CNBL4_ARATH
ID CNBL4_ARATH Reviewed; 222 AA.
AC O81223;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Calcineurin B-like protein 4 {ECO:0000303|PubMed:10590166};
DE AltName: Full=Protein SALT OVERLY SENSITIVE 3 {ECO:0000303|PubMed:11006339, ECO:0000303|PubMed:9632394};
GN Name=CBL4 {ECO:0000303|PubMed:10590166};
GN Synonyms=SOS3 {ECO:0000303|PubMed:11006339, ECO:0000303|PubMed:9632394};
GN OrderedLocusNames=At5g24270 {ECO:0000312|Araport:AT5G24270};
GN ORFNames=MOP9.8 {ECO:0000312|EMBL:BAB10392.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9632394; DOI=10.1126/science.280.5371.1943;
RA Liu J., Zhu J.-K.;
RT "A calcium sensor homolog required for plant salt tolerance.";
RL Science 280:1943-1945(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CIPK6.
RC STRAIN=cv. Columbia;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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=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 [6]
RP FUNCTION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=11006339; DOI=10.2307/3871181;
RA Ishitani M., Liu J., Halfter U., Kim C.-S., Shi W., Zhu J.-K.;
RT "SOS3 function in plant salt tolerance requires N-myristoylation and
RT calcium binding.";
RL Plant Cell 12:1667-1677(2000).
RN [7]
RP FUNCTION, AND INTERACTION WITH CIPK24/SOS2; CIPK6/SIP3; CIPK10/SIP1;
RP CIPK11/SIP4 AND CIPK15/SIP2.
RX PubMed=10725350; DOI=10.1073/pnas.97.7.3735;
RA Halfter U., Ishitani M., Zhu J.-K.;
RT "The Arabidopsis SOS2 protein kinase physically interacts with and is
RT activated by the calcium-binding protein SOS3.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000).
RN [8]
RP FUNCTION.
RX PubMed=12034882; DOI=10.1073/pnas.122224699;
RA Qiu Q.-S., Guo Y., Dietrich M.A., Schumaker K.S., Zhu J.-K.;
RT "Regulation of SOS1, a plasma membrane Na(+)/H(+) exchanger in Arabidopsis
RT thaliana, by SOS2 and SOS3.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8436-8441(2002).
RN [9]
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 [10]
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 [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 FUNCTION, INTERACTION WITH CIPK6, DISRUPTION PHENOTYPE, PHOSPHORYLATION,
RP AND MUTAGENESIS OF GLY-2 AND CYS-3.
RX PubMed=21445098; DOI=10.1038/cr.2011.50;
RA Held K., Pascaud F., Eckert C., Gajdanowicz P., Hashimoto K.,
RA Corratge-Faillie C., Offenborn J.N., Lacombe B., Dreyer I., Thibaud J.B.,
RA Kudla J.;
RT "Calcium-dependent modulation and plasma membrane targeting of the AKT2
RT potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase
RT complex.";
RL Cell Res. 21:1116-1130(2011).
RN [13]
RP PHOSPHORYLATION, INTERACTION WITH CIPK24, AND MUTAGENESIS OF SER-205.
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 [14]
RP FUNCTION.
RX PubMed=23052592; DOI=10.1007/s00299-012-1348-3;
RA Ye J., Zhang W., Guo Y.;
RT "Arabidopsis SOS3 plays an important role in salt tolerance by mediating
RT calcium-dependent microfilament reorganization.";
RL Plant Cell Rep. 32:139-148(2013).
RN [15]
RP INTERACTION WITH ABCG36.
RC STRAIN=cv. Columbia;
RX PubMed=26315018; DOI=10.1111/nph.13582;
RA Campe R., Langenbach C., Leissing F., Popescu G.V., Popescu S.C.,
RA Goellner K., Beckers G.J., Conrath U.;
RT "ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin that, like
RT PEN3, is required for Arabidopsis nonhost resistance.";
RL New Phytol. 209:294-306(2016).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH CALCIUM AND MANGANESE
RP IONS, AND HOMODIMERIZATION.
