PP2B3_DROME
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 03-AUG-2022, entry version 160.
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}.
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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; Q9VXF1; -.
DR PRIDE; Q9VXF1; -.
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 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; CAFLQAN; -.
DR OrthoDB; 463522at2759; -.
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 tissues.
DR ExpressionAtlas; Q9VXF1; baseline and differential.
DR Genevisible; Q9VXF1; DM.
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; 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 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
