CNBL9_ARATH
ID CNBL9_ARATH Reviewed; 213 AA.
AC Q9LTB8;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Calcineurin B-like protein 9;
GN Name=CBL9; OrderedLocusNames=At5g47100; ORFNames=K14A3.5;
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].
RA Albrecht V., Weinl S., Blazevic D., Kudla J.;
RT "Molecular characterization of the CBL gene family from Arabidopsis
RT thaliana.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15208400; DOI=10.1105/tpc.021311;
RA Pandey G.K., Cheong Y.H., Kim K.-N., Grant J.J., Li L., Hung W.,
RA D'Angelo C., Weinl S., Kudla J., Luan S.;
RT "The calcium sensor calcineurin B-like 9 modulates abscisic acid
RT sensitivity and biosynthesis in Arabidopsis.";
RL Plant Cell 16:1912-1924(2004).
RN [6]
RP GENE FAMILY, AND INTERACTION WITH CIPK1; CIPK8; CIPK18; CIPK21; CIPK23 AND
RP 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 [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, AND INTERACTION WITH CIPK3.
RX PubMed=19825536; DOI=10.1093/mp/ssn003;
RA Pandey G.K., Grant J.J., Cheong Y.H., Kim B.G., Li L., Luan S.;
RT "Calcineurin-B-like protein CBL9 interacts with target kinase CIPK3 in the
RT regulation of ABA response in seed germination.";
RL Mol. Plant 1:238-248(2008).
RN [11]
RP MYRISTOYLATION AT GLY-2.
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 [12]
RP SUBCELLULAR LOCATION, AND DOMAIN.
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 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 [14]
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 [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 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 involved in abscisic acid (ABA)
CC signaling and stress-induced ABA biosynthesis pathways. Contributes to
CC the regulation of early stress-related CBF/DREB transcription factors.
CC CBL proteins interact with CIPK serine-threonine protein kinases.
CC Binding of a CBL protein to the regulatory NAF domain of a CIPK protein
CC lead to the activation of the kinase in a calcium-dependent manner. May
CC function as a negative regulator of stress and ABA responses. Mediates
CC the 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 the calcium-dependent regulation by CIPK26 of
CC reactive oxygen species production by the NADPH oxidase RBOHF. The
CC CBL9/CIPK3 complex acts in the regulation of abscisic acid response in
CC seed germination. {ECO:0000269|PubMed:15208400,
CC ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17898163,
CC ECO:0000269|PubMed:17922773, ECO:0000269|PubMed:19825536,
CC ECO:0000269|PubMed:23335733}.
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 CIPK1, CIPK3, CIPK6, CIPK8, CIPK14, CIPK16, CIPK18, CIPK21, CIPK23,
CC CIPK24 and CIPK26. {ECO:0000250, ECO:0000269|PubMed:14730064,
CC ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17898163,
CC ECO:0000269|PubMed:17922773, ECO:0000269|PubMed:19825536,
CC ECO:0000269|PubMed:21685179, ECO:0000269|PubMed:23335733,
CC ECO:0000269|PubMed:25058458}.
CC -!- INTERACTION:
CC Q9LTB8; Q8RWC9: CIPK1; NbExp=5; IntAct=EBI-637381, EBI-1748677;
CC Q9LTB8; Q9C562: CIPK10; NbExp=9; IntAct=EBI-637381, EBI-537572;
CC Q9LTB8; O22932: CIPK11; NbExp=5; IntAct=EBI-637381, EBI-537638;
CC Q9LTB8; P92937: CIPK15; NbExp=3; IntAct=EBI-637381, EBI-537592;
CC Q9LTB8; Q9SEZ7: CIPK16; NbExp=7; IntAct=EBI-637381, EBI-1573415;
CC Q9LTB8; Q9FJ54: CIPK20; NbExp=5; IntAct=EBI-637381, EBI-25514480;
CC Q9LTB8; Q93VD3: CIPK23; NbExp=13; IntAct=EBI-637381, EBI-974277;
CC Q9LTB8; Q9LDI3: CIPK24; NbExp=8; IntAct=EBI-637381, EBI-537551;
CC Q9LTB8; Q2V452: CIPK3; NbExp=5; IntAct=EBI-637381, EBI-1748724;
CC Q9LTB8; Q9LEU7: CIPK5; NbExp=6; IntAct=EBI-637381, EBI-2026322;
CC Q9LTB8; Q9STV4: CIPK8; NbExp=8; IntAct=EBI-637381, EBI-2026454;
CC Q9LTB8; Q9MAM1: CIPK9; NbExp=4; IntAct=EBI-637381, EBI-1765282;
CC Q9LTB8; Q84JU4: IBR5; NbExp=4; IntAct=EBI-637381, EBI-604555;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16814720,
CC ECO:0000269|PubMed:17922773, ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:23482856}; Lipid-anchor
CC {ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17922773,
CC ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:23335733,
CC ECO:0000269|PubMed:23482856}. Note=Plasma membrane localization
CC abolished by 2-bromopalmitate (2-BP) treatment.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Colocalized with CIPK23 in root tips
CC and vascular bundles in the stem and the leaf, as well as in guard
CC cells and root hairs. {ECO:0000269|PubMed:15208400,
CC ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:17922773}.
