CIPKO_ORYSJ
ID CIPKO_ORYSJ Reviewed; 453 AA.
AC Q69Q47;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=CBL-interacting protein kinase 24;
DE EC=2.7.11.1;
DE AltName: Full=OsCIPK24;
GN Name=CIPK24; OrderedLocusNames=Os06g0606000, LOC_Os06g40370;
GN ORFNames=P0029C06.1, P0481H08.35;
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 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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14730064; DOI=10.1104/pp.103.033068;
RA Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT "Calcium sensors and their interacting protein kinases: genomics of the
RT Arabidopsis and rice CBL-CIPK signaling networks.";
RL Plant Physiol. 134:43-58(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH CBL4.
RX PubMed=17142477; DOI=10.1104/pp.106.092635;
RA Martinez-Atienza J., Jiang X., Garciadeblas B., Mendoza I., Zhu J.-K.,
RA Pardo J.M., Quintero F.J.;
RT "Conservation of the salt overly sensitive pathway in rice.";
RL Plant Physiol. 143:1001-1012(2007).
RN [7]
RP INDUCTION.
RX PubMed=17535819; DOI=10.1104/pp.107.101295;
RA Xiang Y., Huang Y., Xiong L.;
RT "Characterization of stress-responsive CIPK genes in rice for stress
RT tolerance improvement.";
RL Plant Physiol. 144:1416-1428(2007).
CC -!- FUNCTION: Involved in the regulatory pathway for the control of
CC intracellular Na(+) and K(+) homeostasis and salt tolerance. Operates
CC in synergy with CBL4 to activate the plasma membrane Na(+)/H(+)
CC antiporter SOS1. CIPK serine-threonine protein kinases interact with
CC CBL proteins. Binding of a CBL protein to the regulatory NAF domain of
CC CIPK protein lead to the activation of the kinase in a calcium-
CC dependent manner. {ECO:0000269|PubMed:17142477}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with CBL4. {ECO:0000269|PubMed:17142477}.
CC -!- INDUCTION: By drought stress and abscisic acid (ABA).
CC {ECO:0000269|PubMed:17535819}.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation/activation by upstream protein kinases. The PPI motif
CC mediates the interaction with the ABI (abscisic acid-insensitive)
CC phosphatases (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AP003629; BAD35545.1; -; Genomic_DNA.
DR EMBL; AP005446; BAD36106.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19938.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98528.1; -; Genomic_DNA.
DR EMBL; AK102270; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015643084.1; XM_015787598.1.
DR AlphaFoldDB; Q69Q47; -.
DR SMR; Q69Q47; -.
DR STRING; 4530.OS06T0606000-01; -.
DR PaxDb; Q69Q47; -.
DR PRIDE; Q69Q47; -.
DR EnsemblPlants; Os06t0606000-01; Os06t0606000-01; Os06g0606000.
DR GeneID; 4341477; -.
DR Gramene; Os06t0606000-01; Os06t0606000-01; Os06g0606000.
DR KEGG; osa:4341477; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q69Q47; -.
DR OMA; KFAINTE; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q69Q47; baseline and differential.
DR Genevisible; Q69Q47; OS.
DR GO; GO:0009705; C:plant-type vacuole membrane; IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018451; NAF/FISL_domain.
DR InterPro; IPR004041; NAF_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03822; NAF; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50816; NAF; 1.
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; Kinase; Manganese; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..453
FT /note="CBL-interacting protein kinase 24"
FT /id="PRO_0000338382"
FT DOMAIN 18..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 310..336
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 159..186
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 343..372
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 317
FT /note="M -> V (in Ref. 4; AK102270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 50936 MW; AFC92ABF332D964A CRC64;
MGGEEGMAAG RKKRVGRYEV GRTIGQGTFA KVKFAVDADT GAAVAMKVLD KDTILNHRML
HQIKREISIM KIVRHPNIVR LNEVLAGKTK IYIILELITG GELFDKIARQ GKLRENEARK
YFQQLIDAIN YCHSKGVYHR DLKPENLLLD SRGNLKVSDF GLSTLAQKGV GLLHTTCGTP
NYVAPEVLSN NGYDGSAADV WSCGVILYVL MAGYLPFEED DLPTLYDKIT AGQFSCPYWF
SPGATSLIHR ILDPNPKTRI TIEQIREDTW FKKTYVAIKR GEDENVDLDD VQAVFDNIED
KYVSEQVTHN DGGPLVMNAF EMITLSQGLD LSALFDRQQE FVKRQTRFVS RKPAKTIVAT
IEVVAETMGL KVHSQNYKLR LEGVSSNRMS PFAVVLQVFE VAPSLFMVDV RKVAGDTLEY
HRFYKNLCNK MESIIWRPIE VSAKSALLRT ATC
