ID PP2B3_DROME Reviewed; 584 AA. AC Q9VXF1; Q27573; Q86NL0; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 4. DT 27-MAR-2024, entry version 167. DE RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit 3; DE EC=3.1.3.16; DE AltName: Full=Calmodulin-dependent calcineurin A3 subunit; GN Name=CanA-14F {ECO:0000312|EMBL:AAF48623.4, GN ECO:0000312|FlyBase:FBgn0267912}; GN Synonyms=CnnA14D {ECO:0000303|PubMed:8849894}; ORFNames=CG9819; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC47079.1} RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S {ECO:0000312|EMBL:AAC47079.1}; RX PubMed=8849894; DOI=10.1093/genetics/142.3.879; RA Hong C.-S., Ganetzky B.; RT "Molecular characterization of neurally expressing genes in the para sodium RT channel gene cluster of Drosophila."; RL Genetics 142:879-892(1996). RN [2] {ECO:0000312|EMBL:AAF48623.4} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF48623.4} RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000312|EMBL:AAO45220.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO45220.1}; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH SRA. RX PubMed=16860743; DOI=10.1016/j.cub.2006.05.058; RA Takeo S., Tsuda M., Akahori S., Matsuo T., Aigaki T.; RT "The calcineurin regulator sra plays an essential role in female meiosis in RT Drosophila."; RL Curr. Biol. 16:1435-1440(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). RN [7] RP INTERACTION WITH SRA. RX PubMed=22421435; DOI=10.1073/pnas.1120367109; RA Takeo S., Swanson S.K., Nandanan K., Nakai Y., Aigaki T., Washburn M.P., RA Florens L., Hawley R.S.; RT "Shaggy/glycogen synthase kinase 3beta and phosphorylation of RT Sarah/regulator of calcineurin are essential for completion of Drosophila RT female meiosis."; RL Proc. Natl. Acad. Sci. U.S.A. 109:6382-6389(2012). CC -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. CC This subunit may have a role in the calmodulin activation of CC calcineurin. {ECO:0000269|PubMed:16860743}. 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; CC Evidence={ECO:0000250|UniProtKB:Q08209}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q08209}; CC -!- SUBUNIT: Interacts with sra in a complex that contains Pp2B-14D. CC {ECO:0000269|PubMed:16860743, ECO:0000269|PubMed:22421435}. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in CC embryos, larvae and adults. {ECO:0000269|PubMed:8849894}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily. CC {ECO:0000255}. 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; U30493; AAC47079.1; -; mRNA. DR EMBL; AE014298; AAF48623.4; -; Genomic_DNA. DR EMBL; AE014298; AAN09410.2; -; Genomic_DNA. DR EMBL; BT004864; AAO45220.1; -; mRNA. DR PIR; S70554; S70554. DR RefSeq; NP_001245717.1; NM_001258788.2. DR RefSeq; NP_001259622.1; NM_001272693.2. DR RefSeq; NP_727985.2; NM_167523.3. DR RefSeq; NP_727986.2; NM_167524.3. DR AlphaFoldDB; Q9VXF1; -. DR SMR; Q9VXF1; -. DR BioGRID; 1073112; 4. DR STRING; 7227.FBpp0293728; -. DR iPTMnet; Q9VXF1; -. DR PaxDb; 7227-FBpp0293728; -. DR DNASU; 8674098; -. DR EnsemblMetazoa; FBtr0074292; FBpp0074067; FBgn0267912. DR EnsemblMetazoa; FBtr0074293; FBpp0074068; FBgn0267912. DR EnsemblMetazoa; FBtr0305198; FBpp0293728; FBgn0267912. DR EnsemblMetazoa; FBtr0332870; FBpp0305092; FBgn0267912. DR GeneID; 8674098; -. DR KEGG; dme:Dmel_CG9819; -. DR