CNBL8_ORYSJ
ID CNBL8_ORYSJ Reviewed; 213 AA.
AC Q3HRN9; A0A0P0VHT1; Q6K870;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Calcineurin B-like protein 8;
GN Name=CBL8; OrderedLocusNames=Os02g0291400, LOC_Os02g18930;
GN ORFNames=OJ1124_E11.15;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP 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=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 [3]
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 [4]
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 [5]
RP 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).
CC -!- FUNCTION: Acts as a calcium sensor. 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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:18395997}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:18395997};
CC Lipid-anchor {ECO:0000305|PubMed:18395997}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, shoots, culms,
CC leaves and young spikelets. {ECO:0000269|PubMed:18395997}.
CC -!- INDUCTION: By drought and cold stresses, and abscisic acid (ABA).
CC {ECO:0000269|PubMed:18395997}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21759.1; 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; DQ201202; ABA54183.1; -; mRNA.
DR EMBL; AP004229; BAD21759.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS78194.1; -; Genomic_DNA.
DR RefSeq; XP_015623984.1; XM_015768498.1.
DR RefSeq; XP_015623985.1; XM_015768499.1.
DR AlphaFoldDB; Q3HRN9; -.
DR SMR; Q3HRN9; -.
DR STRING; 4530.OS02T0291400-00; -.
DR PaxDb; Q3HRN9; -.
DR PRIDE; Q3HRN9; -.
DR EnsemblPlants; Os02t0291400-00; Os02t0291400-00; Os02g0291400.
DR GeneID; 107276173; -.
DR Gramene; Os02t0291400-00; Os02t0291400-00; Os02g0291400.
DR KEGG; osa:107276173; -.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_21_0_1; -.
DR InParanoid; Q3HRN9; -.
DR OMA; PDEWKTF; -.
DR OrthoDB; 1271942at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q3HRN9; 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 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; PF13202; EF-hand_5; 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 2: Evidence at transcript 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..213
FT /note="Calcineurin B-like protein 8"
FT /id="PRO_0000337771"
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 213 AA; 24491 MW; 37EC565663E79CEF CRC64;
MGCVSSKQFK RAAQHEDPAI LAKETTFSVS EVEALFELFK KISHSIFRDG LIHKEEFQLA
LFRNSNKKNL FANRIFDLFD LKRNGVIDFG EFVRSLSIFH PETPLGDKIA FAFRLYDLRG
TGCIEREELH EMVLALLNES DLFLSEEAVE QIVDQTFKQA DLNDDGKIDP DEWKTFASKN
PALLKNMTLP YLKDITMVFP SFILNSEVCE EEL
