CIPKF_ORYSJ
ID CIPKF_ORYSJ Reviewed; 434 AA.
AC Q2RBF0; A0A0P0XY79;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=CBL-interacting protein kinase 15;
DE EC=2.7.11.1;
DE AltName: Full=OsCIPK15;
GN Name=CIPK15; OrderedLocusNames=Os11g0113700, LOC_Os11g02240;
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. Nipponbare;
RA Kurusu T., Hamada J., Kuchitsu K.;
RT "Oryza sativa (japonica cultivar-group) CBL-interacting protein kinase
RT mRNA.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, AND 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 salt stress tolerance. CIPK serine-threonine
CC protein kinases interact with CBL proteins. Binding of a CBL protein to
CC the regulatory NAF domain of CIPK protein lead to the activation of the
CC kinase in a calcium-dependent manner. {ECO:0000269|PubMed:17535819}.
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 -!- INDUCTION: By drought and salt stresses 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; AB264037; BAF34613.1; -; mRNA.
DR EMBL; DP000010; ABA91173.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF27419.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT12391.1; -; Genomic_DNA.
DR RefSeq; XP_015617455.1; XM_015761969.1.
DR AlphaFoldDB; Q2RBF0; -.
DR SMR; Q2RBF0; -.
DR STRING; 4530.OS11T0113700-01; -.
DR PaxDb; Q2RBF0; -.
DR PRIDE; Q2RBF0; -.
DR EnsemblPlants; Os11t0113700-01; Os11t0113700-01; Os11g0113700.
DR EnsemblPlants; Os11t0113700-02; Os11t0113700-02; Os11g0113700.
DR GeneID; 4349594; -.
DR Gramene; Os11t0113700-01; Os11t0113700-01; Os11g0113700.
DR Gramene; Os11t0113700-02; Os11t0113700-02; Os11g0113700.
DR KEGG; osa:4349594; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q2RBF0; -.
DR OMA; KSASTIX; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR Genevisible; Q2RBF0; OS.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR028375; KA1/Ssp2_C.
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; SSF103243; SSF103243; 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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Manganese; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..434
FT /note="CBL-interacting protein kinase 15"
FT /id="PRO_0000338373"
FT DOMAIN 12..267
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 298..333
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 153..182
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 338..367
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 434 AA; 49698 MW; 1EB615196F262147 CRC64;
MESRGKILME RYELGRLLGK GTFGKVHYAR NLESNQSVAI KMMDKQQILK VGLSEQIRRE
ITTMRLVAHK NIVQLHEVMA TRNKIYFVME YVKGGELFEK VAKRGKLTEV VAHKYFQQLI
SAVDYCHSRG VYHRDLKPEN LLLDENENLK VSDFGLSALS ESKRQDGLLH TTCGTPAYVA
PEVISKIGYD GAKSDIWSCG VILFVLVAGY LPFQGPNLME MYRKIQHGEF RCPGWFSRKL
QKLLYKIMDP NPSTRISIQK IKESTWFRKG PEENRILKER TLNENTTKNV APVLGVRRKK
NAHEDVKPMS VTNLNAFEII SFSKGFDLSG MFIVKEWRNE ARFTSDKSAS TIISKLEDVA
KALNLRVRKK DNGVVKMQGR KEGRNGVLQF DIEIFEVTTS YHIIEMKQTS GDSLEYRQLL
EEGIRPALKD IVLA
