CIPKE_ARATH
ID CIPKE_ARATH Reviewed; 442 AA.
AC Q9LZW4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 14;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.15;
DE AltName: Full=SOS2-like protein kinase PKS24;
DE AltName: Full=Serine/threonine-protein kinase SR1;
DE Short=AtSR1;
GN Name=CIPK14; Synonyms=PKS24, SnRK3.15, SR1; OrderedLocusNames=At5g01820;
GN ORFNames=T20L15.90;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11230129; DOI=10.1093/emboj/20.5.1051;
RA Albrecht V., Ritz O., Linder S., Harter K., Kudla J.;
RT "The NAF domain defines a novel protein-protein interaction module
RT conserved in Ca(2+)-regulated kinases.";
RL EMBO J. 20:1051-1063(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11212922; DOI=10.1007/s004380000354;
RA Chikano H., Ogawa M., Ikeda Y., Koizumi N., Kusano T., Sano H.;
RT "Two novel genes encoding SNF-1 related protein kinases from Arabidopsis
RT thaliana: differential accumulation of AtSR1 and AtSR2 transcripts in
RT response to cytokinins and sugars, and phosphorylation of sucrose synthase
RT by AtSR2.";
RL Mol. Gen. Genet. 264:674-681(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP INTERACTION WITH CBL2, AND TISSUE SPECIFICITY.
RX PubMed=11577192; DOI=10.1093/pcp/pce126;
RA Nozawa A., Koizumi N., Sano H.;
RT "An Arabidopsis SNF1-related protein kinase, AtSR1, interacts with a
RT calcium-binding protein, AtCBL2, of which transcripts respond to light.";
RL Plant Cell Physiol. 42:976-981(2001).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12805596; DOI=10.1104/pp.102.011999;
RA Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N.,
RA Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K.,
RA Zhu J.-K., Harmon A.C.;
RT "The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
RL Plant Physiol. 132:666-680(2003).
RN [8]
RP INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15665497; DOI=10.1271/bbb.69.242;
RA Lee E.-J., Iai H., Sano H., Koizumi N.;
RT "Sugar responsible and tissue specific expression of a gene encoding
RT AtCIPK14, an Arabidopsis CBL-interacting protein kinase.";
RL Biosci. Biotechnol. Biochem. 69:242-245(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CBL2; CBL3 AND CBL8.
RX PubMed=19832944; DOI=10.1111/j.1365-313x.2009.04045.x;
RA Batistic O., Waadt R., Steinhorst L., Held K., Kudla J.;
RT "CBL-mediated targeting of CIPKs facilitates the decoding of calcium
RT signals emanating from distinct cellular stores.";
RL Plant J. 61:211-222(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 305-427 IN COMPLEX WITH CBL2, AND
RP MUTAGENESIS OF ASN-311; PHE-313; ILE-316; SER-319; PHE-322; LEU-327;
RP PHE-328 AND ARG-339.
RX PubMed=18237745; DOI=10.1016/j.jmb.2008.01.006;
RA Akaboshi M., Hashimoto H., Ishida H., Saijo S., Koizumi N., Sato M.,
RA Shimizu T.;
RT "The crystal structure of plant-specific calcium-binding protein AtCBL2 in
RT complex with the regulatory domain of AtCIPK14.";
RL J. Mol. Biol. 377:246-257(2008).
RN [11]
RP TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBL2;
RP CBL3; CBL9; KIN10 AND KIN11, AND DISRUPTION PHENOTYPE.
RX PubMed=25058458; DOI=10.1016/j.bbrc.2014.07.064;
RA Yan J., Niu F., Liu W.Z., Zhang H., Wang B., Lan W., Che Y., Yang B.,
RA Luan S., Jiang Y.Q.;
RT "Arabidopsis CIPK14 positively regulates glucose response.";
RL Biochem. Biophys. Res. Commun. 450:1679-1683(2014).
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 -!- SUBUNIT: Interacts with CBL2 (PubMed:11577192, PubMed:19832944,
CC PubMed:18237745, PubMed:25058458). Interacts with CBL3
CC (PubMed:19832944, PubMed:25058458). Interacts with CBL8
CC (PubMed:19832944). Interacts with CBL9 (PubMed:25058458). Interacts
CC with KIN10 and KIN11 (PubMed:25058458). {ECO:0000269|PubMed:11577192,
CC ECO:0000269|PubMed:18237745, ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:25058458}.
CC -!- INTERACTION:
CC Q9LZW4; O80575: At2g44050; NbExp=4; IntAct=EBI-307576, EBI-4473692;
CC Q9LZW4; O22873: BZIP18; NbExp=3; IntAct=EBI-307576, EBI-4438646;
CC Q9LZW4; Q8LAS7: CBL2; NbExp=9; IntAct=EBI-307576, EBI-485991;
CC Q9LZW4; Q39204: MYC2; NbExp=5; IntAct=EBI-307576, EBI-1792336;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:25058458}. Nucleus {ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:25058458}. Note=Targeted to the tonoplast when
CC interacting with CBL2 or CBL3 and to the cell membrane when interacting
CC with CBL8.
