CNBL1_ARATH
ID CNBL1_ARATH Reviewed; 213 AA.
AC O81445; O23603;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Calcineurin B-like protein 1;
DE AltName: Full=SOS3-like calcium-binding protein 5;
GN Name=CBL1; Synonyms=SCABP5; OrderedLocusNames=At4g17615;
GN ORFNames=dl4845w, FCAALL.122;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10200328; DOI=10.1073/pnas.96.8.4718;
RA Kudla J., Xu Q., Harter K., Gruissem W., Luan S.;
RT "Genes for calcineurin B-like proteins in Arabidopsis are differentially
RT regulated by stress signals.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4718-4723(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
RP INTERACTION WITH CIPK1.
RX PubMed=10590166; DOI=10.2307/3870963;
RA Shi J., Kim K.-N., Ritz O., Albrecht V., Gupta R., Harter K., Luan S.,
RA Kudla J.;
RT "Novel protein kinases associated with calcineurin B-like calcium sensors
RT in Arabidopsis.";
RL Plant Cell 11:2393-2405(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CIPK1.
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 [9]
RP INTERACTION WITH CIPK11.
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 [10]
RP INDUCTION.
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 [11]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CIPK15/PKS3.
RX PubMed=12194854; DOI=10.1016/s1534-5807(02)00229-0;
RA Guo Y., Xiong L., Song C.-P., Gong D., Halfter U., Zhu J.-K.;
RT "A calcium sensor and its interacting protein kinase are global regulators
RT of abscisic acid signaling in Arabidopsis.";
RL Dev. Cell 3:233-244(2002).
RN [12]
RP FUNCTION.
RX PubMed=12897256; DOI=10.1105/tpc.012393;
RA Cheong Y.H., Kim K.-N., Pandey G.K., Gupta R., Grant J.J., Luan S.;
RT "CBL1, a calcium sensor that differentially regulates salt, drought, and
RT cold responses in Arabidopsis.";
RL Plant Cell 15:1833-1845(2003).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14617077; DOI=10.1046/j.1365-313x.2003.01892.x;
RA Albrecht V., Weinl S., Blazevic D., D'Angelo C., Batistic O.,
RA Kolukisaoglu U., Bock R., Schulz B., Harter K., Kudla J.;
RT "The calcium sensor CBL1 integrates plant responses to abiotic stresses.";
RL Plant J. 36:457-470(2003).
RN [14]
RP GENE FAMILY, INDUCTION, AND INTERACTION WITH CIPK1; CIPK7; CIPK8; CIPK17;
RP CIPK18 AND CIPK24.
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 [15]
RP FUNCTION, INTERACTION WITH CIPK23, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16814720; DOI=10.1016/j.cell.2006.06.011;
RA Xu J., Li H.-D., Chen L.-Q., Wang Y., Liu L.-L., He L., Wu W.-H.;
RT "A protein kinase, interacting with two calcineurin B-like proteins,
RT regulates K+ transporter AKT1 in Arabidopsis.";
RL Cell 125:1347-1360(2006).
RN [16]
RP INTERACTION WITH PI4KB1.
RX PubMed=16567499; DOI=10.1083/jcb.200508116;
RA Preuss M.L., Schmitz A.J., Thole J.M., Bonner H.K.S., Otegui M.S.,
RA Nielsen E.;
RT "A role for the RabA4b effector protein PI-4Kbeta1 in polarized expansion
RT of root hair cells in Arabidopsis thaliana.";
RL J. Cell Biol. 172:991-998(2006).
RN [17]
RP FUNCTION, INTERACTION WITH CIPK23, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17922773; DOI=10.1111/j.1365-313x.2007.03236.x;
RA Cheong Y.H., Pandey G.K., Grant J.J., Batistic O., Li L., Kim B.-G.,
RA Lee S.-C., Kudla J., Luan S.;
RT "Two calcineurin B-like calcium sensors, interacting with protein kinase
RT CIPK23, regulate leaf transpiration and root potassium uptake in
RT Arabidopsis.";
RL Plant J. 52:223-239(2007).
RN [18]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CIPK24.
RX PubMed=17825054; DOI=10.1111/j.1365-313x.2007.03249.x;
RA Kim B.G., Waadt R., Cheong Y.H., Pandey G.K., Dominguez-Solis J.R.,
RA Schueltke S., Lee S.C., Kudla J., Luan S.;
RT "The calcium sensor CBL10 mediates salt tolerance by regulating ion
RT homeostasis in Arabidopsis.";
RL Plant J. 52:473-484(2007).
RN [19]
RP FUNCTION, AND INTERACTION WITH CIPK6; CIPK16 AND CIPK23.
