ID A0A443PR84_9MAGN Unreviewed; 231 AA.
AC A0A443PR84;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Calcineurin B-like protein {ECO:0000256|RuleBase:RU369080};
GN ORFNames=CKAN_02253800 {ECO:0000313|EMBL:RWR93294.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR93294.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR93294.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR93294.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR93294.1}.
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DR EMBL; QPKB01000010; RWR93294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443PR84; -.
DR STRING; 337451.A0A443PR84; -.
DR Proteomes; UP000283530; 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:SF108; 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; 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:UP000283530};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369080}.
FT DOMAIN 73..108
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 110..145
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 154..189
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 231 AA; 26816 MW; 1852438C7145AD9C CRC64;
MGCTWGKRLI SCIWTKRRHQ YEDPAVLAAE TCFSVREVEA LYELFRKLSC SLSNDGLISK
EEFQLGLFRD RKKQNLFADR IFYLFDDNQD GLIDFGEFIR SLSIFHPNSP EADKITFAYR
MYDIRQTGFI EREEVKEMLL ALLNESEIIL SDDIVEDILD KTFAEADSKT DGKIDQEEWK
EFVLRNPSIM RNMTIPYLKD ITTSFPSFAL REKAGGSDID ESLINTRNGT N
//
