CNBL3_ARATH
ID CNBL3_ARATH Reviewed; 226 AA.
AC Q8LEM7; O81447;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Calcineurin B-like protein 3;
DE AltName: Full=SOS3-like calcium-binding protein 6;
GN Name=CBL3; Synonyms=SCABP6; OrderedLocusNames=At4g26570;
GN ORFNames=T15N24.20;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
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=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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH CIPK1; CIPK2; CIPK3 AND CIPK6.
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 [7]
RP INTERACTION WITH CIPK1; CIPK2; CIPK4; CIPK6; CIPK7; CIPK11; CIPK12 AND
RP CIPK13.
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.
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 [9]
RP INTERACTION WITH CIPK23.
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 [10]
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 [11]
RP INTERACTION WITH MTN1, AND DOMAIN.
RX PubMed=18945934; DOI=10.1104/pp.108.130419;
RA Oh S.I., Park J., Yoon S., Kim Y., Park S., Ryu M., Nam M.J., Ok S.H.,
RA Kim J.K., Shin J.S., Kim K.N.;
RT "The Arabidopsis calcium sensor calcineurin B-like 3 inhibits the 5'-
RT methylthioadenosine nucleosidase in a calcium-dependent manner.";
RL Plant Physiol. 148:1883-1896(2008).
RN [12]
RP SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH CIPK14.
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 [13]
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 [14]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP CALCIUM-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=23184060; DOI=10.1038/cr.2012.161;
RA Tang R.J., Liu H., Yang Y., Yang L., Gao X.S., Garcia V.J., Luan S.,
RA Zhang H.X.;
RT "Tonoplast calcium sensors CBL2 and CBL3 control plant growth and ion
RT homeostasis through regulating V-ATPase activity in Arabidopsis.";
RL Cell Res. 22:1650-1665(2012).
RN [15]
RP SUBCELLULAR LOCATION, AND PALMITOYLATION.
RX PubMed=23482856; DOI=10.1105/tpc.112.108829;
RA Zhou L.Z., Li S., Feng Q.N., Zhang Y.L., Zhao X., Zeng Y.L., Wang H.,
RA Jiang L., Zhang Y.;
RT "Protein S-acyl transferase10 is critical for development and salt
RT tolerance in Arabidopsis.";
RL Plant Cell 25:1093-1107(2013).
RN [16]
RP FUNCTION, INTERACTION WITH CIPK9, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=23109687; DOI=10.1104/pp.112.206896;
RA Liu L.L., Ren H.M., Chen L.Q., Wang Y., Wu W.H.;
RT "A protein kinase, calcineurin B-like protein-interacting protein Kinase9,
RT interacts with calcium sensor calcineurin B-like Protein3 and regulates
RT potassium homeostasis under low-potassium stress in Arabidopsis.";
RL Plant Physiol. 161:266-277(2013).
RN [17]
RP INTERACTION WITH CIPK14.
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: Acts as a calcium sensor. CBL proteins interact with CIPK
CC serine-threonine protein kinases. Binds calcium ions. 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. Negatively regulates the enzyme activity of MTN1 in the
CC presence of calcium. {ECO:0000269|PubMed:17898163,
CC ECO:0000269|PubMed:23109687}.
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, CIPK2, CIPK3, CIPK4, CIPK6, CIPK7, CIPK11, CIPK12,
CC CIPK13, CIPK14, CIPK16, CIPK23, and MTN1. {ECO:0000250,
CC ECO:0000269|PubMed:10590166, ECO:0000269|PubMed:11230129,
CC ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17898163,
CC ECO:0000269|PubMed:18945934, ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:21596690, ECO:0000269|PubMed:23109687,
CC ECO:0000269|PubMed:25058458}.
CC -!- INTERACTION:
CC Q8LEM7; Q8RWC9: CIPK1; NbExp=4; IntAct=EBI-637358, EBI-1748677;
CC Q8LEM7; O65554: CIPK6; NbExp=4; IntAct=EBI-637358, EBI-537615;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060,
CC ECO:0000269|PubMed:23482856}; Lipid-anchor
CC {ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:23109687,
CC ECO:0000269|PubMed:23184060, ECO:0000269|PubMed:23482856}.
