ID M1BQA1_SOLTU Unreviewed; 194 AA.
AC M1BQA1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Calcineurin B-like protein {ECO:0000256|RuleBase:RU369080};
GN Name=102598672 {ECO:0000313|EnsemblPlants:PGSC0003DMT400050431};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400050431, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400050431}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400050431};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 AlphaFoldDB; M1BQA1; -.
DR EnsemblPlants; PGSC0003DMT400050431; PGSC0003DMT400050431; PGSC0003DMG400019601.
DR Gramene; PGSC0003DMT400050431; PGSC0003DMT400050431; PGSC0003DMG400019601.
DR HOGENOM; CLU_061288_21_0_1; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1BQA1; 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:SF147; CALCINEURIN B-LIKE PROTEIN; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 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 Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369080}.
FT DOMAIN 68..103
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 105..140
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 149..184
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 194 AA; 22467 MW; 36AEC983A492A77D CRC64;
MGCFHSKTTL HYTPGYEEPT VLAAETPFTV REVEALYELF KRISSCIIDD GLIHKEEFQL
ALFRNQKMKN LFADRIFDLF DIKRNGVIEF GDFVRSLGIF HPNAPVADKM SFAFRLYDLR
HTGYIEREEL KEMVLALLHE SELVLSDDVV EIIVDETFSD ADTKGDGRID SEEWKEFVSK
NPSLLKNMTL PYLM
//