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 [20]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2 AND CYS-3, MYRISTOYLATION AT
RP GLY-2, STEAROYLATION AT CYS-3, PALMITOYLATION AT CYS-3, AND INTERACTION
RP WITH CIPK1.
RX PubMed=18502848; DOI=10.1105/tpc.108.058123;
RA Batistic O., Sorek N., Schueltke S., Yalovsky S., Kudla J.;
RT "Dual fatty acyl modification determines the localization and plasma
RT membrane targeting of CBL/CIPK Ca2+ signaling complexes in Arabidopsis.";
RL Plant Cell 20:1346-1362(2008).
RN [21]
RP SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH CIPK24.
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 [22]
RP INTERACTION WITH PP2CA.
RX PubMed=21596690; DOI=10.1093/mp/ssr031;
RA Lan W.Z., Lee S.C., Che Y.F., Jiang Y.Q., Luan S.;
RT "Mechanistic analysis of AKT1 regulation by the CBL-CIPK-PP2CA
RT interactions.";
RL Mol. Plant 4:527-536(2011).
RN [23]
RP PHOSPHORYLATION AT SER-201, MUTAGENESIS OF SER-201, AND INTERACTION WITH
RP CIPK23.
RX PubMed=21685179; DOI=10.1104/pp.111.173377;
RA Du W., Lin H., Chen S., Wu Y., Zhang J., Fuglsang A.T., Palmgren M.G.,
RA Wu W., Guo Y.;
RT "Phosphorylation of SOS3-like calcium-binding proteins by their interacting
RT SOS2-like protein kinases is a common regulatory mechanism in
RT Arabidopsis.";
RL Plant Physiol. 156:2235-2243(2011).
RN [24]
RP INTERACTION WITH CIPK7, INDUCTION BY COLD, AND DISRUPTION PHENOTYPE.
RX PubMed=21600398; DOI=10.1016/j.plantsci.2011.03.011;
RA Huang C., Ding S., Zhang H., Du H., An L.;
RT "CIPK7 is involved in cold response by interacting with CBL1 in Arabidopsis
RT thaliana.";
RL Plant Sci. 181:57-64(2011).
RN [25]
RP PHOSPHORYLATION, INTERACTION WITH CIPK24, AND MUTAGENESIS OF SER-201.
RX PubMed=22253446; DOI=10.1074/jbc.m111.279331;
RA Hashimoto K., Eckert C., Anschuetz U., Scholz M., Held K., Waadt R.,
RA Reyer A., Hippler M., Becker D., Kudla J.;
RT "Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by
RT their CBL-interacting protein kinases (CIPKs) is required for full activity
RT of CBL-CIPK complexes toward their target proteins.";
RL J. Biol. Chem. 287:7956-7968(2012).
RN [26]
RP FUNCTION, INTERACTION WITH CIPK26, AND SUBCELLULAR LOCATION.
RX PubMed=23335733; DOI=10.1093/mp/sst009;
RA Drerup M.M., Schluecking K., Hashimoto K., Manishankar P., Steinhorst L.,
RA Kuchitsu K., Kudla J.;
RT "The Calcineurin B-like calcium sensors CBL1 and CBL9 together with their
RT interacting protein kinase CIPK26 regulate the Arabidopsis NADPH oxidase
RT RBOHF.";
RL Mol. Plant 6:559-569(2013).
RN [27]
RP FUNCTION, INDUCTION BY GLUCOSE, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP KINB1.
RC STRAIN=cv. Columbia;
RX PubMed=23437128; DOI=10.1371/journal.pone.0056412;
RA Li Z.Y., Xu Z.S., Chen Y., He G.Y., Yang G.X., Chen M., Li L.C., Ma Y.Z.;
RT "A novel role for Arabidopsis CBL1 in affecting plant responses to glucose
RT and gibberellin during germination and seedling development.";
RL PLoS ONE 8:E56412-E56412(2013).
CC -!- FUNCTION: Acts as a calcium sensor involved in the signaling pathway
CC during growth and development and in response to abiotic stresses. May
CC function as a positive regulator of salt and drought responses and as a
CC negative regulator of cold response. Contributes to the regulation of
CC early stress-related CBF/DREB transcription factors. CBL proteins
CC interact with CIPK serine-threonine protein kinases. Binding of a CBL
CC protein to the regulatory NAF domain of a CIPK protein lead to the
CC activation of the kinase in a calcium-dependent manner. Mediates the
CC activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in
CC response to low potassium conditions and in the context of stomatal
CC movement. Involved in response to glucose and gibberellin during
CC germination and seedling development and in response to cold stress.
CC Involved in the calcium-dependent regulation by CIPK26 of reactive
CC oxygen species production by the NADPH oxidase RBOHF.
