ID CNBL4_ORYSJ Reviewed; 210 AA.
AC Q75KU4; B7ERN3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Calcineurin B-like protein 4;
GN Name=CBL4; OrderedLocusNames=Os05g0534400, LOC_Os05g45810;
GN ORFNames=OJ1014_C08.4, OsJ_19333 {ECO:0000312|EMBL:EEE64483.1},
GN OSJNBa0053E05.21;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND GENE FAMILY.
RC STRAIN=cv. Nipponbare; TISSUE=Seedling;
RX PubMed=18395997; DOI=10.1016/j.gene.2008.02.011;
RA Gu Z., Ma B., Jiang Y., Chen Z., Su X., Zhang H.;
RT "Expression analysis of the calcineurin B-like gene family in rice (Oryza
RT sativa L.) under environmental stresses.";
RL Gene 415:1-12(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
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 [9]
RP SUBCELLULAR LOCATION, AND GENE FAMILY.
RX PubMed=15980189; DOI=10.1104/pp.105.062703;
RA Hwang Y.-S., Bethke P.C., Cheong Y.H., Chang H.-S., Zhu T., Jones R.L.;
RT "A gibberellin-regulated calcineurin B in rice localizes to the tonoplast
RT and is implicated in vacuole function.";
RL Plant Physiol. 138:1347-1358(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH CIPK24.
RX PubMed=17142477; DOI=10.1104/pp.106.092635;
RA Martinez-Atienza J., Jiang X., Garciadeblas B., Mendoza I., Zhu J.-K.,
RA Pardo J.M., Quintero F.J.;
RT "Conservation of the salt overly sensitive pathway in rice.";
RL Plant Physiol. 143:1001-1012(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. Operates in synergy with CIPK24 to activate the plasma
CC membrane Na(+)/H(+) antiporter SOS1. May function as positive regulator
CC of salt stress responses. CBL proteins interact with CIPK serine-
CC threonine protein kinases. Binding of a CBL protein to the regulatory
CC NAF domain of a CIPK protein lead to the activation of the kinase in a
CC calcium-dependent manner. {ECO:0000269|PubMed:17142477}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CIPK24.
CC {ECO:0000250, ECO:0000269|PubMed:17142477}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15980189};
CC Lipid-anchor {ECO:0000269|PubMed:15980189}. Note=Aleurone cells.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:18395997}.
CC -!- INDUCTION: By drought stress and abscisic acid (ABA).
CC {ECO:0000269|PubMed:18395997}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; DQ201198; ABA54179.1; -; mRNA.
DR EMBL; AC097111; AAS75223.1; -; Genomic_DNA.
DR EMBL; AC121365; AAT47091.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18062.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS95062.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64483.1; -; Genomic_DNA.
DR EMBL; AK101368; BAG95030.1; -; mRNA.
DR RefSeq; XP_015637956.1; XM_015782470.1.
DR AlphaFoldDB; Q75KU4; -.
DR SMR; Q75KU4; -.
DR BioGRID; 808469; 23.
DR STRING; 39947.Q75KU4; -.
DR PaxDb; 39947-Q75KU4; -.
DR EnsemblPlants; Os05t0534400-01; Os05t0534400-01; Os05g0534400.
DR GeneID; 4339432; -.
DR Gramene; Os05t0534400-01; Os05t0534400-01; Os05g0534400.
DR KEGG; osa:4339432; -.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR InParanoid; Q75KU4; -.
DR OMA; MCSEAND; -.
DR OrthoDB; 90710at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q75KU4; OS.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; CALCINEURIN B; 1.
DR PANTHER; PTHR23056:SF143; CALCINEURIN B-LIKE PROTEIN 8; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..210
FT /note="Calcineurin B-like protein 4"
FT /id="PRO_0000337767"
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 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 140
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 23916 MW; 47D43F6287CEC537 CRC64;
MGCASSKQFK RPPGYEEPAV LAAQTTFTVN EVEALRELYN KMSYSIIKDG LIHKEEFQLA
LFRNSRKANL FADRVFDLFD LKRNGVIEFG EFVRSLSVFH PKAPKSEKTA FAFKLYDLRG
TGYIEKEELR EMVLALLDES DLHLSECAVE AIVDNTFSQA DSNGDGRIDP EEWEEFVKAN
PASLRNMSLP YLQDITMAFP SFVMHSEAHD
//