RX PubMed=15644219; DOI=10.1016/j.jmb.2004.11.025;
RA Sanchez-Barrena M.J., Martinez-Ripoll M., Zhu J.-K., Albert A.;
RT "The structure of the Arabidopsis thaliana SOS3: molecular mechanism of
RT sensing calcium for salt stress response.";
RL J. Mol. Biol. 345:1253-1264(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-207 IN COMPLEX WITH SOS2;
RP CALCIUM AND MANGANESE IONS, AND INTERACTION WITH SOS2.
RX PubMed=17499048; DOI=10.1016/j.molcel.2007.04.013;
RA Sanchez-Barrena M.J., Fujii H., Angulo I., Martinez-Ripoll M., Zhu J.-K.,
RA Albert A.;
RT "The structure of the C-terminal domain of the protein kinase AtSOS2 bound
RT to the calcium sensor AtSOS3.";
RL Mol. Cell 26:427-435(2007).
CC -!- FUNCTION: Acts as a calcium sensor involved in the regulatory pathway
CC for the control of intracellular Na(+) and K(+) homeostasis and salt
CC tolerance. Binding of a CBL protein to the regulatory NAF domain of a
CC CIPK serine-threonine protein kinase lead to the activation of the
CC kinase in a calcium-dependent manner. Operates in synergy with
CC CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1.
CC Involved in salt stress responses by mediating calcium-dependent
CC microfilament reorganization. The CBL4/CIPK6 complex mediates
CC translocation of AKT2 from the endoplasmic reticulum to the plasma
CC membrane. Both myristoylation and S-acylation are required for AKT2
CC activation. {ECO:0000269|PubMed:10725350, ECO:0000269|PubMed:11006339,
CC ECO:0000269|PubMed:12034882, ECO:0000269|PubMed:21445098,
CC ECO:0000269|PubMed:23052592}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 4 Ca(2+) ions per subunit.;
CC -!- SUBUNIT: Interacts with CIPK24/SOS2, CIPK6/SIP3, CIPK10/SIP1,
CC CIPK11/SIP4 and CIPK15/SIP2. Homodimer, mediated by calcium-binding.
CC Binds to ABCG36 (PubMed:26315018). {ECO:0000269|PubMed:10590166,
CC ECO:0000269|PubMed:10725350, ECO:0000269|PubMed:15644219,
CC ECO:0000269|PubMed:17499048, ECO:0000269|PubMed:21445098,
CC ECO:0000269|PubMed:22253446, ECO:0000269|PubMed:26315018}.
CC -!- INTERACTION:
CC O81223; Q8RWC9: CIPK1; NbExp=3; IntAct=EBI-537541, EBI-1748677;
CC O81223; Q9LDI3: CIPK24; NbExp=10; IntAct=EBI-537541, EBI-537551;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19832944};
CC Lipid-anchor {ECO:0000269|PubMed:19832944}. Cytoplasm
CC {ECO:0000269|PubMed:19832944}. Nucleus {ECO:0000269|PubMed:19832944}.
CC Note=The cell membrane localization is S-acylation dependent.
CC -!- DOMAIN: The calcium-binding domain (165-176) of the EF-hand 4 can also
CC interacts with a manganese ion. The N-terminal 18 amino acids are
CC sufficient for the cell membrane targeting of a heterologous protein.
CC {ECO:0000269|PubMed:19832944}.
CC -!- PTM: Both N-myristoylation and calcium-mediated conformational changes
CC are essential for its function. S-acylated at Cys-3. Phosphorylated by
CC CIPK6 and CIPK24. {ECO:0000269|PubMed:11006339,
CC ECO:0000269|PubMed:18502848, ECO:0000269|PubMed:21445098,
CC ECO:0000269|PubMed:22253446}.
CC -!- DISRUPTION PHENOTYPE: Delayed development and flowering.
CC {ECO:0000269|PubMed:21445098}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; AF060553; AAC26110.1; -; Genomic_DNA.
DR EMBL; Y18870; CAB39731.1; -; mRNA.
DR EMBL; AF192886; AAG28402.1; -; mRNA.
DR EMBL; AB006701; BAB10392.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93277.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93278.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69640.1; -; Genomic_DNA.
