CNBL2_ARATH
ID CNBL2_ARATH Reviewed; 226 AA.
AC Q8LAS7; O81446;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Calcineurin B-like protein 2;
DE AltName: Full=SOS3-like calcium-binding protein 1;
GN Name=CBL2; Synonyms=SCABP1; OrderedLocusNames=At5g55990; ORFNames=MDA7.3;
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 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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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].
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].
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; CIPK4; CIPK6; CIPK7; CIPK9; CIPK11; CIPK12
RP AND 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 [7]
RP INDUCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CIPK14.
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 [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, INTERACTION WITH CIPK11, AND CALCIUM-BINDING.
RX PubMed=17483306; DOI=10.1105/tpc.105.035626;
RA Fuglsang A.T., Guo Y., Cuin T.A., Qiu Q., Song C., Kristiansen K.A.,
RA Bych K., Schulz A., Shabala S., Schumaker K.S., Palmgren M.G., Zhu J.K.;
RT "Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by
RT preventing interaction with 14-3-3 protein.";
RL Plant Cell 19:1617-1634(2007).
RN [11]
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 [12]
RP SUBCELLULAR LOCATION.
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 [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CIPK14 AND 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 [14]
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 [15]
RP PHOSPHORYLATION AT SER-216, MUTAGENESIS OF SER-216, AND INTERACTION WITH
RP CIPK11 AND CIPK14.
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 [16]
RP FUNCTION, MUTAGENESIS OF GLN-3; CYS-4; CYS-12 AND CYS-18, PALMITOYLATION AT
RP CYS-4; CYS-12 AND CYS-18, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22547024; DOI=10.1038/cr.2012.71;
RA Batistic O., Rehers M., Akerman A., Schluecking K., Steinhorst L.,
RA Yalovsky S., Kudla J.;
RT "S-acylation-dependent association of the calcium sensor CBL2 with the
RT vacuolar membrane is essential for proper abscisic acid responses.";
RL Cell Res. 22:1155-1168(2012).
RN [17]
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 [18]
RP SUBCELLULAR LOCATION, AND S-ACYLATION.
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 [19]
RP INTERACTION WITH CIPK9, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP 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 [20]
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).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-220 IN COMPLEX WITH CALCIUM.
RX PubMed=12871972; DOI=10.1074/jbc.m303630200;
RA Nagae M., Nozawa A., Koizumi N., Sano H., Hashimoto H., Sato M.,
RA Shimizu T.;
RT "The crystal structure of the novel calcium-binding protein AtCBL2 from
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 278:42240-42246(2003).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH THE REGULATORY
RP DOMAIN OF CIPK14 AND CALCIUM, AND MUTAGENESIS OF GLU-71; GLU-106; GLU-143
RP AND GLU-187.
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).
CC -!- FUNCTION: Acts as a calcium sensor. CBL proteins interact with CIPK
CC serine-threonine protein kinases. Binding of a CBL protein to the
CC regulatory NAF domain of a CIPK protein lead to the activation of the
CC kinase in a calcium-dependent manner. Binds four calcium ions per
CC subunit. Mediates the activation of AKT1 by CIPK proteins (CIPK6,
CC CIPK16, and CIPK23) in response to low potassium conditions and in the
CC context of stomatal movement. Mediates the inactivation of the proton
CC pump AHA2 by CIPK11. Probably involved in regulating signaling
CC responses to abscisic acid. {ECO:0000269|PubMed:17483306,
CC ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:22547024}.
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, CIPK4, CIPK6, CIPK7, CIPK9, CIPK11, CIPK12,
CC CIPK13, CIPK14/SR1, CIPK16, CIPK23, and CIPK24. {ECO:0000250,
CC ECO:0000269|PubMed:11230129, ECO:0000269|PubMed:11577192,
CC ECO:0000269|PubMed:12871972, ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:17483306, ECO:0000269|PubMed:17898163,
CC ECO:0000269|PubMed:18237745, ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:21596690, ECO:0000269|PubMed:21685179,
CC ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:25058458}.
