CNBLA_ARATH
ID CNBLA_ARATH Reviewed; 256 AA.
AC Q7FRS8; O82641; Q2HIW7; Q8GYR3; Q8GZD7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Calcineurin B-like protein 10;
DE AltName: Full=SOS3-like calcium binding protein 8;
DE Short=SCaBP8;
GN Name=CBL10; OrderedLocusNames=At4g33000; ORFNames=F26P21_120;
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).
RX PubMed=12045290; DOI=10.1105/tpc.001115;
RA Luan S., Kudla J., Rodriguez-Concepcion M., Yalovsky S., Gruissem W.;
RT "Calmodulins and calcineurin B-like proteins: calcium sensors for specific
RT signal response coupling in plants.";
RL Plant Cell 14:S389-S400(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Cheong Y.H., Luan S.;
RT "Isolation of calcineurin B-like gene from Arabidopsis.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP FUNCTION, INTERACTION WITH CIPK24, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17449811; DOI=10.1105/tpc.106.042291;
RA Quan R., Lin H., Mendoza I., Zhang Y., Cao W., Yang Y., Shang M., Chen S.,
RA Pardo J.M., Guo Y.;
RT "SCABP8/CBL10, a putative calcium sensor, interacts with the protein kinase
RT SOS2 to protect Arabidopsis shoots from salt stress.";
RL Plant Cell 19:1415-1431(2007).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH CIPK24,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [10]
RP PHOSPHORYLATION AT SER-247, AND MUTAGENESIS OF SER-247 AND THR-252.
RX PubMed=19448033; DOI=10.1105/tpc.109.066217;
RA Lin H., Yang Y., Quan R., Mendoza I., Wu Y., Du W., Zhao S.,
RA Schumaker K.S., Pardo J.M., Guo Y.;
RT "Phosphorylation of SOS3-LIKE CALCIUM BINDING PROTEIN8 by SOS2 protein
RT kinase stabilizes their protein complex and regulates salt tolerance in
RT Arabidopsis.";
RL Plant Cell 21:1607-1619(2009).
RN [11]
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 [12]
RP PHOSPHORYLATION AT SER-247, INTERACTION WITH CIPK24, AND MUTAGENESIS OF
RP SER-247.
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 [13]
RP FUNCTION, INTERACTION WITH AKT1, AND DISRUPTION PHENOTYPE.
RX PubMed=23331977; DOI=10.1111/tpj.12123;
RA Ren X.L., Qi G.N., Feng H.Q., Zhao S., Zhao S.S., Wang Y., Wu W.H.;
RT "Calcineurin B-like protein CBL10 directly interacts with AKT1 and
RT modulates K+ homeostasis in Arabidopsis.";
RL Plant J. 74:258-266(2013).
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. Mediates salt tolerance, but only
CC when phosphorylated. Competes with CIPK23 for a direct binding to AKT1,
CC negatively regulating its activity via a protein kinase-independent
CC mechanism. {ECO:0000269|PubMed:17449811, ECO:0000269|PubMed:17825054,
CC ECO:0000269|PubMed:23331977}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CIPK24 and AKT1.
CC {ECO:0000250, ECO:0000269|PubMed:17449811, ECO:0000269|PubMed:17825054,
CC ECO:0000269|PubMed:22253446, ECO:0000269|PubMed:23331977}.
CC -!- INTERACTION:
CC Q7FRS8; Q9LDI3: CIPK24; NbExp=5; IntAct=EBI-2026616, EBI-537551;
CC Q7FRS8-2; Q9LDI3: CIPK24; NbExp=4; IntAct=EBI-2026677, EBI-537551;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane. Endosome. Cell membrane.
CC Note=Exclusively targeted to the tonoplast when interacting with CIPK24
CC (PubMed:19832944). PubMed:17449811 indicates a cell membrane
CC localization while PubMed:17825054 shows a vacuole membrane and
CC endosome localization. {ECO:0000269|PubMed:19832944}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7FRS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7FRS8-2; Sequence=VSP_012329;
CC -!- TISSUE SPECIFICITY: Expressed in shoots, leaves, stems, flowers and
CC siliques. Barely detected in roots. {ECO:0000269|PubMed:17825054}.
CC -!- INDUCTION: Not induced by abiotic stresses.
CC {ECO:0000269|PubMed:17825054}.
CC -!- DOMAIN: The N-terminal 40 amino acids are necessary and sufficient for
CC vacuolar and endosomal targeting. {ECO:0000269|PubMed:19832944}.
