(data stored in ACNUC13479 zone)

SWISSPROT: 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   08-MAY-2019, entry version 139.
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;
GN   OrderedLocusNames=At5g01820; ORFNames=T20L15.90;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   Arabidopsis thaliana: differential accumulation of AtSR1 and AtSR2
RT   transcripts in response to cytokinins and sugars, and phosphorylation
RT   of sucrose synthase 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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   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.,
RA   Halford N., Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M.,
RA   Walker-Simmons K., 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
RP   CBL2, AND MUTAGENESIS OF ASN-311; PHE-313; ILE-316; SER-319; PHE-322;
RP   LEU-327; 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
RT   AtCBL2 in 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
RP   CBL2; 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
CC       CIPK protein lead to the activation of the kinase in a calcium-
CC       dependent 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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         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).
CC       Interacts with KIN10 and KIN11 (PubMed:25058458).
CC       {ECO:0000269|PubMed:11577192, ECO:0000269|PubMed:18237745,
CC       ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:25058458}.
CC   -!- INTERACTION:
CC       Q8LAS7:CBL2; NbExp=9; IntAct=EBI-307576, EBI-485991;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19832944,
CC       ECO:0000269|PubMed:25058458}. Nucleus
CC       {ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:25058458}.
CC       Note=Targeted to the tonoplast when interacting with CBL2 or CBL3
CC       and to the cell membrane when interacting with CBL8.
CC   -!- TISSUE SPECIFICITY: Predominant in roots, cauline leaves, and
CC       flowers (PubMed:11577192). Ubiquitous with highest expression in
CC       7-day-old seedlings and flower buds, followed by that in cauline
CC       leaves and young siliques (PubMed:25058458).
CC       {ECO:0000269|PubMed:11577192, ECO:0000269|PubMed:25058458}.
CC   -!- DEVELOPMENTAL STAGE: First observed in imbibed seeds. Mostly
CC       localized in hypocotyls during germination and in seedlings. In
CC       mature plants, confined to vascular tissues of leaves and roots.
CC       In flowers, expressed in the vascular bundle of the stamen
CC       filament and in the stigma, where the filament joins the pistil.
CC       {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
CC       fructose. Induced by several abiotic stresses like salt, cold,
CC       heat, oxidative, drought, PEG8000, glucose treatments as well
CC       exogenous abscisic acid (ABA) application (PubMed:25058458).
CC       {ECO:0000269|PubMed:11212922, ECO:0000269|PubMed:15665497,
CC       ECO:0000269|PubMed:25058458}.
CC   -!- DOMAIN: The activation loop within the kinase domain is the target
CC       of phosphorylation/activation by upstream protein kinases. The PPI
CC       motif mediates the interaction with the ABI (abscisic acid-
CC       insensitive) 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
CC       Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
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   SMR; Q9LZW4; -.
DR   BioGrid; 17041; 49.
DR   IntAct; Q9LZW4; 14.
DR   STRING; 3702.AT5G01820.1; -.
DR   iPTMnet; Q9LZW4; -.
DR   PaxDb; Q9LZW4; -.
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   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000233016; -.
DR   InParanoid; Q9LZW4; -.
DR   OMA; EIAIMHR; -.
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:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; IEA:InterPro.
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;
DR   PRODOM; Q9LZW4.
DR   SWISS-2DPAGE; Q9LZW4.
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Manganese; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    442       CBL-interacting serine/threonine-protein
FT                                kinase 14.
FT                                /FTId=PRO_0000337216.
FT   DOMAIN       22    276       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      305    329       NAF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00256}.
FT   NP_BIND      28     36       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      162    191       Activation loop. {ECO:0000250}.
FT   REGION      335    365       PPI. {ECO:0000250}.
FT   ACT_SITE    144    144       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      51     51       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     166    166       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q93V58}.
FT   MOD_RES     180    180       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q38997}.
FT   MUTAGEN     311    311       N->A: No effect on binding to CBL2.
FT                                {ECO:0000269|PubMed:18237745}.
FT   MUTAGEN     313    313       F->A: Loss of binding to CBL2.
FT                                {ECO:0000269|PubMed:18237745}.
FT   MUTAGEN     316    316       I->A: No effect on binding to CBL2.
FT                                {ECO:0000269|PubMed:18237745}.
FT   MUTAGEN     319    319       S->A,D: No effect on binding to CBL2.
FT                                {ECO:0000269|PubMed:18237745}.
FT   MUTAGEN     322    322       F->A: Loss of binding to CBL2.
FT                                {ECO:0000269|PubMed:18237745}.
FT   MUTAGEN     324    324       L->A: No effect on binding to CBL2.
FT   MUTAGEN     327    327       L->A: No effect on binding to CBL2.
FT                                {ECO:0000269|PubMed:18237745}.
FT   MUTAGEN     328    328       F->A: No effect on binding to CBL2.
FT                                {ECO:0000269|PubMed:18237745}.
FT   MUTAGEN     336    336       R->A: No effect on binding to CBL2.
FT   MUTAGEN     339    339       R->A: No effect on binding to CBL2.
FT                                {ECO:0000269|PubMed:18237745}.
FT   HELIX       312    317       {ECO:0000244|PDB:2ZFD}.
FT   STRAND      322    324       {ECO:0000244|PDB:2ZFD}.
FT   HELIX       325    331       {ECO:0000244|PDB:2ZFD}.
FT   STRAND      338    344       {ECO:0000244|PDB:2ZFD}.
FT   HELIX       346    359       {ECO:0000244|PDB:2ZFD}.
FT   STRAND      363    368       {ECO:0000244|PDB:2ZFD}.
FT   STRAND      371    376       {ECO:0000244|PDB:2ZFD}.
FT   HELIX       377    379       {ECO:0000244|PDB:2ZFD}.
FT   STRAND      381    389       {ECO:0000244|PDB:2ZFD}.
FT   STRAND      391    393       {ECO:0000244|PDB:2ZFD}.
FT   STRAND      395    404       {ECO:0000244|PDB:2ZFD}.
FT   HELIX       412    415       {ECO:0000244|PDB:2ZFD}.
FT   HELIX       417    423       {ECO:0000244|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
//

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