CC Note=Tonoplast localization abolished by 2-bromopalmitate (2-BP)
CC treatment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LEM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LEM7-2; Sequence=VSP_012328;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Stronger expression in roots. Expressed
CC in root tip and root hair zone, leaf veins, vascular bundles and
CC vasculature of sepals. {ECO:0000269|PubMed:10200328,
CC ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060}.
CC -!- DEVELOPMENTAL STAGE: Expressed early during germination and increases
CC to a peak level when seedlings are established.
CC {ECO:0000269|PubMed:23184060}.
CC -!- DOMAIN: The N-terminal 22 amino acids are sufficient for vacuolar
CC membrane targeting. The internal domain (109-199) is sufficient for the
CC interaction with MTN1. {ECO:0000269|PubMed:18945934,
CC ECO:0000269|PubMed:19832944}.
CC -!- PTM: S-acylated by PAT10.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions; due to partial redundancy with CLB2. Tolerant to low-K(+)
CC stress. Clb2 and cbl3 double mutants show stunted growth, reduced
CC fertility and necrotic lesions at leaf tips. They also have a reduced
CC vacuolar H(+)-ATPase activity, are hypersensitive to excessive metal
CC ions and are more tolerant to low-K(+) conditions.
CC {ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; AF076253; AAC26010.1; -; mRNA.
DR EMBL; AL078465; CAB43853.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79512.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85220.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85221.1; -; Genomic_DNA.
DR EMBL; AY072441; AAL62433.1; -; mRNA.
DR EMBL; AY128880; AAM91280.1; -; mRNA.
DR EMBL; AY085344; AAM62575.1; -; mRNA.
DR PIR; T08923; T08923.
DR RefSeq; NP_001320073.1; NM_001341813.1. [Q8LEM7-2]
DR RefSeq; NP_194387.1; NM_118791.4. [Q8LEM7-1]
DR AlphaFoldDB; Q8LEM7; -.
DR SMR; Q8LEM7; -.
DR BioGRID; 14051; 20.
DR DIP; DIP-33307N; -.
DR IntAct; Q8LEM7; 16.
DR STRING; 3702.AT4G26570.2; -.
DR iPTMnet; Q8LEM7; -.
DR SwissPalm; Q8LEM7; -.
DR PaxDb; Q8LEM7; -.
DR PRIDE; Q8LEM7; -.
DR ProteomicsDB; 220284; -. [Q8LEM7-1]
DR EnsemblPlants; AT4G26570.1; AT4G26570.1; AT4G26570. [Q8LEM7-1]
DR EnsemblPlants; AT4G26570.2; AT4G26570.2; AT4G26570. [Q8LEM7-2]
DR GeneID; 828764; -.
DR Gramene; AT4G26570.1; AT4G26570.1; AT4G26570. [Q8LEM7-1]
DR Gramene; AT4G26570.2; AT4G26570.2; AT4G26570. [Q8LEM7-2]
DR KEGG; ath:AT4G26570; -.
DR Araport; AT4G26570; -.
DR TAIR; locus:2133867; AT4G26570.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR InParanoid; Q8LEM7; -.
DR OMA; IHEKLRW; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q8LEM7; -.
DR PRO; PR:Q8LEM7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LEM7; baseline and differential.
DR Genevisible; Q8LEM7; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0005513; P:detection of calcium ion; ISS:TAIR.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:TAIR.
DR InterPro; IPR045198; CNBL1-10.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23056; PTHR23056; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Vacuole.
FT CHAIN 1..226
FT /note="Calcineurin B-like protein 3"
FT /id="PRO_0000073504"
FT DOMAIN 36..81
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 82..117
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 119..154
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 163..198
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 155
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8LAS7"
FT VAR_SEQ 89
FT /note="R -> RYQSQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_012328"
SQ SEQUENCE 226 AA; 26032 MW; F78222E98F64983E CRC64;
MSQCIDGFKH VCSSFFRCFD IDIYKQSGGL GDPELLARET VFSVSEIEAL YELFKKISSA
VIDDGLINKE EFQLALFKTN KKESLFADRV FDLFDTKHNG ILGFEEFARA LSVFHPNAPI
EDKIDFSFQL YDLKQQGFIE RQEVKQMVVA TLAESGMNLS DEIIESIIDK TFEEADTKHD
GRIDKEEWRT LVLRHPSLLK NMTLQYLKDI TTTFPSFVFH SQVEDT
