ID A0A0E0FNH4_ORYNI Unreviewed; 298 AA.
AC A0A0E0FNH4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 28-JUN-2023, entry version 23.
DE RecName: Full=Calcineurin B-like protein {ECO:0000256|RuleBase:RU369080};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA01G23070.2};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA01G23070.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G23070.2};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA01G23070.2}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G23070.2};
RG EnsemblPlants;
RL Submitted (APR-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; A0A0E0FNH4; -.
DR EnsemblPlants; ONIVA01G23070.2; ONIVA01G23070.2; ONIVA01G23070.
DR Gramene; ONIVA01G23070.2; ONIVA01G23070.2; ONIVA01G23070.
DR Proteomes; UP000006591; 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 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:SF26; CALCINEURIN B-LIKE PROTEIN 10; 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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
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:UP000006591};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369080}.
FT DOMAIN 152..187
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 189..224
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 233..268
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 298 AA; 33681 MW; 7BE79D5EF0F54B93 CRC64;
MESGYGFRFS DDDVESASSL TVGERLCAAF LPFVAIAEAV FFALTDCLAD LLPPSTATAA
SRHRRSAASS YLAAVAKKWN NHQNQQRGRV GIGCTSLTLR QLARLADESR CFSVNEVEAL
FELYKKISCS IIDDGLIHKE ELQLALFKTP SGQNLFLDRV FDLFDEKKNG VIEFDEFIHA
LSVFHPLAPL EDKINFAFRL YDLRQTGFIE REEVMQMVIA ILTESDMKLS EELLEAIIDK
TFEDADADRD GKINQQEWKE FVLRHPNLLK NMTLPYLRDI TTVFPSFVFN TADSGAKE
//
