PP2B1_YEAST
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 03-AUG-2022, entry version 192.
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; 121.
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; P23287; -.
DR PRIDE; P23287; -.
DR EnsemblFungi; YLR433C_mRNA; YLR433C; YLR433C.
DR GeneID; 851153; -.
DR KEGG; sce:YLR433C; -.
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; MESFCCL; -.
DR BioCyc; YEAST:G3O-32491-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: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: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: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 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