DR EMBL; AY063993; AAL36349.1; -; mRNA.
DR EMBL; AY096693; AAM20327.1; -; mRNA.
DR RefSeq; NP_001190377.1; NM_001203448.2.
DR RefSeq; NP_001331303.1; NM_001343862.1.
DR RefSeq; NP_197815.1; NM_122333.6.
DR PDB; 1V1F; X-ray; 3.00 A; A=1-222.
DR PDB; 1V1G; X-ray; 2.70 A; A=1-222.
DR PDB; 2EHB; X-ray; 2.10 A; A=1-207.
DR PDB; 5O9U; X-ray; 1.85 A; C/D=2-9.
DR PDBsum; 1V1F; -.
DR PDBsum; 1V1G; -.
DR PDBsum; 2EHB; -.
DR PDBsum; 5O9U; -.
DR AlphaFoldDB; O81223; -.
DR SMR; O81223; -.
DR BioGRID; 17769; 22.
DR DIP; DIP-34746N; -.
DR IntAct; O81223; 13.
DR STRING; 3702.AT5G24270.2; -.
DR iPTMnet; O81223; -.
DR PaxDb; O81223; -.
DR PRIDE; O81223; -.
DR ProteomicsDB; 220285; -.
DR EnsemblPlants; AT5G24270.1; AT5G24270.1; AT5G24270.
DR EnsemblPlants; AT5G24270.2; AT5G24270.2; AT5G24270.
DR EnsemblPlants; AT5G24270.4; AT5G24270.4; AT5G24270.
DR GeneID; 832494; -.
DR Gramene; AT5G24270.1; AT5G24270.1; AT5G24270.
DR Gramene; AT5G24270.2; AT5G24270.2; AT5G24270.
DR Gramene; AT5G24270.4; AT5G24270.4; AT5G24270.
DR KEGG; ath:AT5G24270; -.
DR Araport; AT5G24270; -.
DR TAIR; locus:2169794; AT5G24270.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR InParanoid; O81223; -.
DR OMA; ELWEVVI; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; O81223; -.
DR EvolutionaryTrace; O81223; -.
DR PRO; PR:O81223; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O81223; baseline and differential.
DR Genevisible; O81223; AT.
DR GO; GO:0005955; C:calcineurin complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
DR GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; ISS:TAIR.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:TAIR.
DR GO; GO:0005513; P:detection of calcium ion; IMP:TAIR.
DR GO; GO:0042539; P:hypotonic salinity response; 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; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 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; Cell membrane; Cytoplasm; Lipoprotein; Manganese; Membrane;
KW Myristate; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..222
FT /note="Calcineurin B-like protein 4"
FT /id="PRO_0000073505"
FT DOMAIN 35..70
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 71..106
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 108..143
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 152..187
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 144
FT /note="Involved in dimerization"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8LAS7"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:11006339,
FT ECO:0000269|PubMed:18502848"
FT MUTAGEN 2
FT /note="G->A: Abolishes function in salt tolerance and loss
FT of activation of AKT2."
FT /evidence="ECO:0000269|PubMed:11006339,
FT ECO:0000269|PubMed:21445098"
FT MUTAGEN 3
FT /note="C->S: Loss of activation of AKT2."
FT /evidence="ECO:0000269|PubMed:21445098"
FT MUTAGEN 205
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:22253446"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:2EHB"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2EHB"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1V1G"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:2EHB"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:2EHB"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:2EHB"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:2EHB"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:2EHB"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:2EHB"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2EHB"
SQ SEQUENCE 222 AA; 25693 MW; DF06C3973748AFF7 CRC64;
MGCSVSKKKK KNAMRPPGYE DPELLASVTP FTVEEVEALY ELFKKLSSSI IDDGLIHKEE
FQLALFRNRN RRNLFADRIF DVFDVKRNGV IEFGEFVRSL GVFHPSAPVH EKVKFAFKLY
DLRQTGFIER EELKEMVVAL LHESELVLSE DMIEVMVDKA FVQADRKNDG KIDIDEWKDF
VSLNPSLIKN MTLPYLKDIN RTFPSFVSSC EEEEMELQNV SS
