CANB_KLULA
ID CANB_KLULA Reviewed; 175 AA.
AC Q874T7;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Calcineurin subunit B;
DE AltName: Full=Calcineurin regulatory subunit;
DE AltName: Full=Protein phosphatase 2B regulatory subunit;
GN Name=CNB1; OrderedLocusNames=KLLA0D02992g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RA Palleschi C., Farina F., Uccelletti D.;
RT "The KlCNB1 gene of Kluyveromyces lactis encodes for calcineurin.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Composed of a catalytic subunit (A) and a regulatory subunit
CC (B). {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; AJ428419; CAD21467.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00297.1; -; Genomic_DNA.
DR RefSeq; XP_453201.1; XM_453201.1.
DR AlphaFoldDB; Q874T7; -.
DR SMR; Q874T7; -.
DR STRING; 28985.XP_453201.1; -.
DR EnsemblFungi; CAH00297; CAH00297; KLLA0_D02992g.
DR GeneID; 2892802; -.
DR KEGG; kla:KLLA0_D02992g; -.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; Q874T7; -.
DR OMA; DTNFDRD; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005955; C:calcineurin complex; IEA:EnsemblFungi.
DR GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IEA:EnsemblFungi.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0006873; P:cellular ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:EnsemblFungi.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR015757; Calcineur_B.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR45942; PTHR45942; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 3: Inferred from homology;
KW Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..175
FT /note="Calcineurin subunit B"
FT /id="PRO_0000073494"
FT DOMAIN 21..56
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 58..88
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 90..125
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 131..166
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 175 AA; 19768 MW; F852D8A7AB4C6886 CRC64;
MGAAPSRIVD NLLDDTNFDR AEIERLKKRF MKLDKDSSGS IDKTEFMSIP GVSANPLAKR
IIEVFDEDNS GDVDFQEFIT SLSIFSGRGE TDAKLRFAFR IYDIDKDGYI SNGELFIVLK
IMVGTNLEDE QLQQIVDRTI MENDVDGDGK LSFEEFKKAA ETTEVIQSLT LQHNI
