CAMK3_ARATH
ID CAMK3_ARATH Reviewed; 595 AA.
AC Q9ZUZ2; Q56WX8; Q8W107; Q8W562;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=CDPK-related kinase 3;
DE Short=AtCRK3;
DE EC=2.7.11.1;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase 4;
DE Short=AtCK;
GN Name=CRK3; Synonyms=CaMK4, CK; OrderedLocusNames=At2g46700;
GN ORFNames=T3A4.8;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP AUTOPHOSPHORYLATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INDUCTION BY ABSCISIC ACID, ACTIVITY REGULATION, AND
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX AGRICOLA=IND43694487; DOI=10.1016/j.plantsci.2004.12.019;
RA Du W., Wang Y., Liang S., Lu Y.-T.;
RT "Biochemical and expression analysis of an Arabidopsis calcium-dependent
RT protein kinase-related kinase.";
RL Plant Sci. 168:1181-1192(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP REVIEW, AND GENE FAMILY.
RX PubMed=12959135;
RA Harmon A.C.;
RT "Calcium-regulated protein kinases of plants.";
RL Gravit. Space Biol. Bull. 16:83-90(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [8]
RP FUNCTION, INTERACTION WITH GLN1-1, INDUCTION BY LEAF SENESCENCE, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=16472779; DOI=10.1016/j.bbrc.2006.01.100;
RA Li R.-J., Hua W., Lu Y.-T.;
RT "Arabidopsis cytosolic glutamine synthetase AtGLN1;1 is a potential
RT substrate of AtCRK3 involved in leaf senescence.";
RL Biochem. Biophys. Res. Commun. 342:119-126(2006).
RN [9]
RP INTERACTION WITH CALMODULIN, AND AUTOPHOSPHORYLATION.
RX PubMed=17978582; DOI=10.3390/molecules24020276;
RA Jeong J.C., Shin D., Lee J., Kang C.H., Baek D., Cho M.J., Kim M.C.,
RA Yun D.-J.;
RT "Isolation and characterization of a novel calcium/calmodulin-dependent
RT protein kinase, AtCK, from arabidopsis.";
RL Mol. Cells 24:276-282(2007).
RN [10]
RP PHOSPHORYLATION AT SER-353.
RX PubMed=22645532; DOI=10.3389/fpls.2011.00036;
RA Curran A., Chang I.-F., Chang C.-L., Garg S., Miguel R.M., Barron Y.D.,
RA Li Y., Romanowsky S., Cushman J.C., Gribskov M., Harmon A.C., Harper J.F.;
RT "Calcium-dependent protein kinases from Arabidopsis show substrate
RT specificity differences in an analysis of 103 substrates.";
RL Front. Plant Sci. 2:36-36(2011).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger (By similarity). Serine/threonine kinase
CC that phosphorylates histone H3 an GLN1-1. {ECO:0000250,
CC ECO:0000269|PubMed:16472779, ECO:0000269|Ref.1}.
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 Evidence={ECO:0000269|Ref.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; Evidence={ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Not activated by calcium. Autophosphorylation may
CC play an important role in the regulation of the kinase activity.
CC Stimulated by magnesium ions (optimum at 10-15 mM) and manganese ions.
CC {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.4 uM for GLN1-1 (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16472779, ECO:0000269|Ref.1};
CC KM=6.2 uM for histone H3 (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16472779, ECO:0000269|Ref.1};
CC Vmax=35.5 nmol/min/mg enzyme with histone H3 as substrate (at pH 7.5
CC and 30 degrees Celsius) {ECO:0000269|PubMed:16472779,
CC ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:16472779, ECO:0000269|Ref.1};
CC -!- SUBUNIT: Binds calmodulin (CaM) in a calcium-dependent manner.
CC Interacts with GLN1-1. {ECO:0000269|PubMed:16472779,
CC ECO:0000269|PubMed:17978582}.
CC -!- INTERACTION:
CC Q9ZUZ2; Q56WN1: GLN1-1; NbExp=7; IntAct=EBI-1538748, EBI-1538766;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16472779}. Membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZUZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZUZ2-2; Sequence=VSP_044529, VSP_044530;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in
CC siliques and roots, especially at the root cap. Particularly present in
CC vascular bundles of stems and leaves. {ECO:0000269|PubMed:16472779,
CC ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: During flower development, abundantly present in
CC the apical meristem. During pollen development, there are high levels
CC in pollen mother cells and it accumulates gradually to reach a peak
CC during the tetrad stage. Fades out in mature pollen. Also present in
CC tapetal cells and at stigmatic surface of the stigma.
