CDPK7_ORYSJ
ID CDPK7_ORYSJ Reviewed; 542 AA.
AC P53684; A0A0P0VSL0; O65003; Q10SB0; Q8GV21; Q8H889; Q8H9A7; Q9SNK9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Calcium-dependent protein kinase 7 {ECO:0000305};
DE Short=OsCDPK7 {ECO:0000305};
DE Short=OsCPK7 {ECO:0000303|PubMed:15695435};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Calcium-dependent protein kinase OsCDPK1 {ECO:0000303|Ref.4};
DE AltName: Full=Calcium-dependent protein kinase OsCDPK13 {ECO:0000303|PubMed:15604699, ECO:0000303|Ref.2};
DE AltName: Full=Calcium-dependent protein kinase isoform 11 {ECO:0000303|PubMed:7766885};
DE Short=OsCPKII {ECO:0000303|PubMed:7766885};
GN Name=CPK7 {ECO:0000303|PubMed:15695435};
GN Synonyms=CDPK1 {ECO:0000303|Ref.4}, CDPK12 {ECO:0000303|Ref.3},
GN CPK11 {ECO:0000303|PubMed:7766885};
GN OrderedLocusNames=Os03g0128700 {ECO:0000312|EMBL:BAF10756.1},
GN LOC_Os03g03660 {ECO:0000312|EMBL:ABF93779.1};
GN ORFNames=OJ1528D07.2 {ECO:0000312|EMBL:AAN17388.1};
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].
RC STRAIN=cv. Arborio; TISSUE=Coleoptile;
RX PubMed=7766885; DOI=10.1007/bf00037023;
RA Breviario D., Morello L., Giani S.;
RT "Molecular cloning of two novel rice cDNA sequences encoding putative
RT calcium-dependent protein kinases.";
RL Plant Mol. Biol. 27:953-967(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX DOI=10.1016/S0981-9428(03)00032-9;
RA Yang G., Shen S., Yang S., Komatsu S.;
RT "OsCDPK13, a calcium-dependent protein kinase gene from rice, is induced in
RT response to cold and gibberellin.";
RL Plant Physiol. Biochem. 41:369-374(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RA Yun C.-H., Park J.-H., Lee G.-R., Seok S.J.;
RT "Nucleotide sequence of rice calcium dependent protein kinase.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Callus;
RA Ho S.-L.;
RT "Molecular cloning and functional analysis of a rice calcium-dependent
RT protein kinase, OsCDPK1.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15604699; DOI=10.1007/s11103-004-1178-y;
RA Abbasi F., Onodera H., Toki S., Tanaka H., Komatsu S.;
RT "OsCDPK13, a calcium-dependent protein kinase gene from rice, is induced by
RT cold and gibberellin in rice leaf sheath.";
RL Plant Mol. Biol. 55:541-552(2004).
RN [10]
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 [11]
RP INDUCTION.
RX PubMed=26681628; DOI=10.1111/plb.12427;
RA Kakar K.U., Ren X.L., Nawaz Z., Cui Z.Q., Li B., Xie G.L., Hassan M.A.,
RA Ali E., Sun G.C.;
RT "A consortium of rhizobacterial strains and biochemical growth elicitors
RT improve cold and drought stress tolerance in rice (Oryza sativa L.).";
RL Plant Biol. 18:471-483(2016).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger (By similarity). May be a signaling
CC component in the response to gibberellin and cold stress
CC (PubMed:15604699). {ECO:0000250|UniProtKB:Q06850,
CC ECO:0000269|PubMed:15604699}.
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:0000305};
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:0000305};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:15604699}.
CC -!- TISSUE SPECIFICITY: Expressed in roots (Ref.2). Expressed in leaf
CC sheaths (Ref.2, PubMed:15604699). {ECO:0000269|PubMed:15604699,
CC ECO:0000269|Ref.2}.
CC -!- INDUCTION: By gibberellin (Ref.2, PubMed:15604699). Induced by cold
CC stress (Ref.2, PubMed:15604699, PubMed:26681628). Down-regulated by
CC brassinosteroid, abscisic acid (ABA), and drought or cold stresses
CC (PubMed:15604699). {ECO:0000269|PubMed:15604699,
CC ECO:0000269|PubMed:26681628, ECO:0000269|Ref.2}.