CC {ECO:0000269|PubMed:12194854, ECO:0000269|PubMed:12897256,
CC ECO:0000269|PubMed:14617077, ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:17922773,
CC ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:23437128}.
CC -!- SUBUNIT: Homodimer (By similarity). Part of a K(+)-channel calcium-
CC sensing kinase/phosphatase complex composed by a calcium sensor CBL
CC (CBL1, CBL2, CBL3 or CBL9), a kinase CIPK (CIPK6, CIPK16 or CIPK23), a
CC phosphatase PP2C (AIP1) and a K(+)-channel (AKT1). Interacts with
CC PP2CA, CIPK1, CIPK6, CIPK7, CIPK8, CIPK11, CIPK15/PKS3, CIPK16, CIPK17,
CC CIPK18, CIPK23, CIPK24 and CIPK26. Binds to PI4KB1 and to KINB1.
CC {ECO:0000250, ECO:0000269|PubMed:10590166, ECO:0000269|PubMed:11115898,
CC ECO:0000269|PubMed:11230129, ECO:0000269|PubMed:12194854,
CC ECO:0000269|PubMed:14730064, ECO:0000269|PubMed:16567499,
CC ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17825054,
CC ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:17922773,
CC ECO:0000269|PubMed:18502848, ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:21596690, ECO:0000269|PubMed:21600398,
CC ECO:0000269|PubMed:21685179, ECO:0000269|PubMed:22253446,
CC ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:23437128}.
CC -!- INTERACTION:
CC O81445; Q8RWC9: CIPK1; NbExp=10; IntAct=EBI-974530, EBI-1748677;
CC O81445; Q9C562: CIPK10; NbExp=3; IntAct=EBI-974530, EBI-537572;
CC O81445; Q9LYQ8: CIPK2; NbExp=3; IntAct=EBI-974530, EBI-1748707;
CC O81445; Q93VD3: CIPK23; NbExp=6; IntAct=EBI-974530, EBI-974277;
CC O81445; Q9LDI3: CIPK24; NbExp=6; IntAct=EBI-974530, EBI-537551;
CC O81445; Q9LEU7: CIPK5; NbExp=5; IntAct=EBI-974530, EBI-2026322;
CC O81445; O65554: CIPK6; NbExp=3; IntAct=EBI-974530, EBI-537615;
CC O81445; Q9XIW0: CIPK7; NbExp=3; IntAct=EBI-974530, EBI-1765255;
CC O81445; Q9STV4: CIPK8; NbExp=4; IntAct=EBI-974530, EBI-2026454;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:17825054, ECO:0000269|PubMed:17922773,
CC ECO:0000269|PubMed:18502848, ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:23335733}; Lipid-anchor
CC {ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17825054,
CC ECO:0000269|PubMed:17922773, ECO:0000269|PubMed:18502848,
CC ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:23335733}. Note=The
CC cell membrane localization is S-acylation dependent and is abolished by
CC 2-bromopalmitate (2-BP) treatment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O81445-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in stems, roots and
CC siliques. Coexpressed with CIPK15/PKS3 in guard cells. Co-localized
CC with CIPK23 in root tips and vascular bundles in the stem and the leaf,
CC as well as in guard cells. {ECO:0000269|PubMed:10200328,
CC ECO:0000269|PubMed:12194854, ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:17922773}.
CC -!- INDUCTION: By light, drought, salt, cold and wounding. Up-regulated by
CC glucose, but not by sucrose or fructose. {ECO:0000269|PubMed:10200328,
CC ECO:0000269|PubMed:11577192, ECO:0000269|PubMed:14730064,
CC ECO:0000269|PubMed:21600398, ECO:0000269|PubMed:23437128}.
CC -!- DOMAIN: The N-terminal 12 amino acids are sufficient for cell membrane
CC targeting. {ECO:0000269|PubMed:19832944}.
CC -!- PTM: S-acylated at Cys-3 by either palmitate or stearate.
CC Myristoylation is a prerequisite for the subsequent acylation.
CC Myristoylation is important for endoplasmic reticulum targeting and
CC subsequent acylation at the endoplasmic reticulum enables further
CC trafficking to the plasma membrane. Phosphorylated by CIPK23 and
CC CIPK24. {ECO:0000269|PubMed:18502848, ECO:0000269|PubMed:21685179,
CC ECO:0000269|PubMed:22253446}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotypes when grown under normal
CC conditions, but increased sensitivity to low temperature.
CC Hypersensitivity to paclobutrazol and to drought, glucose and salt
CC stresses. {ECO:0000269|PubMed:14617077, ECO:0000269|PubMed:21600398,
CC ECO:0000269|PubMed:23437128}.
