CANB_CRYNJ
ID CANB_CRYNJ Reviewed; 175 AA.
AC P0CM54; Q55T57; Q5KJ85; Q9HDD3; Q9HDE1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Calcineurin subunit B;
DE AltName: Full=Calcineurin regulatory subunit;
DE AltName: Full=Protein phosphatase 2B regulatory subunit;
GN Name=CNB1; OrderedLocusNames=CND00260;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT FKR1-1 VAL-GLN-128 INS,
RP AND FUNCTION.
RC STRAIN=C21F2, and JEC21 / ATCC MYA-565;
RX PubMed=11251806; DOI=10.1046/j.1365-2958.2001.02295.x;
RA Fox D.S., Cruz M.C., Sia R.A., Ke H., Cox G.M., Cardenas M.E., Heitman J.;
RT "Calcineurin regulatory subunit is essential for virulence and mediates
RT interactions with FKBP12-FK506 in Cryptococcus neoformans.";
RL Mol. Microbiol. 39:835-849(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC Plays a central role in virulence and antifungal drug action.
CC {ECO:0000269|PubMed:11251806}.
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; AF282388; AAG13937.1; -; Genomic_DNA.
DR EMBL; AF282387; AAG13936.1; -; mRNA.
DR EMBL; AF282386; AAG13935.1; -; Genomic_DNA.
DR EMBL; AF282385; AAG13934.1; -; mRNA.
DR EMBL; AE017344; AAW43026.1; -; Genomic_DNA.
DR RefSeq; XP_570333.1; XM_570333.1.
DR AlphaFoldDB; P0CM54; -.
DR SMR; P0CM54; -.
DR STRING; 5207.AAW43026; -.
DR PaxDb; P0CM54; -.
DR EnsemblFungi; AAW43026; AAW43026; CND00260.
DR VEuPathDB; FungiDB:CND00260; -.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; P0CM54; -.
DR OMA; DTNFDRD; -.
DR OrthoDB; 1271942at2759; -.
DR PHI-base; PHI:474; -.
DR Proteomes; UP000002149; Chromosome 4.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
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; 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; IEA:EnsemblFungi.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
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:0006470; P:protein dephosphorylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Metal-binding; Reference proteome; Repeat; Virulence.
FT CHAIN 1..175
FT /note="Calcineurin subunit B"
FT /id="PRO_0000073492"
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 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"
FT VARIANT 128
FT /note="K -> KVQ (in FKR1-1; FK506-resistant)"
FT /evidence="ECO:0000269|PubMed:11251806"
SQ SEQUENCE 175 AA; 19678 MW; EC8CB3CE3A9063AB CRC64;
MGAAESSMFN SLEKNSNFSG PELMRLKKRF MKLDKDGSGS IDKDEFLQIP QIANNPLAHR
MIAIFDEDGS GTVDFQEFVG GLSAFSSKGG RDEKLRFAFK VYDMDRDGYI SNGELYLVLK
QMVGNNLKDQ QLQQIVDKTI MEADKDGDGK LSFEEFTQMV ASTDIVKQMT LEDLF