AGR; FB:FBgn0267912; -. DR CTD; 8674098; -. DR FlyBase; FBgn0267912; CanA-14F. DR VEuPathDB; VectorBase:FBgn0267912; -. DR eggNOG; KOG0375; Eukaryota. DR GeneTree; ENSGT00940000154115; -. DR HOGENOM; CLU_004962_6_0_1; -. DR InParanoid; Q9VXF1; -. DR OMA; KTTGFPA; -. DR OrthoDB; 1488111at2759; -. DR PhylomeDB; Q9VXF1; -. DR Reactome; R-DME-2025928; Calcineurin activates NFAT. DR Reactome; R-DME-2871809; FCERI mediated Ca+2 mobilization. DR Reactome; R-DME-4086398; Ca2+ pathway. DR Reactome; R-DME-5607763; CLEC7A (Dectin-1) induces NFAT activation. DR SignaLink; Q9VXF1; -. DR BioGRID-ORCS; 8674098; 0 hits in 3 CRISPR screens. DR ChiTaRS; CanA-14F; fly. DR GenomeRNAi; 8674098; -. DR PRO; PR:Q9VXF1; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0267912; Expressed in brain and 26 other cell types or tissues. DR ExpressionAtlas; Q9VXF1; baseline and differential. DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central. 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; IMP:UniProtKB. 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:0004722; F:protein serine/threonine phosphatase activity; ISS:FlyBase. DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central. DR GO; GO:0030431; P:sleep; IDA:FlyBase. 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. DR Genevisible; Q9VXF1; DM. PE 1: Evidence at protein level; KW Calcium; Calmodulin-binding; Hydrolase; Iron; Metal-binding; KW Phosphoprotein; Protein phosphatase; Reference proteome; Zinc. FT CHAIN 1..584 FT /note="Serine/threonine-protein phosphatase 2B catalytic FT subunit 3" FT /id="PRO_0000308356" FT REGION 1..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 546..584 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..84 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 225 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q08209" FT BINDING 164 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250|UniProtKB:Q08209" FT BINDING 166 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250|UniProtKB:Q08209" FT BINDING 192 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250|UniProtKB:Q08209" FT BINDING 192 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q08209" FT BINDING 224 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q08209" FT BINDING 273 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q08209" FT BINDING 355 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q08209" FT MOD_RES 61 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18327897" FT CONFLICT 555..584 FT /note="ATPSPAEEGQKSLSAAAAAAANANANSING -> QPPTPSEDPNQHSQQGGK FT NGAGHG (in Ref. 1; AAC47079)" FT /evidence="ECO:0000305" SQ SEQUENCE 584 AA; 64285 MW; B9428CE90283984C CRC64; MSSPAAQSNS SSSQSQSAAQ QQQQQNQKAN VNNTHDNKNA AATTGTAAGS GSGGAAGSAG TQQQGQGGTG TSSGPSSPTK RSTISTKERV IDSVAFPPSR KLTCADVFDA RTGKPQHDVL KQHFILEGRI EESAALRIIQ EGATLLRTEK TMIDIEAPVT VCGDIHGQFY DLMKLFEIGG SPATTKYLFL GDYVDRGYFS IECVLYLWSL KITYPQTLFL LRGNHECRHL TEYFTFKQEC KIKYSERVYD ACMDAFDCLP LAALMNQQFL CVHGGLSPEI HELEDIRRLD RFKEPPAFGP MCDLLWSDPL EDFGNEKNSD FYTHNSVRGC SYFYSYAACC DFLQNNNLLS IIRAHEAQDA GYRMYRKSQT TGFPSLITIF SAPNYLDVYN NKAAVLKYEN NVMNIRQFNC SPHPYWLPNF MDVFTWSLPF VGEKVTEMLV NVLNICSDDE LMTEESEEPL SDDEAALRKE VIRNKIRAIG KMARVFSVLR EESESVLQLK GLTPTGALPL GALSGGKQSL KNAMQGFSPN HKITSFAEAK GLDAVNERMP PRRDATPSPA EEGQKSLSAA AAAAANANAN SING //