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Calcineurin B-like protein 4 (Protein SALT OVERLY SENSITIVE 3)

 CNBL4_ARATH             Reviewed;         222 AA.
O81223;
21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 146.
RecName: Full=Calcineurin B-like protein 4;
AltName: Full=Protein SALT OVERLY SENSITIVE 3;
Name=CBL4; Synonyms=SOS3; OrderedLocusNames=At5g24270;
ORFNames=MOP9.8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9632394; DOI=10.1126/science.280.5371.1943;
Liu J., Zhu J.-K.;
"A calcium sensor homolog required for plant salt tolerance.";
Science 280:1943-1945(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CIPK6.
STRAIN=cv. Columbia;
PubMed=10590166; DOI=10.1105/tpc.11.12.2393;
Shi J., Kim K.-N., Ritz O., Albrecht V., Gupta R., Harter K., Luan S.,
Kudla J.;
"Novel protein kinases associated with calcineurin B-like calcium
sensors in Arabidopsis.";
Plant Cell 11:2393-2405(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9405937; DOI=10.1093/dnares/4.4.291;
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. II.
Sequence features of the regions of 1,044,062 bp covered by thirteen
physically assigned P1 clones.";
DNA Res. 4:291-300(1997).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
PubMed=11006339; DOI=10.1105/tpc.12.9.1667;
Ishitani M., Liu J., Halfter U., Kim C.-S., Shi W., Zhu J.-K.;
"SOS3 function in plant salt tolerance requires N-myristoylation and
calcium binding.";
Plant Cell 12:1667-1677(2000).
[7]
FUNCTION, AND INTERACTION WITH CIPK24/SOS2; CIPK6/SIP3; CIPK10/SIP1;
CIPK11/SIP4 AND CIPK15/SIP2.
PubMed=10725350; DOI=10.1073/pnas.97.7.3735;
Halfter U., Ishitani M., Zhu J.-K.;
"The Arabidopsis SOS2 protein kinase physically interacts with and is
activated by the calcium-binding protein SOS3.";
Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000).
[8]
FUNCTION.
PubMed=12034882; DOI=10.1073/pnas.122224699;
Qiu Q.-S., Guo Y., Dietrich M.A., Schumaker K.S., Zhu J.-K.;
"Regulation of SOS1, a plasma membrane Na(+)/H(+) exchanger in
Arabidopsis thaliana, by SOS2 and SOS3.";
Proc. Natl. Acad. Sci. U.S.A. 99:8436-8441(2002).
[9]
GENE FAMILY.
PubMed=14730064; DOI=10.1104/pp.103.033068;
Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
"Calcium sensors and their interacting protein kinases: genomics of
the Arabidopsis and rice CBL-CIPK signaling networks.";
Plant Physiol. 134:43-58(2004).
[10]
MYRISTOYLATION AT GLY-2.
PubMed=18502848; DOI=10.1105/tpc.108.058123;
Batistic O., Sorek N., Schueltke S., Yalovsky S., Kudla J.;
"Dual fatty acyl modification determines the localization and plasma
membrane targeting of CBL/CIPK Ca2+ signaling complexes in
Arabidopsis.";
Plant Cell 20:1346-1362(2008).
[11]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=19832944; DOI=10.1111/j.1365-313X.2009.04045.x;
Batistic O., Waadt R., Steinhorst L., Held K., Kudla J.;
"CBL-mediated targeting of CIPKs facilitates the decoding of calcium
signals emanating from distinct cellular stores.";
Plant J. 61:211-222(2010).
[12]
FUNCTION, INTERACTION WITH CIPK6, DISRUPTION PHENOTYPE,
PHOSPHORYLATION, AND MUTAGENESIS OF GLY-2 AND CYS-3.
PubMed=21445098; DOI=10.1038/cr.2011.50;
Held K., Pascaud F., Eckert C., Gajdanowicz P., Hashimoto K.,
Corratge-Faillie C., Offenborn J.N., Lacombe B., Dreyer I.,
Thibaud J.B., Kudla J.;
"Calcium-dependent modulation and plasma membrane targeting of the
AKT2 potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase
complex.";
Cell Res. 21:1116-1130(2011).
[13]
PHOSPHORYLATION, INTERACTION WITH CIPK24, AND MUTAGENESIS OF SER-205.
PubMed=22253446; DOI=10.1074/jbc.M111.279331;
Hashimoto K., Eckert C., Anschuetz U., Scholz M., Held K., Waadt R.,
Reyer A., Hippler M., Becker D., Kudla J.;
"Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins
by their CBL-interacting protein kinases (CIPKs) is required for full
activity of CBL-CIPK complexes toward their target proteins.";
J. Biol. Chem. 287:7956-7968(2012).
[14]
FUNCTION.
