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Database: UniProt
Entry: W1P6F9_AMBTC
LinkDB: W1P6F9_AMBTC
Original site: W1P6F9_AMBTC 
ID   W1P6F9_AMBTC            Unreviewed;        83 AA.
AC   W1P6F9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Calcineurin B-like protein {ECO:0000256|RuleBase:RU369080};
GN   ORFNames=AMTR_s00003p00187870 {ECO:0000313|EMBL:ERN03244.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN03244.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
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; KI394358; ERN03244.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1P6F9; -.
DR   STRING; 13333.W1P6F9; -.
DR   EnsemblPlants; ERN03244; ERN03244; AMTR_s00003p00187870.
DR   Gramene; ERN03244; ERN03244; AMTR_s00003p00187870.
DR   eggNOG; KOG0034; Eukaryota.
DR   HOGENOM; CLU_061288_21_4_1; -.
DR   OMA; EVTNDYF; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
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   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; 1.
DR   SMART; SM00054; EFh; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU369080};
KW   Membrane {ECO:0000256|RuleBase:RU369080};
KW   Metal-binding {ECO:0000256|RuleBase:RU369080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369080}.
FT   DOMAIN          21..56
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   83 AA;  9515 MW;  5B71F281913677E9 CRC64;
     MVKEMVLALL NESDMSLSDD IIEAIVDKTF IDADSNGDGK IDREEWKAFV ARNPSSMKIM
     TVPYFDCKQL PLEVTNDYFD YLN
//
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