ID   PP2B1_YEAST             Reviewed;         553 AA.
AC   P23287; D6VZ68;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit A1;
DE            EC=3.1.3.16;
DE   AltName: Full=Calcineurin A1;
DE   AltName: Full=Calmodulin-binding protein 1;
GN   Name=CNA1; Synonyms=CMP1; OrderedLocusNames=YLR433C; ORFNames=L9753.6;
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 [GENOMIC DNA].
RC   STRAIN=S288c / GRF88;
RX   PubMed=1651503; DOI=10.1073/pnas.88.16.7376;
RA   Cyert M.S., Kunisawa R., Kaim D., Thorner J.;
RT   "Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin,
RT   a calmodulin-regulated phosphoprotein phosphatase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7376-7380(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=20B-12;
RX   PubMed=1311678; DOI=10.1111/j.1432-1033.1992.tb16686.x;
RA   Ye R.R., Bretscher A.;
RT   "Identification and molecular characterization of the calmodulin-binding
RT   subunit gene (CMP1) of protein phosphatase 2B from Saccharomyces
RT   cerevisiae. An alpha-factor inducible gene.";
RL   Eur. J. Biochem. 204:713-723(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1646387; DOI=10.1007/bf00260706;
RA   Liu Y., Ishii S., Tokai M., Tsutsumi H., Ohki O., Akada R., Tanaka K.,
RA   Tsuchiya E., Fukui S., Miyakawa T.;
RT   "The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-
RT   binding proteins homologous to the catalytic subunit of mammalian protein
RT   phosphatase 2B.";
RL   Mol. Gen. Genet. 227:52-59(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [5]
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).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase.
CC       This subunit may have a role in the calmodulin activation of
CC       calcineurin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Composed of two components (A and B), the A component is the
CC       catalytic subunit and the B component confers calcium sensitivity.
CC   -!- INTERACTION:
CC       P23287; P06787: CMD1; NbExp=4; IntAct=EBI-12771, EBI-3976;
CC   -!- MISCELLANEOUS: Present with 7040 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M64839; AAA34465.1; -; Genomic_DNA.
DR   EMBL; X66490; CAA47117.1; -; Genomic_DNA.
DR   EMBL; X54963; CAA38711.1; -; Genomic_DNA.
DR   EMBL; U21094; AAB67518.1; -; Genomic_DNA.
DR   EMBL; AY693079; AAT93098.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09734.1; -; Genomic_DNA.
DR   PIR; S16809; S16809.
DR   RefSeq; NP_013537.1; NM_001182321.1.
DR   PDB; 2LHI; NMR; -; A=453-476.
DR   PDBsum; 2LHI; -.
DR   AlphaFoldDB; P23287; -.
DR   SMR; P23287; -.
DR   BioGRID; 31692; 124.
DR   ComplexPortal; CPX-588; Calcineurin complex variant 1.
DR   DIP; DIP-662N; -.
DR   IntAct; P23287; 26.
DR   MINT; P23287; -.
DR   STRING; 4932.YLR433C; -.
DR   iPTMnet; P23287; -.
DR   MaxQB; P23287; -.
DR   PaxDb; 4932-YLR433C; -.
DR   PeptideAtlas; P23287; -.
DR   EnsemblFungi; YLR433C_mRNA; YLR433C; YLR433C.
DR   GeneID; 851153; -.
DR   KEGG; sce:YLR433C; -.
DR   AGR; SGD:S000004425; -.
DR   SGD; S000004425; CNA1.
DR   VEuPathDB; FungiDB:YLR433C; -.
DR   eggNOG; KOG0375; Eukaryota.
DR   GeneTree; ENSGT00940000176583; -.
DR   HOGENOM; CLU_004962_6_2_1; -.
DR   InParanoid; P23287; -.
DR   OMA; YPAACNF; -.
DR   OrthoDB; 1488111at2759; -.
DR   BioCyc; YEAST:G3O-32491-MONOMER; -.
DR   BioGRID-ORCS; 851153; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P23287; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P23287; Protein.
DR   GO; GO:0005955; C:calcineurin complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR   GO; GO:0071444; P:cellular response to pheromone; IMP:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR   GO; GO:0006873; P:intracellular monoatomic ion homeostasis; IMP:SGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; NAS:ComplexPortal.
DR   CDD; cd07416; MPP_PP2B; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041751; MPP_PP2B.
DR   InterPro; IPR043360; PP2B.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR   PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calmodulin-binding; Hydrolase; Iron;
KW   Metal-binding; Protein phosphatase; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..553
FT                   /note="Serine/threonine-protein phosphatase 2B catalytic
FT                   subunit A1"
FT                   /id="PRO_0000058836"
FT   REGION          413..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   VARIANT         45..46
FT                   /note="PI -> SY (in strain: S288c / GRF88)"
FT   HELIX           455..458
FT                   /evidence="ECO:0007829|PDB:2LHI"
FT   HELIX           460..474
FT                   /evidence="ECO:0007829|PDB:2LHI"
SQ   SEQUENCE   553 AA;  63002 MW;  D5D6F91CC0BD277B CRC64;
     MSKDLNSSRI KIIKPNDSYI KVDRKKDLTK YELENGKVIS TKDRPIASVP AITGKIPSDE
     EVFDSKTGLP NHSFLREHFF HEGRLSKEQA IKILNMSTVA LSKEPNLLKL KAPITICGDI
     HGQYYDLLKL FEVGGDPAEI DYLFLGDYVD RGAFSFECLI YLYSLKLNNL GRFWMLRGNH
     ECKHLTSYFT FKNEMLHKYD MEVYDACCRS FNVLPLAALM NGQYFCVHGG ISPELKSVED
     VNKINRFREI PSRGLMCDLL WADPVENYDD ARDGSEFDQS EDEFVPNSLR GCSFAFTFKA
     SCKFLKANGL LSIIRAHEAQ DAGYRMYKNN KVTGFPSLIT MFSAPNYLDT YHNKAAVLKY
     EENVMNIRQF HMSPHPYWLP DFMDVFTWSL PFVGEKVTSM LVSILNICSE QELDPESEPK
     AAEETVKARA NATKETGTPS DEKASSAILE DETRRKALRN KILAIAKVSR MFSVLREESE
     KVEYLKTMNA GVLPRGALAR GTEGLNETLS TFEKARKEDL INEKLPPSLS EVEQEKIKYY
     EKILKGAEKK PQL
//