ID   PP2B2_YEAST             Reviewed;         604 AA.
AC   P14747; D6VZB7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   27-MAR-2024, entry version 211.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit A2;
DE            EC=3.1.3.16;
DE   AltName: Full=Calcineurin A2;
DE   AltName: Full=Calmodulin-binding protein 2;
GN   Name=CMP2; Synonyms=CNA2; OrderedLocusNames=YML057W;
GN   ORFNames=YM9958.05;
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].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 100-604.
RX   PubMed=2557079; DOI=10.1016/0167-4781(89)90118-8;
RA   da Cruz e Silva E.F., Cohen P.T.W.;
RT   "Isolation of a cDNA likely to encode a novel Ca2+-dependent/calmodulin-
RT   stimulated protein phosphatase.";
RL   Biochim. Biophys. Acta 1009:293-296(1989).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
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       P14747; P25296: CNB1; NbExp=5; IntAct=EBI-12778, EBI-3968;
CC   -!- MISCELLANEOUS: Present with 7110 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}.
CC   -!- CAUTION: Was originally thought to originate from a rabbit cDNA library
CC       and was known as protein phosphatase 2Bw (PP2Bw).
CC       {ECO:0000305|PubMed:2557079}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M64840; AAA34466.1; -; Genomic_DNA.
DR   EMBL; X16804; CAA34722.1; -; mRNA.
DR   EMBL; Z46729; CAA86718.1; -; Genomic_DNA.
DR   EMBL; X54964; CAA38712.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09841.1; -; Genomic_DNA.
DR   PIR; S49804; S49804.
DR   RefSeq; NP_013655.1; NM_001182415.1.
DR   AlphaFoldDB; P14747; -.
DR   SMR; P14747; -.
DR   BioGRID; 35110; 137.
DR   ComplexPortal; CPX-590; Calcineurin complex variant 2.
DR   DIP; DIP-833N; -.
DR   IntAct; P14747; 28.
DR   MINT; P14747; -.
DR   STRING; 4932.YML057W; -.
DR   iPTMnet; P14747; -.
DR   MaxQB; P14747; -.
DR   PaxDb; 4932-YML057W; -.
DR   PeptideAtlas; P14747; -.
DR   TopDownProteomics; P14747; -.
DR   EnsemblFungi; YML057W_mRNA; YML057W; YML057W.
DR   GeneID; 854946; -.
DR   KEGG; sce:YML057W; -.
DR   AGR; SGD:S000004521; -.
DR   SGD; S000004521; CMP2.
DR   VEuPathDB; FungiDB:YML057W; -.
DR   eggNOG; KOG0375; Eukaryota.
DR   GeneTree; ENSGT00940000176583; -.
DR   HOGENOM; CLU_004962_6_2_1; -.
DR   InParanoid; P14747; -.
DR   OMA; PSHGLMC; -.
DR   OrthoDB; 1488111at2759; -.
DR   BioCyc; YEAST:G3O-32652-MONOMER; -.
DR   BioGRID-ORCS; 854946; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P14747; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P14747; Protein.
DR   GO; GO:0005955; C:calcineurin complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
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; IBA:GO_Central.
DR   GO; GO:0006873; P:intracellular monoatomic ion homeostasis; IMP:SGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; EXP: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   Calmodulin-binding; Hydrolase; Iron; Metal-binding; Phosphoprotein;
KW   Protein phosphatase; Reference proteome; Zinc.
FT   CHAIN           1..604
FT                   /note="Serine/threonine-protein phosphatase 2B catalytic
FT                   subunit A2"
FT                   /id="PRO_0000058837"
FT   REGION          21..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..523
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         31
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        87..88
FT                   /note="EL -> DV (in Ref. 2; CAA38712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        581
FT                   /note="N -> K (in Ref. 5; CAA34722)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   604 AA;  68528 MW;  4A605598FD04207F CRC64;
     MSSDAIRNTE QINAAIKIIE NKTERPQSST TPIDSKASTV AAANSTATET SRDLTQYTLD
     DGRVVSTNRR IMNKVPAITS HVPTDEELFQ PNGIPRHEFL RDHFKREGKL SAAQAARIVT
     LATELFSKEP NLISVPAPIT VCGDIHGQYF DLLKLFEVGG DPATTSYLFL GDYVDRGSFS
     FECLIYLYSL KLNFNDHFWL LRGNHECKHL TSYFTFKNEM LHKYNLDIYE KCCESFNNLP
     LAALMNGQYL CVHGGISPEL NSLQDINNLN RFREIPSHGL MCDLLWADPI EEYDEVLDKD
     LTEEDIVNSK TMVPHHGKMA PSRDMFVPNS VRGCSYAFTY RAACHFLQET GLLSIIRAHE
     AQDAGYRMYK NTKTLGFPSL LTLFSAPNYL DTYNNKAAIL KYENNVMNIR QFNMTPHPYW
     LPDFMDVFTW SLPFVGEKVT EMLVAILNIC TEDELENDTP VIEELVGTDK KLPQAGKSEA
     TPQPATSASP KHASILDDEH RRKALRNKIL AVAKVSRMYS VLREETNKVQ FLKDHNSGVL
     PRGALSNGVK GLDEALSTFE RARKHDLINE KLPPSLDELK NENKKYYEKV WQKVHEHDAK
     NDSK
//