CAMK1_ARATH
ID CAMK1_ARATH Reviewed; 576 AA.
AC O80673;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=CDPK-related kinase 1;
DE Short=AtCRK1;
DE EC=2.7.11.1;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase 3;
DE AltName: Full=Calmodulin-binding protein kinase 3;
DE Short=AtCBK3;
DE Short=CaM-binding protein kinase 3;
GN Name=CRK1; Synonyms=CaMK3, CBK3; OrderedLocusNames=At2g41140;
GN ORFNames=T3K9.9;
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], FUNCTION, AUTOPHOSPHORYLATION, CATALYTIC
RP ACTIVITY, INTERACTION WITH CALMODULIN, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15196054; DOI=10.1042/bj20031907;
RA Wang Y., Liang S., Xie Q.-G., Lu Y.-T.;
RT "Characterization of a calmodulin-regulated Ca2+-dependent-protein-kinase-
RT related protein kinase, AtCRK1, from Arabidopsis.";
RL Biochem. J. 383:73-81(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RA Choi J.H., Lala H.;
RT "CDPK-related kinases in Arabidopsis.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 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 [6]
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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH HSFA1A.
RX PubMed=18466301; DOI=10.1111/j.1365-313x.2008.03544.x;
RA Liu H.-T., Gao F., Li G.-L., Han J.-L., Liu D.-L., Sun D.-Y., Zhou R.-G.;
RT "The calmodulin-binding protein kinase 3 is part of heat-shock signal
RT transduction in Arabidopsis thaliana.";
RL Plant J. 55:760-773(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP PHOSPHORYLATION AT SER-333.
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. Confers thermotolerance; involved in
CC the heat-shock-mediated calmodulin-dependent signal transduction
CC leading to the activation of heat-shock transcription factors (HSFs);
CC phosphorylates HSFA1A. {ECO:0000250, ECO:0000269|PubMed:15196054,
CC ECO:0000269|PubMed:18466301}.
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|PubMed:15196054};
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|PubMed:15196054};
CC -!- ACTIVITY REGULATION: Activated by calcium and calmodulin.
CC Autophosphorylation may play an important role in the regulation of the
CC kinase activity. {ECO:0000269|PubMed:15196054}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 uM for histone H3 (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC KM=4.4 uM for histone H3 (in the presence of CaM2 at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15196054};
CC KM=4.5 uM for histone H3 (in the presence of CaM4 at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15196054};
CC KM=4.9 uM for histone H3 (in the presence of CaM7 at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15196054};
CC KM=5.3 uM for histone H3 (in the presence of CaM8 at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15196054};
CC KM=5.2 uM for syntide-2 (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC KM=3.8 uM for syntide-2 (in the presence of CaM2 at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15196054};
CC KM=4 uM for syntide-2 (in the presence of CaM4 at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15196054};
CC KM=4.6 uM for syntide-2 (in the presence of CaM7 at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15196054};
CC KM=4.9 uM for syntide-2 (in the presence of CaM8 at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15196054};
CC Vmax=28.3 nmol/min/mg enzyme with histone H3 as substrate (at pH 7.5
CC and 30 degrees Celsius) {ECO:0000269|PubMed:15196054};
CC Vmax=354.4 nmol/min/mg enzyme with histone H3 as substrate (in the
CC presence of CaM2 at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC Vmax=358.5 nmol/min/mg enzyme with histone H3 as substrate (in the
CC presence of CaM4 at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC Vmax=349.2 nmol/min/mg enzyme with histone H3 as substrate (in the
CC presence of CaM7 at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC Vmax=341 nmol/min/mg enzyme with histone H3 as substrate (in the
CC presence of CaM8 at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC Vmax=105.9 nmol/min/mg enzyme with syntide-2 as substrate (at pH 7.5
CC and 30 degrees Celsius) {ECO:0000269|PubMed:15196054};
CC Vmax=768.2 nmol/min/mg enzyme with syntide-2 as substrate (in the
CC presence of CaM2 at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC Vmax=772.3 nmol/min/mg enzyme with syntide-2 as substrate (in the
CC presence of CaM4 at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC Vmax=759.1 nmol/min/mg enzyme with syntide-2 as substrate (in the
CC presence of CaM7 at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC Vmax=751 nmol/min/mg enzyme with syntide-2 as substrate (in the
CC presence of CaM8 at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15196054};
CC -!- SUBUNIT: Binds calmodulin (CaM) in a calcium-dependent manner.
