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Calcium-dependent protein kinase 7 (OsCDPK7) (OsCPK7) (EC 2.7.11.1) (Calcium-dependent protein kinase OsCDPK1) (Calcium-dependent protein kinase OsCDPK13) (Calcium-dependent protein kinase isoform 11) (OsCPKII)

 CDPK7_ORYSJ             Reviewed;         542 AA.
P53684; A0A0P0VSL0; O65003; Q10SB0; Q8GV21; Q8H889; Q8H9A7; Q9SNK9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-NOV-2005, sequence version 2.
23-MAY-2018, entry version 143.
RecName: Full=Calcium-dependent protein kinase 7 {ECO:0000305};
Short=OsCDPK7 {ECO:0000305};
Short=OsCPK7 {ECO:0000303|PubMed:15695435};
EC=2.7.11.1 {ECO:0000305};
AltName: Full=Calcium-dependent protein kinase OsCDPK1 {ECO:0000303|Ref.4};
AltName: Full=Calcium-dependent protein kinase OsCDPK13 {ECO:0000303|PubMed:15604699, ECO:0000303|Ref.2};
AltName: Full=Calcium-dependent protein kinase isoform 11 {ECO:0000303|PubMed:7766885};
Short=OsCPKII {ECO:0000303|PubMed:7766885};
Name=CPK7 {ECO:0000303|PubMed:15695435};
Synonyms=CDPK1 {ECO:0000303|Ref.4}, CDPK12 {ECO:0000303|Ref.3},
CPK11 {ECO:0000303|PubMed:7766885};
OrderedLocusNames=Os03g0128700 {ECO:0000312|EMBL:BAF10756.1},
LOC_Os03g03660 {ECO:0000312|EMBL:ABF93779.1};
ORFNames=OJ1528D07.2 {ECO:0000312|EMBL:AAN17388.1};
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Arborio; TISSUE=Coleoptile;
PubMed=7766885; DOI=10.1007/BF00037023;
Breviario D., Morello L., Giani S.;
"Molecular cloning of two novel rice cDNA sequences encoding putative
calcium-dependent protein kinases.";
Plant Mol. Biol. 27:953-967(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1016/S0981-9428(03)00032-9;
Yang G., Shen S., Yang S., Komatsu S.;
"OsCDPK13, a calcium-dependent protein kinase gene from rice, is
induced in response to cold and gibberellin.";
Plant Physiol. Biochem. 41:369-374(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Ilpoombyeo;
Yun C.-H., Park J.-H., Lee G.-R., Seok S.J.;
"Nucleotide sequence of rice calcium dependent protein kinase.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Callus;
Ho S.-L.;
"Molecular cloning and functional analysis of a rice calcium-dependent
protein kinase, OsCDPK1.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16109971; DOI=10.1101/gr.3869505;
The rice chromosome 3 sequencing consortium;
Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R.,
Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L.,
Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S.,
Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S.,
Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J.,
de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.,
Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F.,
Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A.,
Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J.,
Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L.,
Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A.,
Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W.,
Lee H.R., Jiang J., Jackson S.;
"Sequence, annotation, and analysis of synteny between rice chromosome
3 and diverged grass species.";
Genome Res. 15:1284-1291(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[7]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[8]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[9]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15604699; DOI=10.1007/s11103-004-1178-y;
Abbasi F., Onodera H., Toki S., Tanaka H., Komatsu S.;
"OsCDPK13, a calcium-dependent protein kinase gene from rice, is
induced by cold and gibberellin in rice leaf sheath.";
Plant Mol. Biol. 55:541-552(2004).
[10]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15695435; DOI=10.1093/pcp/pci035;
Asano T., Tanaka N., Yang G., Hayashi N., Komatsu S.;
"Genome-wide identification of the rice calcium-dependent protein
kinase and its closely related kinase gene families: comprehensive
analysis of the CDPKs gene family in rice.";
Plant Cell Physiol. 46:356-366(2005).
[11]
INDUCTION.
PubMed=26681628; DOI=10.1111/plb.12427;
Kakar K.U., Ren X.L., Nawaz Z., Cui Z.Q., Li B., Xie G.L.,
Hassan M.A., Ali E., Sun G.C.;
"A consortium of rhizobacterial strains and biochemical growth
elicitors improve cold and drought stress tolerance in rice (Oryza
sativa L.).";
Plant Biol. 18:471-483(2016).
-!- FUNCTION: May play a role in signal transduction pathways that
involve calcium as a second messenger (By similarity). May be a
signaling component in the response to gibberellin and cold stress
(PubMed:15604699). {ECO:0000250|UniProtKB:Q06850,
ECO:0000269|PubMed:15604699}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000305}.
-!- ENZYME REGULATION: Activated by calcium. Autophosphorylation may
play an important role in the regulation of the kinase activity.
{ECO:0000250|UniProtKB:Q06850}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:15604699}.
-!- TISSUE SPECIFICITY: Expressed in roots (Ref.2). Expressed in leaf
sheaths (Ref.2, PubMed:15604699). {ECO:0000269|PubMed:15604699,
ECO:0000269|Ref.2}.
