CANB_YEAST
ID CANB_YEAST Reviewed; 175 AA.
AC P25296; D6VX10;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Calcineurin subunit B;
DE AltName: Full=Calcineurin regulatory subunit;
DE AltName: Full=Protein phosphatase 2B regulatory subunit;
GN Name=CNB1; Synonyms=YCN2, YCNB; OrderedLocusNames=YKL190W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=1659397; DOI=10.1016/s0006-291x(05)81188-x;
RA Kuno T., Tanaka H., Mukai H., Chang C.-D., Hiraga K., Miyakawa T.,
RA Tanaka C.;
RT "cDNA cloning of a calcineurin B homolog in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 180:1159-1163(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MYRISTOYLATION AT GLY-2.
RX PubMed=1321337; DOI=10.1128/mcb.12.8.3460-3469.1992;
RA Cyert M.S., Thorner J.;
RT "Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent
RT phosphoprotein phosphatases is required for adaptation to pheromone.";
RL Mol. Cell. Biol. 12:3460-3469(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=8394042; DOI=10.1002/yea.320090612;
RA Cheret G., Mattheakis L.C., Sor F.;
RT "DNA sequence analysis of the YCN2 region of chromosome XI in Saccharomyces
RT cerevisiae.";
RL Yeast 9:661-667(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC -!- SUBUNIT: Composed of a catalytic subunit (A) and a regulatory subunit
CC (B).
CC -!- INTERACTION:
CC P25296; P14747: CMP2; NbExp=5; IntAct=EBI-3968, EBI-12778;
CC P25296; P19880: YAP1; NbExp=2; IntAct=EBI-3968, EBI-31265;
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z26521; CAA81290.1; -; Genomic_DNA.
DR EMBL; D10293; BAA01136.1; -; mRNA.
DR EMBL; M87508; AAA34505.1; -; Genomic_DNA.
DR EMBL; X69765; CAA49421.1; -; Genomic_DNA.
DR EMBL; X74151; CAA52248.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z28190; CAA82034.1; -; Genomic_DNA.
DR EMBL; Z28189; CAA82033.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08976.1; -; Genomic_DNA.
DR PIR; JH0462; JH0462.
DR RefSeq; NP_012731.1; NM_001179756.1.
DR AlphaFoldDB; P25296; -.
DR SMR; P25296; -.
DR BioGRID; 33931; 368.
DR ComplexPortal; CPX-588; Calcineurin complex variant 1.
DR ComplexPortal; CPX-590; Calcineurin complex variant 2.
DR DIP; DIP-510N; -.
DR IntAct; P25296; 14.
DR MINT; P25296; -.
DR STRING; 4932.YKL190W; -.
DR iPTMnet; P25296; -.
DR MaxQB; P25296; -.
DR PaxDb; P25296; -.
DR PRIDE; P25296; -.
DR EnsemblFungi; YKL190W_mRNA; YKL190W; YKL190W.
DR GeneID; 853644; -.
DR KEGG; sce:YKL190W; -.
DR SGD; S000001673; CNB1.
DR VEuPathDB; FungiDB:YKL190W; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000156530; -.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; P25296; -.
DR OMA; DTNFDRD; -.
DR BioCyc; YEAST:G3O-31953-MON; -.
DR Reactome; R-SCE-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-SCE-4086398; Ca2+ pathway.
DR Reactome; R-SCE-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR PRO; PR:P25296; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P25296; protein.
DR GO; GO:0005955; C:calcineurin complex; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:SGD.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0019902; F:phosphatase binding; IBA:GO_Central.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IC:ComplexPortal.
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 1: Evidence at protein level;
KW Calcium; Lipoprotein; Metal-binding; Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..175
FT /note="Calcineurin subunit B"
FT /id="PRO_0000073498"
FT DOMAIN 21..56
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 60..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 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"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:1321337"
SQ SEQUENCE 175 AA; 19639 MW; 6E42DB350DA05BC0 CRC64;
MGAAPSKIVD GLLEDTNFDR DEIERLRKRF MKLDRDSSGS IDKNEFMSIP GVSSNPLAGR
IMEVFDADNS GDVDFQEFIT GLSIFSGRGS KDEKLRFAFK IYDIDKDGFI SNGELFIVLK
IMVGSNLDDE QLQQIVDRTI VENDSDGDGR LSFEEFKNAI ETTEVAKSLT LQYDV