CC -!- INTERACTION:
CC Q8LAS7; Q8RWC9: CIPK1; NbExp=4; IntAct=EBI-485991, EBI-1748677;
CC Q8LAS7; O22932: CIPK11; NbExp=5; IntAct=EBI-485991, EBI-537638;
CC Q8LAS7; Q9SN43: CIPK12; NbExp=4; IntAct=EBI-485991, EBI-637523;
CC Q8LAS7; O22971: CIPK13; NbExp=4; IntAct=EBI-485991, EBI-637402;
CC Q8LAS7; Q9LZW4: CIPK14; NbExp=9; IntAct=EBI-485991, EBI-307576;
CC Q8LAS7; O65554: CIPK6; NbExp=3; IntAct=EBI-485991, EBI-537615;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:18502848,
CC ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:22547024,
CC ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060,
CC ECO:0000269|PubMed:23482856}; Lipid-anchor
CC {ECO:0000269|PubMed:18502848, ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:22547024, ECO:0000269|PubMed:23109687,
CC ECO:0000269|PubMed:23184060, ECO:0000269|PubMed:23482856}. Note=The
CC tonoplast localization is S-acylation dependent and is abolished by 2-
CC bromopalmitate (2-BP) treatment.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Stronger expression in aerial parts.
CC Expressed in guard cells, meristems and elongation zones of roots,
CC mesophyll cells of leaves, cortex and pith of inflorescence stems and
CC anthers and stamen filaments in flowers. {ECO:0000269|PubMed:10200328,
CC ECO:0000269|PubMed:11577192, ECO:0000269|PubMed:23109687,
CC 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 -!- INDUCTION: By light. {ECO:0000269|PubMed:11577192}.
CC -!- DOMAIN: EF-hands 1 and 4 have been shown to bind calcium. It is not
CC known if EF-hands 2 and 3 are capable of calcium-binding. The N-
CC terminal 22 amino acids are necessary and sufficient for vacuolar
CC membrane targeting. {ECO:0000269|PubMed:22547024}.
CC -!- PTM: S-acylated in vivo by PAT10. The ratio of acylation by either
CC palmitate or stearate between Cys-4, Cys-12 and Cys-18 is unknown.
CC {ECO:0000269|PubMed:22547024}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions; due to partial redundancy with CLB3. Chlorotic symptoms
CC under low-K(+) stress. Clb2 and cbl3 double mutants show stunted
CC growth, reduced fertility and necrotic lesions at leaf tips. They have
CC also a reduced vacuolar H(+)-ATPase activity, are hypersensitive to
CC excessive metal ions and are more tolerant to low-K(+) conditions.
CC {ECO:0000269|PubMed:22547024, ECO:0000269|PubMed:23109687,
CC ECO:0000269|PubMed:23184060}.
CC -!- MISCELLANEOUS: Blockage of vesicle trafficking by Brefeldin-A does not
CC affect S-acylation and vacuolar membrane targeting of CBL2.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; AF076252; AAC26009.1; -; mRNA.
DR EMBL; AB011476; BAB09281.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96707.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71100.1; -; Genomic_DNA.
DR EMBL; AY052304; AAK96497.1; -; mRNA.
DR EMBL; AY139808; AAM98114.1; -; mRNA.
DR EMBL; AY087638; AAM65177.1; -; mRNA.
DR PIR; T51357; T51357.
DR RefSeq; NP_001332655.1; NM_001345176.1.
DR RefSeq; NP_200410.1; NM_124981.4.
DR PDB; 1UHN; X-ray; 2.10 A; A=32-220.
DR PDB; 2ZFD; X-ray; 1.20 A; A=1-226.
DR PDBsum; 1UHN; -.
DR PDBsum; 2ZFD; -.
DR AlphaFoldDB; Q8LAS7; -.
DR SMR; Q8LAS7; -.
DR BioGRID; 20941; 20.
DR DIP; DIP-32474N; -.
DR IntAct; Q8LAS7; 19.