PubMed=23052592; DOI=10.1007/s00299-012-1348-3;
Ye J., Zhang W., Guo Y.;
"Arabidopsis SOS3 plays an important role in salt tolerance by
mediating calcium-dependent microfilament reorganization.";
Plant Cell Rep. 32:139-148(2013).
[15]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
MANGANESE IONS, AND HOMODIMERIZATION.
PubMed=15644219; DOI=10.1016/j.jmb.2004.11.025;
Sanchez-Barrena M.J., Martinez-Ripoll M., Zhu J.-K., Albert A.;
"The structure of the Arabidopsis thaliana SOS3: molecular mechanism
of sensing calcium for salt stress response.";
J. Mol. Biol. 345:1253-1264(2005).
[16]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-207 IN COMPLEX WITH SOS2;
CALCIUM AND MANGANESE IONS, AND INTERACTION WITH SOS2.
PubMed=17499048; DOI=10.1016/j.molcel.2007.04.013;
Sanchez-Barrena M.J., Fujii H., Angulo I., Martinez-Ripoll M.,
Zhu J.-K., Albert A.;
"The structure of the C-terminal domain of the protein kinase AtSOS2
bound to the calcium sensor AtSOS3.";
Mol. Cell 26:427-435(2007).
-!- FUNCTION: Acts as a calcium sensor involved in the regulatory
pathway for the control of intracellular Na(+) and K(+)
homeostasis and salt tolerance. Binding of a CBL protein to the
regulatory NAF domain of a CIPK serine-threonine protein kinase
lead to the activation of the kinase in a calcium-dependent
manner. Operates in synergy with CIPK24/SOS2 to activate the
plasma membrane Na(+)/H(+) antiporter SOS1. Involved in salt
stress responses by mediating calcium-dependent microfilament
reorganization. The CBL4/CIPK6 complex mediates translocation of
AKT2 from the endoplasmic reticulum to the plasma membrane. Both
myristoylation and S-acylation are required for AKT2 activation.
{ECO:0000269|PubMed:10725350, ECO:0000269|PubMed:11006339,
ECO:0000269|PubMed:12034882, ECO:0000269|PubMed:21445098,
ECO:0000269|PubMed:23052592}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 4 Ca(2+) ions per subunit.;
-!- SUBUNIT: Interacts with CIPK24/SOS2, CIPK6/SIP3, CIPK10/SIP1,
CIPK11/SIP4 and CIPK15/SIP2. Homodimer, mediated by calcium-
binding. {ECO:0000269|PubMed:10590166,
ECO:0000269|PubMed:10725350, ECO:0000269|PubMed:15644219,
ECO:0000269|PubMed:17499048, ECO:0000269|PubMed:21445098,
ECO:0000269|PubMed:22253446}.
-!- INTERACTION:
Q8RWC9:CIPK1; NbExp=3; IntAct=EBI-537541, EBI-1748677;
Q9LDI3:CIPK24; NbExp=10; IntAct=EBI-537541, EBI-537551;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19832944};
Lipid-anchor {ECO:0000269|PubMed:19832944}. Cytoplasm
{ECO:0000269|PubMed:19832944}. Nucleus
{ECO:0000269|PubMed:19832944}. Note=The cell membrane localization
is S-acylation dependent.
-!- DOMAIN: The calcium-binding domain (165-176) of the EF-hand 4 can
also interacts with a manganese ion. The N-terminal 18 amino acids
are sufficient for the cell membrane targeting of a heterologous
protein. {ECO:0000269|PubMed:19832944}.
-!- PTM: Both N-myristoylation and calcium-mediated conformational
changes are essential for its function. S-acylated at Cys-3.
Phosphorylated by CIPK6 and CIPK24. {ECO:0000269|PubMed:11006339,
ECO:0000269|PubMed:18502848, ECO:0000269|PubMed:21445098,
ECO:0000269|PubMed:22253446}.
-!- DISRUPTION PHENOTYPE: Delayed development and flowering.
{ECO:0000269|PubMed:21445098}.
-!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF060553; AAC26110.1; -; Genomic_DNA.
EMBL; Y18870; CAB39731.1; -; mRNA.
EMBL; AF192886; AAG28402.1; -; mRNA.
EMBL; AB006701; BAB10392.1; -; Genomic_DNA.
EMBL; CP002688; AED93277.1; -; Genomic_DNA.
EMBL; CP002688; AED93278.1; -; Genomic_DNA.
EMBL; CP002688; ANM69640.1; -; Genomic_DNA.
EMBL; AY063993; AAL36349.1; -; mRNA.
EMBL; AY096693; AAM20327.1; -; mRNA.
RefSeq; NP_001190377.1; NM_001203448.2.
RefSeq; NP_001331303.1; NM_001343862.1.