CC -!- MISCELLANEOUS: Calcium binding of CBL1 is not required for membrane
CC association and the endoplasmic reticulum-to-plasma membrane
CC trafficking relies on a brefeldin A-insensitive pathway. Lipid
CC modification is not required for interaction between CBL1 and CIPK1
CC (PubMed:18502848). {ECO:0000305|PubMed:18502848}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10542.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g17620 has been split into 3 genes: At4g17615, At4g17616 and At4g17620.; Evidence={ECO:0000305};
CC Sequence=CAB78765.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g17620 has been split into 3 genes: At4g17615, At4g17616 and At4g17620.; Evidence={ECO:0000305};
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DR EMBL; AF076251; AAC26008.1; -; mRNA.
DR EMBL; Z97343; CAB10542.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161546; CAB78765.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83921.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67719.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67720.1; -; Genomic_DNA.
DR EMBL; AK118798; BAC43389.1; -; mRNA.
DR EMBL; BT005567; AAO63987.1; -; mRNA.
DR PIR; A71446; A71446.
DR PIR; T51356; T51356.
DR RefSeq; NP_001329534.1; NM_001341238.1. [O81445-1]
DR RefSeq; NP_001329535.1; NM_001341237.1. [O81445-1]
DR RefSeq; NP_567533.1; NM_117870.4. [O81445-1]
DR AlphaFoldDB; O81445; -.
DR SMR; O81445; -.
DR BioGRID; 12774; 25.
DR DIP; DIP-36763N; -.
DR IntAct; O81445; 19.
DR STRING; 3702.AT4G17615.1; -.
DR iPTMnet; O81445; -.
DR PaxDb; O81445; -.
DR ProteomicsDB; 220477; -. [O81445-1]
DR EnsemblPlants; AT4G17615.1; AT4G17615.1; AT4G17615. [O81445-1]
DR EnsemblPlants; AT4G17615.4; AT4G17615.4; AT4G17615. [O81445-1]
DR EnsemblPlants; AT4G17615.5; AT4G17615.5; AT4G17615. [O81445-1]
DR GeneID; 827481; -.
DR Gramene; AT4G17615.1; AT4G17615.1; AT4G17615. [O81445-1]
DR Gramene; AT4G17615.4; AT4G17615.4; AT4G17615. [O81445-1]
DR Gramene; AT4G17615.5; AT4G17615.5; AT4G17615. [O81445-1]
DR KEGG; ath:AT4G17615; -.
DR Araport; AT4G17615; -.
DR TAIR; locus:2129306; AT4G17615.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR OMA; RGHEDPI; -.
DR PhylomeDB; O81445; -.
DR PRO; PR:O81445; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81445; baseline and differential.
DR Genevisible; O81445; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0019722; P:calcium-mediated signaling; TAS:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR045198; CNBL1-10.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23056; PTHR23056; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Calcium;
KW Cell membrane; Lipoprotein; Membrane; Metal-binding; Myristate; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..213
FT /note="Calcineurin B-like protein 1"
FT /id="PRO_0000073502"
FT DOMAIN 31..66
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 67..102
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 104..139
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 148..183
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 140
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphoserine; by CIPK23"
FT /evidence="ECO:0000269|PubMed:21685179"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:18502848"
FT LIPID 3
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:18502848"
FT LIPID 3
FT /note="S-stearoyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:18502848"
FT MUTAGEN 2
FT /note="G->A: Cytoplasmic and nucleoplasmic distribution and
FT loss of function."
FT /evidence="ECO:0000269|PubMed:18502848"
FT MUTAGEN 3
FT /note="C->S: Endoplasmic reticulum distribution and loss of
FT function."
FT /evidence="ECO:0000269|PubMed:18502848"
FT MUTAGEN 201
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:21685179,
FT ECO:0000269|PubMed:22253446"
FT MUTAGEN 201
FT /note="S->D: Increased interaction with CIPK23."
FT /evidence="ECO:0000269|PubMed:21685179,
FT ECO:0000269|PubMed:22253446"
SQ SEQUENCE 213 AA; 24554 MW; 1C310FC449D027B1 CRC64;
MGCFHSKAAK EFRGHEDPVK LASETAFSVS EVEALFELFK SISSSVVDDG LINKEEFQLA
LFKSRKRENI FANRIFDMFD VKRKGVIDFG DFVRSLNVFH PNASLEDKID FTFRLYDMDC
TGYIERQEVK QMLIALLCES EMKLADETIE IILDKTFEDA DVNQDGKIDK LEWSDFVNKN
PSLLKIMTLP YLRDITTTFP SFVFHSEVDE IAT
