CIPK6_ARATH
ID CIPK6_ARATH Reviewed; 441 AA.
AC O65554;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 6;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.14;
DE AltName: Full=SOS2-like protein kinase PKS4;
DE AltName: Full=SOS3-interacting protein 3;
GN Name=CIPK6; Synonyms=PKS4, SIP3, SnRK3.14; OrderedLocusNames=At4g30960;
GN ORFNames=F6I18.130;
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], AND INTERACTION WITH CBL3 AND CBL4.
RC STRAIN=cv. Columbia;
RX PubMed=11115898; DOI=10.1104/pp.124.4.1844;
RA Kim K.-N., Cheong Y.H., Gupta R., Luan S.;
RT "Interaction specificity of Arabidopsis calcineurin B-like calcium sensors
RT and their target kinases.";
RL Plant Physiol. 124:1844-1853(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11402167; DOI=10.2307/3871302;
RA Guo Y., Halfter U., Ishitani M., Zhu J.-K.;
RT "Molecular characterization of functional domains in the protein kinase
RT SOS2 that is required for plant salt tolerance.";
RL Plant Cell 13:1383-1400(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 CBL4.
RX PubMed=10725350; DOI=10.1073/pnas.97.7.3735;
RA Halfter U., Ishitani M., Zhu J.-K.;
RT "The Arabidopsis SOS2 protein kinase physically interacts with and is
RT activated by the calcium-binding protein SOS3.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000).
RN [7]
RP INTERACTION WITH CBL2 AND CBL3.
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 [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH AKT1; CBL1; CBL2; CBL3 AND CBL9.
RX PubMed=17898163; DOI=10.1073/pnas.0707912104;
RA Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G.,
RA Buchanan B.B., Luan S.;
RT "A protein phosphorylation/dephosphorylation network regulates a plant
RT potassium channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007).
RN [10]
RP FUNCTION, INTERACTION WITH CBL4 AND AKT2, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF THR-182, AND AUTOPHOSPHORYLATION.
RX PubMed=21445098; DOI=10.1038/cr.2011.50;
RA Held K., Pascaud F., Eckert C., Gajdanowicz P., Hashimoto K.,
RA Corratge-Faillie C., Offenborn J.N., Lacombe B., Dreyer I., Thibaud J.B.,
RA Kudla J.;
RT "Calcium-dependent modulation and plasma membrane targeting of the AKT2
RT potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase
RT complex.";
RL Cell Res. 21:1116-1130(2011).
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. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by
CC phosphorylation the K(+) conductance and uptake of AKT1. Binds to CBL4
CC to modulate AKT2 activity by promoting a kinase interaction-dependent
CC but phosphorylation-independent translocation of the channel to the
CC plasma membrane. {ECO:0000269|PubMed:17898163,
CC ECO:0000269|PubMed:21445098}.
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: Part of a K(+)-channel calcium-sensing kinase/phosphatase
CC complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a
CC kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a
CC K(+)-channel (AKT1). Interacts with AKT1, AKT2,CBL1, CBL2, CBL3,
CC CBL4/SOS3 and CBL9. {ECO:0000269|PubMed:10725350,
CC ECO:0000269|PubMed:11115898, ECO:0000269|PubMed:11230129,
CC ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:21445098}.
CC -!- INTERACTION:
CC O65554; P25854: CAM4; NbExp=2; IntAct=EBI-537615, EBI-1235664;
CC O65554; O81445: CBL1; NbExp=3; IntAct=EBI-537615, EBI-974530;
CC O65554; Q8LAS7: CBL2; NbExp=3; IntAct=EBI-537615, EBI-485991;
CC O65554; Q8LEM7: CBL3; NbExp=4; IntAct=EBI-537615, EBI-637358;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:21445098}. Note=Targeted to the cell membrane when
CC interacting with CBL4 and ATK2.
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC {ECO:0000269|PubMed:11402167}.
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 -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Delayed development and flowering.
CC {ECO:0000269|PubMed:21445098}.
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; AF285106; AAF86505.1; -; mRNA.
DR EMBL; AF339145; AAK26843.1; -; mRNA.
DR EMBL; AL022198; CAA18197.1; -; Genomic_DNA.
DR EMBL; AL161578; CAB79814.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85835.1; -; Genomic_DNA.
DR EMBL; AF436831; AAL32013.1; -; mRNA.
DR EMBL; AY035046; AAK59551.1; -; mRNA.
DR EMBL; AY051051; AAK93728.1; -; mRNA.
DR PIR; E85362; E85362.
DR RefSeq; NP_194825.1; NM_119244.3.
DR AlphaFoldDB; O65554; -.
DR SMR; O65554; -.
DR BioGRID; 14508; 17.
DR DIP; DIP-34749N; -.
DR IntAct; O65554; 13.
DR STRING; 3702.AT4G30960.1; -.
DR iPTMnet; O65554; -.
DR PaxDb; O65554; -.
DR PRIDE; O65554; -.
DR ProteomicsDB; 246855; -.
DR EnsemblPlants; AT4G30960.1; AT4G30960.1; AT4G30960.
DR GeneID; 829221; -.
DR Gramene; AT4G30960.1; AT4G30960.1; AT4G30960.
DR KEGG; ath:AT4G30960; -.
DR Araport; AT4G30960; -.
DR TAIR; locus:2126749; AT4G30960.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; O65554; -.
DR OMA; KVEMRFA; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; O65554; -.
DR PRO; PR:O65554; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65554; baseline and differential.
DR Genevisible; O65554; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0010540; P:basipetal auxin transport; IMP:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051592; P:response to calcium ion; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
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 ATP-binding; Endoplasmic reticulum; Kinase; Manganese; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..441
FT /note="CBL-interacting serine/threonine-protein kinase 6"
FT /id="PRO_0000337209"
FT DOMAIN 24..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 310..334
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 164..193
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 341..371
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT MUTAGEN 182
FT /note="T->D: Increased activity and autophosphorylation."
FT /evidence="ECO:0000269|PubMed:21445098"
SQ SEQUENCE 441 AA; 49357 MW; 469728C6CB83F428 CRC64;
MVGAKPVENG SDGGSSTGLL HGRYELGRLL GHGTFAKVYH ARNIQTGKSV AMKVVGKEKV
VKVGMVDQIK REISVMRMVK HPNIVELHEV MASKSKIYFA MELVRGGELF AKVAKGRLRE
DVARVYFQQL ISAVDFCHSR GVYHRDLKPE NLLLDEEGNL KVTDFGLSAF TEHLKQDGLL
HTTCGTPAYV APEVILKKGY DGAKADLWSC GVILFVLLAG YLPFQDDNLV NMYRKIYRGD
FKCPGWLSSD ARRLVTKLLD PNPNTRITIE KVMDSPWFKK QATRSRNEPV AATITTTEED
VDFLVHKSKE ETETLNAFHI IALSEGFDLS PLFEEKKKEE KREMRFATSR PASSVISSLE
EAARVGNKFD VRKSESRVRI EGKQNGRKGK LAVEAEIFAV APSFVVVEVK KDHGDTLEYN
NFCSTALRPA LKDIFWTSTP A
