CIPKE_ORYSJ
ID CIPKE_ORYSJ Reviewed; 439 AA.
AC Q2QYM3; A0A0P0Y685; B7F9N0; O24180;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=CBL-interacting protein kinase 14;
DE EC=2.7.11.1;
DE AltName: Full=OsCIPK14;
GN Name=CIPK14; OrderedLocusNames=Os12g0113500, LOC_Os12g02200;
GN ORFNames=OsJ_031406;
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. Ilpoombyeo; TISSUE=Seedling;
RA Yun C.-H., Lee J.S., Lee M.C., Yun K.J., Park Y.J., Eun M.Y.;
RT "Nucleotide sequence of a novel protein kinase in rice.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
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).
CC -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL
CC proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK
CC protein lead to the activation of the kinase in a calcium-dependent
CC manner (By similarity). {ECO:0000250}.
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62693.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAF28996.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF004947; AAB62693.1; ALT_FRAME; mRNA.
DR EMBL; AB264036; BAF34612.1; -; mRNA.
DR EMBL; DP000011; ABA96272.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF28996.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014968; BAT15582.1; -; Genomic_DNA.
DR EMBL; CM000148; EAZ17197.1; -; Genomic_DNA.
DR EMBL; AK242733; BAH01328.1; -; mRNA.
DR EMBL; AK243050; BAH01425.1; -; mRNA.
DR PIR; T03444; T03444.
DR RefSeq; XP_015620143.1; XM_015764657.1.
DR AlphaFoldDB; Q2QYM3; -.
DR SMR; Q2QYM3; -.
DR STRING; 4530.OS12T0113500-01; -.
DR PaxDb; Q2QYM3; -.
DR PRIDE; Q2QYM3; -.
DR EnsemblPlants; Os12t0113500-01; Os12t0113500-01; Os12g0113500.
DR EnsemblPlants; Os12t0113500-02; Os12t0113500-02; Os12g0113500.
DR GeneID; 4351307; -.
DR Gramene; Os12t0113500-01; Os12t0113500-01; Os12g0113500.
DR Gramene; Os12t0113500-02; Os12t0113500-02; Os12g0113500.
DR KEGG; osa:4351307; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q2QYM3; -.
DR OMA; GHENVMD; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QYM3; 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..439
FT /note="CBL-interacting protein kinase 14"
FT /id="PRO_0000338372"
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"
FT CONFLICT 4
FT /note="R -> K (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="R -> K (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="R -> G (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="V -> F (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="A -> G (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="K -> N (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="TT -> PP (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="R -> P (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="D -> N (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="E -> K (in Ref. 1; AAB62693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 50324 MW; 9A6E95E5B9712A68 CRC64;
MESRGKILME RYELGRLLGK GTFGKVHYAR NLESNQSVAI KMMDKQQVLK VGLSEQIRRE
ITTMRLVAHK NIVQLHEVMA TRNKIYFVME YVKGGELFEK VAKRGKLTEV VAHKYFQQLI
SAVDYCHSRG VYHRDLKPEN LLLDENENLK VSDFGLSALS ESKRQDGLLH TTCGTPAYVA
PEVISKIGYD GAKSDIWSCG VILFVLVAGY LPFQGPNLME MYRKIQHGEF RCPGWFSRKL
QKLLYKIMDP NPSTRISIQK IKESTWFRKG PEENRILKER TLNENTTKNV ALVLGVRRKK
NAHEDVKPMS VTNLNAFEII SFSKGFDLSG MFIVKEWRNE ARFTSDKSAS TIISKLEDVA
KALNLRVRKK DNGVVKMQGR KEGRNGVLQF DIEIFEVTTS YHIIEMKQTS GDSLEYRQLL
EEGIRPALKD IVLAWHGDE