CC {ECO:0000269|Ref.1}.
CC -!- INDUCTION: By abscisic acid (ABA) and during leaf senescence.
CC {ECO:0000269|PubMed:16472779, ECO:0000269|Ref.1}.
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 (409-439) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:22645532}.
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; AF435449; AAL30817.1; -; mRNA.
DR EMBL; AC005819; AAC69927.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10742.1; -; Genomic_DNA.
DR EMBL; AF462819; AAL58909.1; -; mRNA.
DR EMBL; AK221901; BAD94271.1; -; mRNA.
DR PIR; B84906; B84906.
DR RefSeq; NP_182193.1; NM_130235.5. [Q9ZUZ2-1]
DR AlphaFoldDB; Q9ZUZ2; -.
DR SMR; Q9ZUZ2; -.
DR BioGRID; 4617; 4.
DR IntAct; Q9ZUZ2; 1.
DR STRING; 3702.AT2G46700.1; -.
DR iPTMnet; Q9ZUZ2; -.
DR PaxDb; Q9ZUZ2; -.
DR PRIDE; Q9ZUZ2; -.
DR ProteomicsDB; 222798; -. [Q9ZUZ2-1]
DR EnsemblPlants; AT2G46700.1; AT2G46700.1; AT2G46700. [Q9ZUZ2-1]
DR GeneID; 819282; -.
DR Gramene; AT2G46700.1; AT2G46700.1; AT2G46700. [Q9ZUZ2-1]
DR KEGG; ath:AT2G46700; -.
DR Araport; AT2G46700; -.
DR TAIR; locus:2062764; AT2G46700.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_2_1; -.
DR OMA; TMEPLAY; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q9ZUZ2; -.
DR PRO; PR:Q9ZUZ2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUZ2; baseline and differential.
DR Genevisible; Q9ZUZ2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
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:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IEP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
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 Alternative splicing; ATP-binding; Calcium; Cytoplasm; Kinase; Lipoprotein;
KW Magnesium; Manganese; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SG12"
FT CHAIN 2..595
FT /note="CDPK-related kinase 3"
FT /id="PRO_0000420530"
FT DOMAIN 143..405
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 446..482
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 483..518
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 519..558
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 559..588
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..439
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 428..448
FT /note="Calmodulin binding (CaMBD)"
FT COMPBIAS 1..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 149..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 568
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 570
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT MOD_RES 353
FT /note="Phosphoserine; by CPK1 and CPK34"
FT /evidence="ECO:0000269|PubMed:22645532"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_044529"
FT VAR_SEQ 225
FT /note="E -> M (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_044530"
FT CONFLICT 22
FT /note="T -> A (in Ref. 4; AAL58909)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="R -> A (in Ref. 1; AAL30817)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="A -> K (in Ref. 1; AAL30817)"
FT /evidence="ECO:0000305"
FT CONFLICT 476..477
FT /note="MQ -> IE (in Ref. 1; AAL30817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 66600 MW; C6D9C158BA41A39C CRC64;
MGQCYGKVNQ SKQNGEEEAN TTTYVVSGDG NQIQPLTPVN YGRAKNTPAR SSNPSPWPSP
FPHGSASPLP SGVSPSPART STPRRFFRRP FPPPSPAKHI KASLIKRLGV KPKEGPIPEE
RGTEPEQSLD KSFGYGKNFG AKYELGKEVG RGHFGHTCSG RGKKGDIKDH PIAVKIISKA
KMTTAIAIED VRREVKLLKS LSGHKYLIKY YDACEDANNV YIVMELCDGG ELLDRILARG
GKYPEDDAKA IVVQILTVVS FCHLQGVVHR DLKPENFLFT SSREDSDLKL IDFGLSDFIR
PDERLNDIVG SAYYVAPEVL HRSYSLEADI WSIGVITYIL LCGSRPFWAR TESGIFRTVL
RTEPNYDDVP WPSCSSEGKD FVKRLLNKDY RKRMSAVQAL THPWLRDDSR VIPLDILIYK
LVKAYLHATP LRRAALKALA KALTENELVY LRAQFMLLGP NKDGSVSLEN FKTALMQNAT
DAMRESRVPE ILHTMESLAY RKMYFEEFCA AAISIHQLEA VDAWEEIATA GFQHFETEGN
RVITIEELAR ELNVGASAYG HLRDWVRSSD GKLSYLGFTK FLHGVTLRAA HARPR