CC -!- INDUCTION: By drought, cold, salt and abscisic acid (ABA) treatments.
CC {ECO:0000269|PubMed:15208400}.
CC -!- DOMAIN: The N-terminal 12 amino acids are sufficient for cell membrane
CC targeting. {ECO:0000269|PubMed:19832944}.
CC -!- PTM: Both N-myristoylation and calcium-mediated conformational changes
CC are essential for its function. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to abscisic acid in the early
CC developmental stages. {ECO:0000269|PubMed:15208400}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; AF411958; AAL10301.1; -; mRNA.
DR EMBL; AB025609; BAA98105.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95471.1; -; Genomic_DNA.
DR EMBL; AB060590; BAB69895.1; -; mRNA.
DR EMBL; BT002995; AAO22803.1; -; mRNA.
DR EMBL; BT004458; AAO42452.1; -; mRNA.
DR RefSeq; NP_199521.1; NM_124081.4.
DR AlphaFoldDB; Q9LTB8; -.
DR SMR; Q9LTB8; -.
DR BioGRID; 20004; 20.
DR DIP; DIP-33308N; -.
DR IntAct; Q9LTB8; 23.
DR STRING; 3702.AT5G47100.1; -.
DR iPTMnet; Q9LTB8; -.
DR SwissPalm; Q9LTB8; -.
DR PaxDb; Q9LTB8; -.
DR PRIDE; Q9LTB8; -.
DR ProteomicsDB; 220535; -.
DR EnsemblPlants; AT5G47100.1; AT5G47100.1; AT5G47100.
DR GeneID; 834756; -.
DR Gramene; AT5G47100.1; AT5G47100.1; AT5G47100.
DR KEGG; ath:AT5G47100; -.
DR Araport; AT5G47100; -.
DR TAIR; locus:2152012; AT5G47100.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR InParanoid; Q9LTB8; -.
DR OMA; REYSGHE; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q9LTB8; -.
DR PRO; PR:Q9LTB8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTB8; baseline and differential.
DR Genevisible; Q9LTB8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA: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; IEA:UniProtKB-KW.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0009860; P:pollen tube growth; 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; PF13202; EF-hand_5; 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; Calcium; Cell membrane; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Phosphoprotein; Reference proteome;
KW Repeat; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..213
FT /note="Calcineurin B-like protein 9"
FT /id="PRO_0000073510"
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 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 MUTAGEN 201
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:21685179"
FT MUTAGEN 201
FT /note="S->D: Increased interaction with CIPK23."
FT /evidence="ECO:0000269|PubMed:21685179"
SQ SEQUENCE 213 AA; 24532 MW; E848102CD14211EE CRC64;
MGCFHSTAAR EFPDHENPVK LASETAFSVS EVEALYELFK SISSSVVDDG LINKEEFQLA
LFKNRKKENL FANRIFDLFD VKRKGVIDFG DFVRSLNVFH PNASLEEKTD FTFRLYDMDC
TGFIERQEVK QMLIALLCES EMKLADDTIE MILDQTFEDA DVDRDGKIDK TEWSNFVIKN
PSLLKIMTLP YLRDITTTFP SFVFNSEVDE IAT