CC -!- TISSUE SPECIFICITY: Predominant in roots, cauline leaves, and flowers
CC (PubMed:11577192). Ubiquitous with highest expression in 7-day-old
CC seedlings and flower buds, followed by that in cauline leaves and young
CC siliques (PubMed:25058458). {ECO:0000269|PubMed:11577192,
CC ECO:0000269|PubMed:25058458}.
CC -!- DEVELOPMENTAL STAGE: First observed in imbibed seeds. Mostly localized
CC in hypocotyls during germination and in seedlings. In mature plants,
CC confined to vascular tissues of leaves and roots. In flowers, expressed
CC in the vascular bundle of the stamen filament and in the stigma, where
CC the filament joins the pistil. {ECO:0000269|PubMed:15665497}.
CC -!- INDUCTION: By light in a cytokinin-dependent manner and N(6)-
CC benzylaminopurine (BA). Also induced by sucrose, glucose and fructose.
CC Induced by several abiotic stresses like salt, cold, heat, oxidative,
CC drought, PEG8000, glucose treatments as well exogenous abscisic acid
CC (ABA) application (PubMed:25058458). {ECO:0000269|PubMed:11212922,
CC ECO:0000269|PubMed:15665497, ECO:0000269|PubMed:25058458}.
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 -!- DISRUPTION PHENOTYPE: Increased sensitivity to glucose.
CC {ECO:0000269|PubMed:25058458}.
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; AF295669; AAK16689.1; -; mRNA.
DR EMBL; AB035147; BAB11737.1; -; mRNA.
DR EMBL; AL162351; CAB82752.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90397.1; -; Genomic_DNA.
DR EMBL; AF360189; AAK25899.1; -; mRNA.
DR EMBL; AY142684; AAN13222.1; -; mRNA.
DR PIR; T48203; T48203.
DR RefSeq; NP_195802.1; NM_120260.3.
DR PDB; 2ZFD; X-ray; 1.20 A; B=305-427.
DR PDBsum; 2ZFD; -.
DR AlphaFoldDB; Q9LZW4; -.
DR SMR; Q9LZW4; -.
DR BioGRID; 17041; 54.
DR IntAct; Q9LZW4; 16.
DR STRING; 3702.AT5G01820.1; -.
DR iPTMnet; Q9LZW4; -.
DR PaxDb; Q9LZW4; -.
DR PRIDE; Q9LZW4; -.
DR ProteomicsDB; 246799; -.
DR DNASU; 831765; -.
DR EnsemblPlants; AT5G01820.1; AT5G01820.1; AT5G01820.
DR GeneID; 831765; -.
DR Gramene; AT5G01820.1; AT5G01820.1; AT5G01820.
DR KEGG; ath:AT5G01820; -.
DR Araport; AT5G01820; -.
DR TAIR; locus:2181057; AT5G01820.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9LZW4; -.
DR OMA; VMIEVRK; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9LZW4; -.
DR EvolutionaryTrace; Q9LZW4; -.
DR PRO; PR:Q9LZW4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZW4; baseline and differential.
DR Genevisible; Q9LZW4; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
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:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 3D-structure; ATP-binding; Cytoplasm; Kinase; Manganese;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..442
FT /note="CBL-interacting serine/threonine-protein kinase 14"
FT /id="PRO_0000337216"
FT DOMAIN 22..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 305..329
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 162..191
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 335..365
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT MUTAGEN 311
FT /note="N->A: No effect on binding to CBL2."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 313
FT /note="F->A: Loss of binding to CBL2."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 316
FT /note="I->A: No effect on binding to CBL2."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 319
FT /note="S->A,D: No effect on binding to CBL2."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 322
FT /note="F->A: Loss of binding to CBL2."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 324
FT /note="L->A: No effect on binding to CBL2."
FT MUTAGEN 327
FT /note="L->A: No effect on binding to CBL2."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 328
FT /note="F->A: No effect on binding to CBL2."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 336
FT /note="R->A: No effect on binding to CBL2."
FT MUTAGEN 339
FT /note="R->A: No effect on binding to CBL2."
FT /evidence="ECO:0000269|PubMed:18237745"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 346..359
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 395..404
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 417..423
FT /evidence="ECO:0007829|PDB:2ZFD"
SQ SEQUENCE 442 AA; 50298 MW; 319532FEFB7244C8 CRC64;
MVDSDPVEFP PENRRGQLFG KYEVGKLVGC GAFAKVYHGR STATGQSVAI KVVSKQRLQK
GGLNGNIQRE IAIMHRLRHP SIVRLFEVLA TKSKIFFVME FAKGGELFAK VSKGRFCEDL
SRRYFQQLIS AVGYCHSRGI FHRDLKPENL LLDEKLDLKI SDFGLSALTD QIRPDGLLHT
LCGTPAYVAP EVLAKKGYDG AKIDIWSCGI ILFVLNAGYL PFNDHNLMVM YRKIYKGEFR
IPKWTSPDLR RLLTRLLDTN PQTRITIEEI IHDPWFKQGY DDRMSKFHLE DSDMKLPADE
TDSEMGARRM NAFDIISGSP GFNLSGLFGD ARKYDRVERF VSAWTAERVV ERLEEIVSAE
NLTVAKKETW GMKIEGQKGN FAMVVEINQL TDELVMIEVR KRQRAAASGR DLWTDTLRPF
FVELVHESDQ TDPEPTQVHT TS