CC -!- PTM: Phosphorylated by CIPK24. The level of phosphorylation is enhanced
CC by CIPK24-CBL10 interaction. The phosphorylation is induced by salt
CC stress and limited to membrane-bound CBL10.
CC {ECO:0000269|PubMed:19448033, ECO:0000269|PubMed:22253446}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions but hypersensitivity to salt stress.
CC {ECO:0000269|PubMed:17449811, ECO:0000269|PubMed:17825054,
CC ECO:0000269|PubMed:23331977}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA21209.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80017.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF490607; AAO72364.1; -; mRNA.
DR EMBL; AF513507; AAO14864.2; -; mRNA.
DR EMBL; AL031804; CAA21209.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161582; CAB80017.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86156.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86157.1; -; Genomic_DNA.
DR EMBL; AK117439; BAC42104.1; -; mRNA.
DR EMBL; BT024464; ABD19645.1; -; mRNA.
DR PIR; H85387; H85387.
DR PIR; T05308; T05308.
DR RefSeq; NP_195026.1; NM_119454.2. [Q7FRS8-1]
DR RefSeq; NP_849485.1; NM_179154.2. [Q7FRS8-2]
DR AlphaFoldDB; Q7FRS8; -.
DR SMR; Q7FRS8; -.
DR BioGRID; 14722; 3.
DR IntAct; Q7FRS8; 3.
DR STRING; 3702.AT4G33000.1; -.
DR iPTMnet; Q7FRS8; -.
DR PaxDb; Q7FRS8; -.
DR PRIDE; Q7FRS8; -.
DR ProteomicsDB; 220536; -. [Q7FRS8-1]
DR EnsemblPlants; AT4G33000.1; AT4G33000.1; AT4G33000. [Q7FRS8-1]
DR EnsemblPlants; AT4G33000.2; AT4G33000.2; AT4G33000. [Q7FRS8-2]
DR GeneID; 829437; -.
DR Gramene; AT4G33000.1; AT4G33000.1; AT4G33000. [Q7FRS8-1]
DR Gramene; AT4G33000.2; AT4G33000.2; AT4G33000. [Q7FRS8-2]
DR KEGG; ath:AT4G33000; -.
DR Araport; AT4G33000; -.
DR TAIR; locus:2123767; AT4G33000.
DR eggNOG; KOG0034; Eukaryota.
DR InParanoid; Q7FRS8; -.
DR OMA; PHLKCIT; -.
DR PhylomeDB; Q7FRS8; -.
DR PRO; PR:Q7FRS8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q7FRS8; baseline and differential.
DR Genevisible; Q7FRS8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
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; IDA:TAIR.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0050801; P:ion homeostasis; IMP:TAIR.
DR GO; GO:0043266; P:regulation of potassium ion transport; IMP:TAIR.
DR CDD; cd00051; EFh; 2.
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 Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Endosome; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Vacuole.
FT CHAIN 1..256
FT /note="Calcineurin B-like protein 10"
FT /id="PRO_0000073511"
FT DOMAIN 77..112
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 113..148
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 150..185
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 194..229
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 186
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 247
FT /note="Phosphoserine; by CIPK24"
FT /evidence="ECO:0000269|PubMed:19448033,
FT ECO:0000269|PubMed:22253446"
FT VAR_SEQ 1..16
FT /note="MTTGRPNNILALKIST -> MEQVSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.6"
FT /id="VSP_012329"
FT MUTAGEN 247
FT /note="S->A: Loss of phosphorylation. Loss of
FT phosphorylation; when associated with A-252."
FT /evidence="ECO:0000269|PubMed:19448033,
FT ECO:0000269|PubMed:22253446"
FT MUTAGEN 252
FT /note="T->A: No effect on phosphorylation. Loss of
FT phosphorylation; when associated with A-247."
FT /evidence="ECO:0000269|PubMed:19448033"
SQ SEQUENCE 256 AA; 29342 MW; F7A579108C935AED CRC64;
MTTGRPNNIL ALKISTRSSS LTVGEQFCAV FIPFFAIIDV LVSSVGQCFD CRSTSPRTCQ
HADLERLARE SQFSVNEVEA LYELFKKLSC SIIDDGLIHK EELRLALFQA PYGENLFLDR
VFDLFDEKKN GVIEFEEFIH ALSVFHPYAS IQEKTDFAFR LYDLRQTGFI EREEVQQMVS
AILLESDMML SDELLTMIID KTFADADSDK DGKISKDEWN VYVHKHPSLL KNMTLPYLKD
VTTAFPSFIF NTEVED
