CDPKI_ORYSJ
ID CDPKI_ORYSJ Reviewed; 512 AA.
AC Q0D715; Q9SE24;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Calcium-dependent protein kinase 18 {ECO:0000305};
DE Short=OsCDPK18 {ECO:0000305};
DE Short=OsCPK18 {ECO:0000303|PubMed:15695435};
DE EC=2.7.11.1 {ECO:0000269|PubMed:25035404};
DE AltName: Full=OsCDPK5 {ECO:0000303|PubMed:23456295};
GN Name=CPK18 {ECO:0000303|PubMed:15695435};
GN Synonyms=CDPK5 {ECO:0000303|Ref.1};
GN OrderedLocusNames=Os07g0409900 {ECO:0000312|EMBL:BAF21358.1},
GN LOC_Os07g22710 {ECO:0000305};
GN ORFNames=OsJ_23937 {ECO:0000312|EMBL:EEE67015.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheong Y.H., Moon B.C., Cho M.J.;
RT "Isolation of calcium-dependent protein kinases from rice.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15695435; DOI=10.1093/pcp/pci035;
RA Asano T., Tanaka N., Yang G., Hayashi N., Komatsu S.;
RT "Genome-wide identification of the rice calcium-dependent protein kinase
RT and its closely related kinase gene families: comprehensive analysis of the
RT CDPKs gene family in rice.";
RL Plant Cell Physiol. 46:356-366(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY GLOMUS INTRARADICES,
RP MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=21595879; DOI=10.1186/1471-2229-11-90;
RA Campos-Soriano L., Gomez-Ariza J., Bonfante P., San Segundo B.;
RT "A rice calcium-dependent protein kinase is expressed in cortical root
RT cells during the presymbiotic phase of the arbuscular mycorrhizal
RT symbiosis.";
RL BMC Plant Biol. 11:90-90(2011).
RN [9]
RP FUNCTION.
RX PubMed=23456295; DOI=10.1007/s10059-013-2185-0;
RA Kang C.H., Moon B.C., Park H.C., Koo S.C., Chi Y.H., Cheong Y.H.,
RA Yoon B.D., Lee S.Y., Kim C.Y.;
RT "Rice small C2-domain proteins are phosphorylated by calcium-dependent
RT protein kinase.";
RL Mol. Cells 35:381-387(2013).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MPK5, AND MUTAGENESIS OF
RP ASP-178.
RX PubMed=25035404; DOI=10.1105/tpc.114.126441;
RA Xie K., Chen J., Wang Q., Yang Y.;
RT "Direct phosphorylation and activation of a mitogen-activated protein
RT kinase by a calcium-dependent protein kinase in rice.";
RL Plant Cell 26:3077-3089(2014).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger (By similarity). Functions upstream of
CC MPK5 in a signaling pathway that represses defense gene expression and
CC negatively regulates resistance to rice blast fungus. Phosphorylates
CC MPK5 at Thr-14 and Thr-32 and activates MPK5 independently of MAP
CC kinase kinase (MKK) phosphorylation (PubMed:25035404). May be involved
CC in arbuscular mycorrhizal presymbiotic phase signaling
CC (PubMed:21595879). Phosphorylates the elicitor-responsive protein ERG1
CC in vitro. Phosphorylation is calcium-dependent (PubMed:23456295).
CC {ECO:0000250|UniProtKB:Q06850, ECO:0000269|PubMed:21595879,
CC ECO:0000269|PubMed:23456295, ECO:0000269|PubMed:25035404}.
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:25035404};
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:25035404};
CC -!- ACTIVITY REGULATION: Activated by calcium. Autophosphorylation may play
CC an important role in the regulation of the kinase activity.
CC {ECO:0000250|UniProtKB:Q06850}.
CC -!- SUBUNIT: Interacts with MPK5. {ECO:0000269|PubMed:25035404}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21595879};
CC Lipid-anchor {ECO:0000269|PubMed:21595879}.
CC -!- INDUCTION: By the mycorrhizal fungus G.intraradices colonization in
CC roots. {ECO:0000269|PubMed:21595879}.
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 (318-348) inactivates kinase
CC activity under calcium-free conditions. {ECO:0000250|UniProtKB:Q06850}.
CC -!- PTM: Autophosphorylated. Phosphorylated by MPK5.
CC {ECO:0000269|PubMed:25035404}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000305}.
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DR EMBL; AF194414; AAF23901.2; -; mRNA.
DR EMBL; AP008213; BAF21358.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01120.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE67015.1; -; Genomic_DNA.
DR EMBL; AK121471; BAH00509.1; -; mRNA.
DR RefSeq; XP_015647495.1; XM_015792009.1.
DR AlphaFoldDB; Q0D715; -.
DR SMR; Q0D715; -.
DR STRING; 4530.OS07T0409900-01; -.
DR iPTMnet; Q0D715; -.
DR PaxDb; Q0D715; -.
DR PRIDE; Q0D715; -.
DR EnsemblPlants; Os07t0409900-01; Os07t0409900-01; Os07g0409900.
DR GeneID; 4343002; -.
DR Gramene; Os07t0409900-01; Os07t0409900-01; Os07g0409900.
DR KEGG; osa:4343002; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_3_1; -.
DR InParanoid; Q0D715; -.
DR OMA; PEVIDGC; -.
DR OrthoDB; 330091at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q0D715; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0010857; F:calcium-dependent protein kinase activity; IDA:UniProtKB.
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:0050832; P:defense response to fungus; IDA: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; 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; Cell membrane; Kinase; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..512
FT /note="Calcium-dependent protein kinase 18"
FT /id="PRO_0000437562"
FT DOMAIN 52..312
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 355..390
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 392..427
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 434..469
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 472..499
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..348
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q06850"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 58..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 477
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 481
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 488
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:21595879"
FT MUTAGEN 2
FT /note="G->A: Abolishes plasma membrane localization."
FT /evidence="ECO:0000269|PubMed:21595879"
FT MUTAGEN 178
FT /note="D->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25035404"
SQ SEQUENCE 512 AA; 57584 MW; 89E38CEFB9537FF6 CRC64;
MGLCSSSSAR RDAGTPGGGN GAGNKDNAGR KGIVACGKRT DFGYDKDFEA RYALGKLLGH
GQFGYTFAAV DRRSSERVAV KRIDKNKMVL PVAVEDVKRE VKILKALQGH ENVVHFYNAF
EDDNYVYIVM ELCEGGELLD RILAKKDSRY SEKDAAVVVR QMLKVAAECH LHGLVHRDMK
PENFLFKSTK EDSSLKATDF GLSDFIRPGK HFRDIVGSAY YVAPEVLKRK SGPESDVWSI
GVITYILLCG RRPFWDKTED GIFKEVLKNK PDFRRKPWPN ITPCAKDFVQ KLLVKDPRAR
LTAAQALSHE WVREGGQASD IPLDISVLHN MRQFVKYSRF KQFALRALAS TLNAEELSDL
RDQFNAIDVD KNGTISLEEL KQALAKDVPW RLKGPRVLEI VEAIDSNTDG LVDFEEFVAA
TLHVHQLVEH DTEKWKSLSQ AAFDKFDVDG DGYITSDELR MQTGLKGSID PLLEEADIDR
DGKISLDEFR RLLKTASMSS RNVQTPRSVH RS
