PP2B2_YEAST
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 03-AUG-2022, entry version 203.
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; 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}.
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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; 135.
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; P14747; -.
DR PRIDE; P14747; -.
DR TopDownProteomics; P14747; -.
DR EnsemblFungi; YML057W_mRNA; YML057W; YML057W.
DR GeneID; 854946; -.
DR KEGG; sce:YML057W; -.
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; TNRRIMN; -.
DR BioCyc; YEAST:G3O-32652-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: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: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; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IC: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; PTHR45673; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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
