CNBL5_ARATH
ID CNBL5_ARATH Reviewed; 203 AA.
AC Q7FZF1; O81328;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Calcineurin B-like protein 5;
DE AltName: Full=SOS3-like calcium-binding protein 4;
GN Name=CBL5; Synonyms=SCABP4; OrderedLocusNames=At4g01420; ORFNames=F3D13.2;
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].
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 [2]
RP SEQUENCE REVISION.
RA Kudla J.;
RL Submitted (MAR-2003) 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 [MRNA] OF 1-192.
RC STRAIN=cv. Columbia;
RX PubMed=11115898; DOI=10.1104/pp.124.4.1844;
RA Kim K.-N., Cheong Y.H., Gupta R., Luan S.;
RT "Interaction specificity of Arabidopsis calcineurin B-like calcium sensors
RT and their target kinases.";
RL Plant Physiol. 124:1844-1853(2000).
RN [6]
RP INTERACTION WITH CIPK2 AND CIPK11.
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 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 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 [9]
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 [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20077023; DOI=10.1007/s10059-010-0025-z;
RA Cheong Y.H., Sung S.J., Kim B.G., Pandey G.K., Cho J.S., Kim K.N., Luan S.;
RT "Constitutive overexpression of the calcium sensor CBL5 confers osmotic or
RT drought stress tolerance in Arabidopsis.";
RL Mol. Cells 29:159-165(2010).
RN [11]
RP SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH 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 [12]
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).
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. May function as a positive
CC regulator of salt or drought responses. {ECO:0000269|PubMed:20077023}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PP2CA, CIPK2,
CC CIPK11, CIPK23 and CIPK24. {ECO:0000250, ECO:0000269|PubMed:11230129,
CC ECO:0000269|PubMed:16814720, ECO:0000269|PubMed:19832944,
CC ECO:0000269|PubMed:21596690}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19832944}. Nucleus
CC {ECO:0000269|PubMed:19832944}. Note=Targeted to the cell membrane when
CC interacting with CIPK24.
CC -!- TISSUE SPECIFICITY: Expressed in green tissues, but not in the roots.
CC {ECO:0000269|PubMed:20077023}.
CC -!- DOMAIN: The N-terminal 12 amino acids are sufficient for cell membrane
CC targeting of a heterologous protein. {ECO:0000269|PubMed:19832944}.
CC -!- PTM: Both N-myristoylation and calcium-mediated conformational changes
CC are essential for its function. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19290.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80951.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF192885; AAG28401.2; -; mRNA.
DR EMBL; AF069300; AAC19290.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161491; CAB80951.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82023.1; -; Genomic_DNA.
DR EMBL; AF290435; AAG10060.1; -; mRNA.
DR PIR; T01375; T01375.
DR RefSeq; NP_001329076.1; NM_001340311.1.
DR RefSeq; NP_192051.2; NM_116372.3.
DR AlphaFoldDB; Q7FZF1; -.
DR SMR; Q7FZF1; -.
DR BioGRID; 11970; 7.
DR IntAct; Q7FZF1; 7.
DR STRING; 3702.AT4G01420.1; -.
DR iPTMnet; Q7FZF1; -.
DR PaxDb; Q7FZF1; -.
DR PRIDE; Q7FZF1; -.
DR EnsemblPlants; AT4G01420.1; AT4G01420.1; AT4G01420.
DR GeneID; 826671; -.
DR Gramene; AT4G01420.1; AT4G01420.1; AT4G01420.
DR KEGG; ath:AT4G01420; -.
DR Araport; AT4G01420; -.
DR TAIR; locus:2125162; AT4G01420.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR InParanoid; Q7FZF1; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q7FZF1; -.
DR PRO; PR:Q7FZF1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q7FZF1; baseline and differential.
DR Genevisible; Q7FZF1; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; TAS:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; 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; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR PANTHER; PTHR23056; PTHR23056; 1.
DR Pfam; PF12763; EF-hand_4; 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 Cytoplasm; Lipoprotein; Myristate; Nucleus; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..203
FT /note="Calcineurin B-like protein 5"
FT /id="PRO_0000073506"
FT DOMAIN 30..65
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 66..101
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 103..138
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 147..182
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 139
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:18502848"
SQ SEQUENCE 203 AA; 23518 MW; 853C31FB4060F548 CRC64;
MGCVCSKQLE GRRQEDISLL ASQTFFSEAE VEVLHGLFIK LTSCLSNDNL LTKEKFQFIL
IKNTKKRSLS AERIFGLFDM RNDGAIDFGE FVHTLNIFHP NSSPRDKAIF AFRLYDTRET
GFIEPEEVKE MIIDVLEESE LMLSESIIDS IVSKTFEEAD WKKDGIIDLE EWENFVATYP
LTLKNMTIPF LKDIPRIFPT FLR