CC Interacts with HSFA1A. {ECO:0000269|PubMed:15196054,
CC ECO:0000269|PubMed:18466301}.
CC -!- INTERACTION:
CC O80673; P41151: HSFA1A; NbExp=3; IntAct=EBI-1804894, EBI-1544927;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
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 (390-420) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:22645532}.
CC -!- DISRUPTION PHENOTYPE: Impaired basal thermotolerance.
CC {ECO:0000269|PubMed:18466301}.
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; AF435448; AAL30816.1; -; mRNA.
DR EMBL; AF153351; AAD38058.1; -; mRNA.
DR EMBL; AC004261; AAD12016.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09936.1; -; Genomic_DNA.
DR PIR; T02105; T02105.
DR RefSeq; NP_181647.1; NM_129679.2.
DR AlphaFoldDB; O80673; -.
DR SMR; O80673; -.
DR BioGRID; 4050; 2.
DR IntAct; O80673; 1.
DR STRING; 3702.AT2G41140.1; -.
DR iPTMnet; O80673; -.
DR PaxDb; O80673; -.
DR PRIDE; O80673; -.
DR ProteomicsDB; 239192; -.
DR EnsemblPlants; AT2G41140.1; AT2G41140.1; AT2G41140.
DR GeneID; 818713; -.
DR Gramene; AT2G41140.1; AT2G41140.1; AT2G41140.
DR KEGG; ath:AT2G41140; -.
DR Araport; AT2G41140; -.
DR TAIR; locus:2063197; AT2G41140.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_2_1; -.
DR OMA; GKECEIG; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; O80673; -.
DR PRO; PR:O80673; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80673; baseline and differential.
DR Genevisible; O80673; 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: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; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
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; IDA:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; 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; Kinase; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SG12"
FT CHAIN 2..576
FT /note="CDPK-related kinase 1"
FT /id="PRO_0000420528"
FT DOMAIN 123..385
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 427..463
FT /note="EF-hand 1"
FT DOMAIN 464..499
FT /note="EF-hand 2"
FT DOMAIN 500..539
FT /note="EF-hand 3"
FT DOMAIN 542..571
FT /note="EF-hand 4"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..420
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 409..429
FT /note="Calmodulin binding (CaMBD)"
FT COMPBIAS 12..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 129..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 528
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT MOD_RES 333
FT /note="Phosphoserine; by CPK1 and CPK34"
FT /evidence="ECO:0000269|PubMed:22645532"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 576 AA; 64315 MW; 90DCFE905CAC4CA9 CRC64;
MGICHGKPVE QQSKSLPVSG ETNEAPTNSQ PPAKSSGFPF YSPSPVPSLF KSSPSVSSSV
SSTPLRIFKR PFPPPSPAKH IRAFLARRYG SVKPNEVSIP EGKECEIGLD KSFGFSKQFA
SHYEIDGEVG RGHFGYTCSA KGKKGSLKGQ EVAVKVIPKS KMTTAIAIED VSREVKMLRA
LTGHKNLVQF YDAFEDDENV YIVMELCKGG ELLDKILQRG GKYSEDDAKK VMVQILSVVA
YCHLQGVVHR DLKPENFLFS TKDETSPLKA IDFGLSDYVK PDERLNDIVG SAYYVAPEVL
HRTYGTEADM WSIGVIAYIL LCGSRPFWAR TESGIFRAVL KAEPNFEEAP WPSLSPEAVD
FVKRLLNKDY RKRLTAAQAL CHPWLVGSHE LKIPSDMIIY KLVKVYIMST SLRKSALAAL
AKTLTVPQLA YLREQFTLLG PSKNGYISMQ NYKTAILKSS TDAMKDSRVF DFVHMISCLQ
YKKLDFEEFC ASALSVYQLE AMETWEQHAR RAYELFEKDG NRPIMIEELA SELGLGPSVP
VHVVLQDWIR HSDGKLSFLG FVRLLHGVSS RTLQKA
