592
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 593..628
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 27..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..480
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 30..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 192..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 504
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 511
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 536
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 576
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 583
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 606
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 608
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 617
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:11891256,
FT ECO:0000269|PubMed:12912986, ECO:0000269|PubMed:19029837"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q06850"
FT MUTAGEN 2
FT /note="G->A: Decreases membrane association by
FT approximately 50%."
FT /evidence="ECO:0000269|PubMed:11891256"
SQ SEQUENCE 646 AA; 72254 MW; AD6AA8282B81729F CRC64;
MGNACVGPNI SGNGFLQTVT AAMWRPRIGA EQASSSSHGN GQVSKEAASE PATDQVQNKP
PEPITMPSSK TNPETKLKPD LEIQPEEKKE KVLAEETKQK VVPEESKQEV PPEESKREVV
VQPESAKPET KSESKPETTK PETTSETKPE TKAEPQKPKH MRRVSSAGLR TESVLQRKTE
NFKEFYSLGR KLGQGQFGTT FLCLEKGTGN EYACKSISKR KLLTDEDVED VRREIQIMHH
LAGHPNVISI KGAYEDVVAV HLVMELCSGG ELFDRIIQRG HYTERKAAEL ARTIVGVLEA
CHSLGVMHRD LKPENFLFVS REEDSLLKTI DFGLSMFFKP DEVFTDVVGS PYYVAPEVLR
KRYGPESDVW SAGVIVYILL SGVPPFWAET EQGIFEQVLH GDLDFSSDPW PSISESAKDL
VRKMLVRDPK RRLTAHQVLC HPWVQIDGVA PDKPLDSAVL SRMKQFSAMN KFKKMALRVI
AESLSEEEIA GLKQMFKMID ADNSGQITFE ELKAGLKRVG ANLKESEILD LMQAADVDNS
GTIDYKEFIA ATLHLNKIER EDHLFAAFSY FDKDESGFIT PDELQQACEE FGVEDARIEE
MMRDVDQDKD GRIDYNEFVA MMQKGSIMGG PVKMGLENSI SISLKH