DR STRING; 3702.AT5G55990.1; -.
DR iPTMnet; Q8LAS7; -.
DR SwissPalm; Q8LAS7; -.
DR PaxDb; Q8LAS7; -.
DR PRIDE; Q8LAS7; -.
DR ProteomicsDB; 220478; -.
DR EnsemblPlants; AT5G55990.1; AT5G55990.1; AT5G55990.
DR EnsemblPlants; AT5G55990.2; AT5G55990.2; AT5G55990.
DR GeneID; 835697; -.
DR Gramene; AT5G55990.1; AT5G55990.1; AT5G55990.
DR Gramene; AT5G55990.2; AT5G55990.2; AT5G55990.
DR KEGG; ath:AT5G55990; -.
DR Araport; AT5G55990; -.
DR TAIR; locus:2161760; AT5G55990.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR InParanoid; Q8LAS7; -.
DR OMA; GMNLADD; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q8LAS7; -.
DR EvolutionaryTrace; Q8LAS7; -.
DR PRO; PR:Q8LAS7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LAS7; baseline and differential.
DR Genevisible; Q8LAS7; AT.
DR GO; GO:0022626; C:cytosolic ribosome; 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:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA: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; TAS:TAIR.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:TAIR.
DR CDD; cd00051; EFh; 1.
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 3D-structure; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Vacuole.
FT CHAIN 1..226
FT /note="Calcineurin B-like protein 2"
FT /id="PRO_0000073503"
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; by CIPK11 and CIPK14"
FT /evidence="ECO:0000269|PubMed:21685179"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:22547024"
FT LIPID 12
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:22547024"
FT LIPID 18
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:22547024"
FT MUTAGEN 3
FT /note="Q->E: No effect on tonoplast targeting."
FT /evidence="ECO:0000269|PubMed:22547024"
FT MUTAGEN 4
FT /note="C->S: Loss of tonoplast targeting. Loss of tonoplast
FT targeting; when associated with S-12 and S-18."
FT /evidence="ECO:0000269|PubMed:22547024"
FT MUTAGEN 12
FT /note="C->S: Decreased tonoplast targeting. Loss of
FT tonoplast targeting; when associated with S-18. Loss of
FT tonoplast targeting; when associated with S-4 and S-18."
FT /evidence="ECO:0000269|PubMed:22547024"
FT MUTAGEN 18
FT /note="C->S: Loss of tonoplast targeting. Loss of tonoplast
FT targeting; when associated with S-12. Loss of tonoplast
FT targeting; when associated with S-4 and S-12."
FT /evidence="ECO:0000269|PubMed:22547024"
FT MUTAGEN 71
FT /note="E->A: No effect on binding to CIPK14."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 106
FT /note="E->A: No effect on binding to CIPK14."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 143
FT /note="E->A: No effect on binding to CIPK14."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 187
FT /note="E->A: No effect on binding to CIPK14."
FT /evidence="ECO:0000269|PubMed:18237745"
FT MUTAGEN 216
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:21685179"
FT MUTAGEN 216
FT /note="S->D: Increased interaction with CIPK11."
FT /evidence="ECO:0000269|PubMed:21685179"
FT CONFLICT 202
FT /note="M -> V (in Ref. 5; AAM65177)"
FT /evidence="ECO:0000305"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:2ZFD"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1UHN"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:2ZFD"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:2ZFD"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2ZFD"
SQ SEQUENCE 226 AA; 25809 MW; 342A013FC28D1445 CRC64;
MSQCVDGIKH LCTSVLGCFD LDLYKQSGGL GDPELLARDT VFSVSEIEAL YELFKKISSA
VIDDGLINKE EFQLALFKTN KKESLFADRV FDLFDTKHNG ILGFEEFARA LSVFHPNAPI
DDKIHFSFQL YDLKQQGFIE RQEVKQMVVA TLAESGMNLK DTVIEDIIDK TFEEADTKHD
GKIDKEEWRS LVLRHPSLLK NMTLQYLKDI TTTFPSFVFH SQVEDT
