CDPKK_ORYSJ
ID CDPKK_ORYSJ Reviewed; 550 AA.
AC Q84SL0;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Calcium-dependent protein kinase 20 {ECO:0000305};
DE Short=OsCDPK20 {ECO:0000305};
DE Short=OsCPK20 {ECO:0000303|PubMed:15695435};
DE EC=2.7.11.1 {ECO:0000305};
GN Name=CPK20 {ECO:0000303|PubMed:15695435};
GN OrderedLocusNames=Os07g0568600 {ECO:0000312|EMBL:BAF21945.1},
GN LOC_Os07g38120;
GN ORFNames=OJ1092_A07.132 {ECO:0000312|EMBL:BAC83205.1},
GN OsJ_24795 {ECO:0000312|EMBL:EAZ40349.1};
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP INDUCTION BY N-ACETYLCHITOOLIGOSACCHARIDE ELICITOR.
RX PubMed=12956525; DOI=10.1023/a:1024890601888;
RA Akimoto-Tomiyama C., Sakata K., Yazaki J., Nakamura K., Fujii F.,
RA Shimbo K., Yamamoto K., Sasaki T., Kishimoto N., Kikuchi S., Shibuya N.,
RA Minami E.;
RT "Rice gene expression in response to N-acetylchitooligosaccharide elicitor:
RT comprehensive analysis by DNA microarray with randomly selected ESTs.";
RL Plant Mol. Biol. 52:537-551(2003).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
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 [7]
RP INDUCTION BY UV-C.
RX PubMed=24035516; DOI=10.1016/j.phytochem.2013.08.012;
RA Park H.L., Lee S.W., Jung K.H., Hahn T.R., Cho M.H.;
RT "Transcriptomic analysis of UV-treated rice leaves reveals UV-induced
RT phytoalexin biosynthetic pathways and their regulatory networks in rice.";
RL Phytochemistry 96:57-71(2013).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. {ECO:0000250|UniProtKB:Q06850}.
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:0000250|UniProtKB:P53684};
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:0000250|UniProtKB:P53684};
CC -!- ACTIVITY REGULATION: Activated by calcium. Autophosphorylation may play
CC an important role in the regulation of the kinase activity.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaf blades.
CC {ECO:0000269|PubMed:15695435}.
CC -!- INDUCTION: By N-acetylchitooligosaccharide elicitor (PubMed:12956525).
CC Induced by UV-C (PubMed:24035516). {ECO:0000269|PubMed:12956525,
CC ECO:0000269|PubMed:24035516}.
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 (339-369) inactivates kinase
CC activity under calcium-free conditions. {ECO:0000250|UniProtKB:Q06850}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000305}.
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DR EMBL; AP003866; BAC83205.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21945.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT02209.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ40349.1; -; Genomic_DNA.
DR RefSeq; XP_015647618.1; XM_015792132.1.
DR AlphaFoldDB; Q84SL0; -.
DR SMR; Q84SL0; -.
DR STRING; 4530.OS07T0568600-01; -.
DR iPTMnet; Q84SL0; -.
DR PaxDb; Q84SL0; -.
DR PRIDE; Q84SL0; -.
DR EnsemblPlants; Os07t0568600-01; Os07t0568600-01; Os07g0568600.
DR GeneID; 4343644; -.
DR Gramene; Os07t0568600-01; Os07t0568600-01; Os07g0568600.
DR KEGG; osa:4343644; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q84SL0; -.
DR OMA; KMANEEH; -.
DR OrthoDB; 330091at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q84SL0; 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; 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; 1.
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; 1.
DR Pfam; PF13833; EF-hand_8; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Calcium; Kinase; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..550
FT /note="Calcium-dependent protein kinase 20"
FT /id="PRO_0000437563"
FT DOMAIN 75..333
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 376..411
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 412..447
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 448..483
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 484..519
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..369
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q06850"
FT COMPBIAS 14..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 497
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 503
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 508
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:0000255"
SQ SEQUENCE 550 AA; 62408 MW; E8AFF800200E0B55 CRC64;
MGNCCVTPEG SGRGRKKQQQ EQKQKQKEPK QQQQQQKKGK KPNPFSIEYN RSSAPSGHRL
VVLREPTGRD IAARYELGGE LGRGEFGVTY LCTERETGDA YACKSISKKK LRTAVDIEDV
RREVDIMRHL PKHPNIVTLR DTYEDDNAVH LVMELCEGGE LFDRIVARGH YTERAAALVT
RTIVEVVQMC HKHGVMHRDL KPENFLFANK KETAALKAID FGLSVFFTPG ERFTEIVGSP
YYMAPEVLKR NYGPEVDVWS AGVILYILLC GVPPFWAETE QGVAQAIIRS VIDFKRDPWP
RVSDNAKDLV KGMLNPDPRR RLNAQQVLDH PWLQNIKKAP NVNLGETVKA RLQQFSVMNK
FKKHALRVIA EHLSVEEVAG IKDMFEKMDL NKDNMINFDE LKLGLHKLGH QMADADVQIL
MDAADVDGNG SLDYGEFVAL SVHLRKIGND EHLHKAFAYF DRNQSGYIEI DELRESLADD
LGANHEEVIN AIIRDVDTDK DGKISYDEFA AMMKAGTDWR KASRQYSRER FTSLSLKLQK
DGSLQLTTTQ