-!- INDUCTION: By gibberellin (Ref.2, PubMed:15604699). Induced by
cold stress (Ref.2, PubMed:15604699, PubMed:26681628). Down-
regulated by brassinosteroid, abscisic acid (ABA), and drought or
cold stresses (PubMed:15604699). {ECO:0000269|PubMed:15604699,
ECO:0000269|PubMed:26681628, ECO:0000269|Ref.2}.
-!- DOMAIN: There are 3 contiguous domains conserved in the CDPK
subfamily: a kinase domain, an autoinhibitory (junction) domain
and a calmodulin-like domain. The autoinhibitory domain (343-373)
inactivates kinase activity under calcium-free conditions.
{ECO:0000250|UniProtKB:Q06850}.
-!- MISCELLANEOUS: Plants over-expressing CPK7 show increased recovery
rates after cold stress. {ECO:0000269|PubMed:15604699}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CDPK subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN17388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X81393; CAA57156.1; -; mRNA.
EMBL; AB078634; BAC19839.1; -; mRNA.
EMBL; AF048691; AAC05270.1; -; mRNA.
EMBL; AY158077; AAN76358.1; -; mRNA.
EMBL; AC099739; AAN17388.1; ALT_SEQ; Genomic_DNA.
EMBL; AP000615; BAA85396.1; -; Genomic_DNA.
EMBL; DP000009; ABF93779.1; -; Genomic_DNA.
EMBL; DP000009; ABF93780.1; -; Genomic_DNA.
EMBL; DP000009; ABF93781.1; -; Genomic_DNA.
EMBL; AP008209; BAF10756.1; -; Genomic_DNA.
EMBL; AP014959; BAS82107.1; -; Genomic_DNA.
PIR; S56651; S56651.
RefSeq; XP_015631535.1; XM_015776049.1.
RefSeq; XP_015631536.1; XM_015776050.1.
UniGene; Os.2691; -.
ProteinModelPortal; P53684; -.
SMR; P53684; -.
STRING; 39947.LOC_Os03g03660.1; -.
PaxDb; P53684; -.
EnsemblPlants; Os03t0128700-01; Os03t0128700-01; Os03g0128700.
GeneID; 4331490; -.
Gramene; Os03t0128700-01; Os03t0128700-01; Os03g0128700.
KEGG; osa:4331490; -.
eggNOG; KOG0032; Eukaryota.
eggNOG; ENOG410XRMJ; LUCA.
InParanoid; P53684; -.
KO; K13412; -.
OMA; GNQCPNG; -.
OrthoDB; EOG0936055E; -.
BRENDA; 2.7.11.1; 4460.
Reactome; R-OSA-111932; CaMK IV-mediated phosphorylation of CREB.
Reactome; R-OSA-442745; Activation of CaMK IV.
Reactome; R-OSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-OSA-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-OSA-69473; G2/M DNA damage checkpoint.
Proteomes; UP000059680; Chromosome 3.
ExpressionAtlas; P53684; differential.
Genevisible; P53684; OS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
GO; GO:0009409; P:response to cold; IMP:UniProtKB.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF13499; EF-hand_7; 1.
Pfam; PF13833; EF-hand_8; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00054; EFh; 4.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
ATP-binding; Calcium; Complete proteome; Cytoplasm; Kinase;
Lipoprotein; Membrane; Metal-binding; Myristate; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Stress response; Transferase.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 542 Calcium-dependent protein kinase 7.
/FTId=PRO_0000085831.
DOMAIN 79 337 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 380 415 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 416 451 EF-hand 2; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00448}.
DOMAIN 452 487 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 488 521 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
NP_BIND 85 93 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CA_BIND 393 404 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 429 440 2; atypical.
CA_BIND 465 476 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 499 510 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 343 373 Autoinhibitory domain.
{ECO:0000250|UniProtKB:Q06850}.
ACT_SITE 203 203 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 108 108 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000255}.
CONFLICT 88 88 G -> A (in Ref. 1; CAA57156).
{ECO:0000305}.
CONFLICT 159 159 L -> P (in Ref. 2; BAC19839).
{ECO:0000305}.
CONFLICT 252 252 L -> W (in Ref. 2; BAC19839).
{ECO:0000305}.
CONFLICT 357 357 K -> E (in Ref. 3; AAC05270).
{ECO:0000305}.
CONFLICT 451 451 I -> M (in Ref. 3; AAC05270).
{ECO:0000305}.
CONFLICT 478 478 Q -> R (in Ref. 3; AAC05270).
{ECO:0000305}.
CONFLICT 497 497 E -> Q (in Ref. 3; AAC05270).
{ECO:0000305}.
CONFLICT 516 516 Q -> P (in Ref. 3; AAC05270).
{ECO:0000305}.
CONFLICT 523 523 G -> R (in Ref. 3; AAC05270).
{ECO:0000305}.
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


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