RefSeq; NP_197815.1; NM_122333.6.
UniGene; At.20610; -.
PDB; 1V1F; X-ray; 3.00 A; A=1-222.
PDB; 1V1G; X-ray; 2.70 A; A=1-222.
PDB; 2EHB; X-ray; 2.10 A; A=1-207.
PDB; 5O9U; X-ray; 1.85 A; C/D=2-9.
PDBsum; 1V1F; -.
PDBsum; 1V1G; -.
PDBsum; 2EHB; -.
PDBsum; 5O9U; -.
ProteinModelPortal; O81223; -.
SMR; O81223; -.
BioGrid; 17769; 22.
DIP; DIP-34746N; -.
IntAct; O81223; 13.
STRING; 3702.AT5G24270.1; -.
iPTMnet; O81223; -.
PaxDb; O81223; -.
EnsemblPlants; AT5G24270.1; AT5G24270.1; AT5G24270.
EnsemblPlants; AT5G24270.2; AT5G24270.2; AT5G24270.
EnsemblPlants; AT5G24270.4; AT5G24270.4; AT5G24270.
GeneID; 832494; -.
Gramene; AT5G24270.1; AT5G24270.1; AT5G24270.
Gramene; AT5G24270.2; AT5G24270.2; AT5G24270.
Gramene; AT5G24270.4; AT5G24270.4; AT5G24270.
KEGG; ath:AT5G24270; -.
Araport; AT5G24270; -.
TAIR; locus:2169794; AT5G24270.
eggNOG; KOG0034; Eukaryota.
eggNOG; COG5126; LUCA.
HOGENOM; HOG000233019; -.
InParanoid; O81223; -.
KO; K06268; -.
OMA; MNRCPRR; -.
OrthoDB; EOG09360M5E; -.
PhylomeDB; O81223; -.
EvolutionaryTrace; O81223; -.
PRO; PR:O81223; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; O81223; baseline and differential.
Genevisible; O81223; AT.
GO; GO:0005955; C:calcineurin complex; ISS:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; ISS:TAIR.
GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:TAIR.
GO; GO:0005513; P:detection of calcium ion; IMP:TAIR.
GO; GO:0042539; P:hypotonic salinity response; IMP:TAIR.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13202; EF-hand_5; 1.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS50222; EF_HAND_2; 3.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Complete proteome; Cytoplasm;
Lipoprotein; Manganese; Membrane; Metal-binding; Myristate; Nucleus;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed.
CHAIN 2 222 Calcineurin B-like protein 4.
/FTId=PRO_0000073505.
DOMAIN 35 70 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 71 106 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 108 143 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 152 187 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 47 60 1; atypical.
CA_BIND 84 95 2.
CA_BIND 121 132 3.
CA_BIND 165 176 4.
COMPBIAS 211 216 Poly-Glu.
SITE 144 144 Involved in dimerization.
MOD_RES 205 205 Phosphoserine.
{ECO:0000250|UniProtKB:Q8LAS7}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:11006339,
ECO:0000269|PubMed:18502848}.
MUTAGEN 2 2 G->A: Abolishes function in salt
tolerance and loss of activation of AKT2.
{ECO:0000269|PubMed:11006339,
ECO:0000269|PubMed:21445098}.
MUTAGEN 3 3 C->S: Loss of activation of AKT2.
{ECO:0000269|PubMed:21445098}.
MUTAGEN 205 205 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:22253446}.
HELIX 22 28 {ECO:0000244|PDB:2EHB}.
HELIX 33 46 {ECO:0000244|PDB:2EHB}.
STRAND 49 51 {ECO:0000244|PDB:2EHB}.
STRAND 53 56 {ECO:0000244|PDB:1V1G}.
HELIX 58 66 {ECO:0000244|PDB:2EHB}.
HELIX 74 83 {ECO:0000244|PDB:2EHB}.
STRAND 88 91 {ECO:0000244|PDB:2EHB}.
HELIX 93 100 {ECO:0000244|PDB:2EHB}.
HELIX 101 103 {ECO:0000244|PDB:2EHB}.
HELIX 109 120 {ECO:0000244|PDB:2EHB}.
STRAND 126 129 {ECO:0000244|PDB:2EHB}.
HELIX 130 144 {ECO:0000244|PDB:2EHB}.
HELIX 150 164 {ECO:0000244|PDB:2EHB}.
STRAND 169 172 {ECO:0000244|PDB:2EHB}.
HELIX 174 183 {ECO:0000244|PDB:2EHB}.
HELIX 185 191 {ECO:0000244|PDB:2EHB}.
TURN 194 197 {ECO:0000244|PDB:2EHB}.
TURN 199 201 {ECO:0000244|PDB:2EHB}.
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


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