CCAMK_ORYSJ
ID CCAMK_ORYSJ Reviewed; 516 AA.
AC Q6AVM3; A0A0P0WNT9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase;
DE Short=OsCCaMK;
DE EC=2.7.11.17;
GN Name=CCAMK; Synonyms=DMI3; OrderedLocusNames=Os05g0489900, LOC_Os05g41090;
GN ORFNames=OJ1119_H02.20, OsJ_19014;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
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 IDENTIFICATION, AND FUNCTION.
RX PubMed=16673936; DOI=10.1094/mpmi-19-0495;
RA Godfroy O., Debelle F., Timmers T., Rosenberg C.;
RT "A rice calcium- and calmodulin-dependent protein kinase restores
RT nodulation to a legume mutant.";
RL Mol. Plant Microbe Interact. 19:495-501(2006).
RN [8]
RP IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17965173; DOI=10.1104/pp.107.109876;
RA Chen C., Gao M., Liu J., Zhu H.;
RT "Fungal symbiosis in rice requires an ortholog of a legume common symbiosis
RT gene encoding a Ca2+/calmodulin-dependent protein kinase.";
RL Plant Physiol. 145:1619-1628(2007).
RN [9]
RP FUNCTION.
RX PubMed=18852152; DOI=10.1093/pcp/pcn153;
RA Banba M., Gutjahr C., Miyao A., Hirochika H., Paszkowski U., Kouchi H.,
RA Imaizumi-Anraku H.;
RT "Divergence of evolutionary ways among common sym genes: CASTOR and CCaMK
RT show functional conservation between two symbiosis systems and constitute
RT the root of a common signaling pathway.";
RL Plant Cell Physiol. 49:1659-1671(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=22869603; DOI=10.1093/mp/sss068;
RA Shi B., Ni L., Zhang A., Cao J., Zhang H., Qin T., Tan M., Zhang J.,
RA Jiang M.;
RT "OsDMI3 is a novel component of abscisic acid signaling in the induction of
RT antioxidant defense in leaves of rice.";
RL Mol. Plant 5:1359-1374(2012).
RN [11]
RP FUNCTION.
RX PubMed=23777258; DOI=10.1111/pce.12154;
RA Shi B., Ni L., Liu Y., Zhang A., Tan M., Jiang M.;
RT "OsDMI3-mediated activation of OsMPK1 regulates the activities of
RT antioxidant enzymes in abscisic acid signalling in rice.";
RL Plant Cell Environ. 37:341-352(2014).
CC -!- FUNCTION: Calcium- and calmodulin-dependent protein kinase required for
CC arbuscular mycorrhizal (AM) symbiosis (PubMed:16673936,
CC PubMed:17965173, PubMed:18852152). Involved in response to water
CC deprivation stress. Required for abscisic acid-induced antioxidant
CC defense and oxidative stress tolerance during dehydration stress
CC (PubMed:22869603). Functions upstream of MPK1 in an abscisic acid
CC signaling pathway that regulates the activities of antioxidant enzymes
CC and the production of hydrogen peroxide (PubMed:23777258).
CC {ECO:0000269|PubMed:16673936, ECO:0000269|PubMed:17965173,
CC ECO:0000269|PubMed:18852152, ECO:0000269|PubMed:22869603,
CC ECO:0000269|PubMed:23777258}.
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=2.7.11.17;
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=2.7.11.17;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22869603}. Cytoplasm
CC {ECO:0000269|PubMed:22869603}. Cell membrane
CC {ECO:0000269|PubMed:22869603}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots and panicles. Detected in
CC leaves, shoots and culms. {ECO:0000269|PubMed:17965173}.
CC -!- INDUCTION: Not induced by mycorrhization (PubMed:17965173). Induced by
CC hydrogen peroxide, abscisic acid (ABA) and dehydration
CC (PubMed:22869603). {ECO:0000269|PubMed:17965173,
CC ECO:0000269|PubMed:22869603}.
CC -!- PTM: Autophosphorylation. {ECO:0000250}.
CC -!- MISCELLANEOUS: Can restore mycorrhizal and rhizobial symbiosis and
CC induces spontaneous nodulation in a Ljccamk mutant of Lotus japonicus.
CC Can restore nodulation and mycorrhizal symbiosis to a Medicago
CC truncatula dmi3 mutant.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AC097175; AAT77292.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17809.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS94647.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64182.1; -; Genomic_DNA.
DR EMBL; AK070533; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q6AVM3; -.
DR SMR; Q6AVM3; -.
DR STRING; 4530.OS05T0489900-01; -.
DR PaxDb; Q6AVM3; -.
DR PRIDE; Q6AVM3; -.
DR EnsemblPlants; Os05t0489900-01; Os05t0489900-01; Os05g0489900.
DR Gramene; Os05t0489900-01; Os05t0489900-01; Os05g0489900.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q6AVM3; -.
DR OMA; KQQMIMA; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q6AVM3; OS.
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; IEA:UniProtKB-SubCell.
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:0009877; P:nodulation; IEA:UniProtKB-KW.
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; 2.
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; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
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; Calmodulin-binding; Cell membrane; Coiled coil;
KW Cytoplasm; Kinase; Membrane; Metal-binding; Nodulation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..516
FT /note="Calcium and calcium/calmodulin-dependent
FT serine/threonine-protein kinase"
FT /id="PRO_0000395509"
FT DOMAIN 13..298
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 392..427
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 428..463
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 470..505
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 321..334
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COILED 343..363
FT /evidence="ECO:0000255"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 445
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 487
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 263
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CONFLICT 295
FT /note="H -> R (in Ref. 6; AK070533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 57440 MW; D296EAA8513408A8 CRC64;
MSKTESRKLS DDYEVVDVLG RGGFSIVRRG VSKSEEKTQV AIKTLRRLGP AMAGMKQGTK
PVPGSGLPMW KQVSISDALL TNEILVMRRI VESVAPHPNV INLHDVYEDV HGVHLVLELC
SGGELFDRIV GRDRYSEFDA ACVIRQIASG LEALHKASIV HRDLKPENCL FSDKDEKSTL
KIMDFGLSSV EDFSDPIVAL FGSIDYVSPE ALSRQEVSAA SDMWSVGVIL YILLSGCPPF
HAATNREKQQ RILQGEFSFQ DHTWKTISSS AKDLISRLLS VQPYKRPTAS DLLRHPWVIG
DCAKQDLMDA EVVSKLQKFN ARRKLRAAAI ASVLSCKVAL RTKRLRNLLG THDLTSEELD
NLRLHFGRIC ADGENATLSE FEQVLRAMKM DSLIPLAPRV FDLFDNNRDG TVDMREILCG
FSSLRNSRGD DALRLCFQMY DADRSGCISK EELASMLRAL PEECLPGDIT EPGKLDEVFD
QMDADSDGKV TFDEFKAAMN KDSALQDVLL SSLRPQ