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 (343-373) inactivates kinase
CC activity under calcium-free conditions. {ECO:0000250|UniProtKB:Q06850}.
CC -!- MISCELLANEOUS: Plants over-expressing CPK7 show increased recovery
CC rates after cold stress. {ECO:0000269|PubMed:15604699}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN17388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X81393; CAA57156.1; -; mRNA.
DR EMBL; AB078634; BAC19839.1; -; mRNA.
DR EMBL; AF048691; AAC05270.1; -; mRNA.
DR EMBL; AY158077; AAN76358.1; -; mRNA.
DR EMBL; AC099739; AAN17388.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP000615; BAA85396.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF93779.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF93780.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF93781.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF10756.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82107.1; -; Genomic_DNA.
DR PIR; S56651; S56651.
DR RefSeq; XP_015631535.1; XM_015776049.1.
DR RefSeq; XP_015631536.1; XM_015776050.1.
DR AlphaFoldDB; P53684; -.
DR SMR; P53684; -.
DR STRING; 4530.OS03T0128700-01; -.
DR PaxDb; P53684; -.
DR PRIDE; P53684; -.
DR EnsemblPlants; Os03t0128700-01; Os03t0128700-01; Os03g0128700.
DR GeneID; 4331490; -.
DR Gramene; Os03t0128700-01; Os03t0128700-01; Os03g0128700.
DR KEGG; osa:4331490; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; P53684; -.
DR OMA; MQGNNVG; -.
DR OrthoDB; 330091at2759; -.
DR BRENDA; 2.7.11.1; 4460.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; P53684; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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: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 GO; GO:0009409; P:response to cold; IMP:UniProtKB.
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; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
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; Cytoplasm; Kinase; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Stress response; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..542
FT /note="Calcium-dependent protein kinase 7"
FT /id="PRO_0000085831"
FT DOMAIN 79..337
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 380..415
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 416..451
FT /note="EF-hand 2; degenerate"
FT /evidence="ECO:0000305"
FT DOMAIN 452..487
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 488..521
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 343..373
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q06850"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 85..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
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 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 510
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"
FT CONFLICT 88
FT /note="G -> A (in Ref. 1; CAA57156)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="L -> P (in Ref. 2; BAC19839)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="L -> W (in Ref. 2; BAC19839)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="K -> E (in Ref. 3; AAC05270)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="I -> M (in Ref. 3; AAC05270)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="Q -> R (in Ref. 3; AAC05270)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="E -> Q (in Ref. 3; AAC05270)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="Q -> P (in Ref. 3; AAC05270)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="G -> R (in Ref. 3; AAC05270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 61153 MW; C72ED59D39094F83 CRC64;
MGNQCQNGTL GSDYHNRFPR EHAVGYVQGD SYLDLKKFDD TWPEVNNFKP TAASILRRGL
DPTSINVLGR KTADLREHYI IGRKLGQGQF GTTYLCTEIN TGCEYACKTI PKRKLITKED
VEDVRREIQI MHHLSGHKNV VAIKDVYEDG QAVHIVMELC AGGELFDRIQ EKGHYSERKA
AELIRIIVSI VAMCHSLGVM HRDLKPENFL LLDKDDDLSI KAIDFGLSVF FKPGQVFTEL
VGSPYYVAPE VLHKRYGPES DVWSAGVILY VLLSGVPPFW AETQQGIFDA VLKGHIDFQS
DPWPKISDSA KDLIRKMLSH CPSERLKAHE VLRHPWICEN GVATDQALDP SVISRLKQFS
AMNKLKKLAL RVIAERLSEE EIAGLREMFK AVDTKNRGVI TFGELREGLR RFGAEFKDTE
IGDIMEAAHN DNNVTIHYEE FIAATLPLNK IEREEHLLAA FTYFDKDGSG YITVDKLQRA
CGEHNMEDSL LEEIISEVDQ NNDGQIDYAE FVAMMQGSNV GLGWQTMESS LNVALRDAPQ
VH
