ID A0A067KAT8_JATCU Unreviewed; 218 AA.
AC A0A067KAT8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Calcineurin B-like protein {ECO:0000256|RuleBase:RU369080};
GN ORFNames=JCGZ_19369 {ECO:0000313|EMBL:KDP28939.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP28939.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP28939.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP28939.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
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; KK914780; KDP28939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067KAT8; -.
DR STRING; 180498.A0A067KAT8; -.
DR Proteomes; UP000027138; 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; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23056; CALCINEURIN B; 1.
DR PANTHER; PTHR23056:SF116; CALCINEURIN B-LIKE PROTEIN 2; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13833; EF-hand_8; 1.
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, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU369080};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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 155..190
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 218 AA; 25176 MW; F039D7E94BC666CE CRC64;
MYVIVVIAIR SMVVFSLKIV AFLTLYAVSV SEIEALYELF KKISSAVIDD GLINKEEFQL
ALFKTNKKES LFADRVFDLF DTKHNGILGF EEFARALSVF HPNAPIDDKI EFSFQLYDLK
QQGFIERQEF FNFLCIEQMV VATRAESGMN LSDDVIESII DKTFEEADTK HDGKIDKEEW
RSLVIRHPSL LKNMTLQYLK DITTTFPSFV FHSQVDDT
//
