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Database: UniProt
Entry: A0A1D6NLC2_MAIZE
LinkDB: A0A1D6NLC2_MAIZE
Original site: A0A1D6NLC2_MAIZE 
ID   A0A1D6NLC2_MAIZE        Unreviewed;       236 AA.
AC   A0A1D6NLC2;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Calcineurin B-like protein {ECO:0000256|RuleBase:RU369080};
GN   ORFNames=ZEAMMB73_Zm00001d044389 {ECO:0000313|EMBL:ONM41025.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM41025.1};
RN   [1] {ECO:0000313|EMBL:ONM41025.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM41025.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU369080}.
CC   -!- SUBUNIT: Homodimer. Interacts with CIPK.
CC       {ECO:0000256|RuleBase:RU369080}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU369080}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       {ECO:0000256|ARBA:ARBA00023774, ECO:0000256|RuleBase:RU369080}.
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DR   EMBL; CM007649; ONM41025.1; -; Genomic_DNA.
DR   RefSeq; XP_008673401.1; XM_008675179.1.
DR   AlphaFoldDB; A0A1D6NLC2; -.
DR   SMR; A0A1D6NLC2; -.
DR   IntAct; A0A1D6NLC2; 17.
DR   STRING; 4577.A0A1D6NLC2; -.
DR   GeneID; 101027228; -.
DR   InParanoid; A0A1D6NLC2; -.
DR   OrthoDB; 339700at2759; -.
DR   ExpressionAtlas; A0A1D6NLC2; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019900; F:kinase binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEA:UniProtKB-UniRule.
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; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23056; CALCINEURIN B; 1.
DR   PANTHER; PTHR23056:SF88; CALCINEURIN B-LIKE PROTEIN 5; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU369080};
KW   Membrane {ECO:0000256|RuleBase:RU369080};
KW   Metal-binding {ECO:0000256|RuleBase:RU369080};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369080}.
SQ   SEQUENCE   236 AA;  26993 MW;  CECA745FDBBFABD0 CRC64;
     MGCLQTKHAS RSPHLLDTRE AVALAAETSC EKVDLPDFVN IATGTLRLTV SEVEALHDLF
     RKISNSVIRD NLIHKEEFQL ALFRGKKQQN LFVDRVFDLF DQKRNGVIEF GEFVRSLGVF
     HPDAPEDQKV AFAFKLYDLK QTGFIERHEL KEMVLALLDE SDLDIASDAV EMIVDRTFDQ
     ADTKGDGKID QEEWTEYAKD NPYVLRNMTL PYLKDITMVF PSFVMHSEIS ETDMAV
//
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