PP2B2_DROME
ID PP2B2_DROME Reviewed; 570 AA.
AC Q27889; Q26248; Q9VXF2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit 2;
DE EC=3.1.3.16;
DE AltName: Full=Calmodulin-dependent calcineurin A2 subunit;
GN Name=Pp2B-14D; ORFNames=CG9842;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Eye imaginal disk;
RX PubMed=8313960; DOI=10.1016/0014-5793(94)80398-6;
RA Brown L., Chen M.X., Cohen P.T.W.;
RT "Identification of a cDNA encoding a Drosophila calcium/calmodulin
RT regulated protein phosphatase, which has its most abundant expression in
RT the early embryo.";
RL FEBS Lett. 339:124-128(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; 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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [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, ECO:0000269|PubMed:8313960}.
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: Interacts with sra in a complex that contains CanA-14F.
CC {ECO:0000269|PubMed:16860743, ECO:0000269|PubMed:22421435}.
CC -!- INTERACTION:
CC Q27889; Q9VE19: euc; NbExp=4; IntAct=EBI-132663, EBI-9936648;
CC -!- TISSUE SPECIFICITY: Expressed in CNS and PNS.
CC {ECO:0000269|PubMed:8849894}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC embryos, larvae and adults. {ECO:0000269|PubMed:8313960,
CC ECO:0000269|PubMed:8849894}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000305}.
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DR EMBL; X77768; CAA54807.1; -; mRNA.
DR EMBL; S68806; AAB29893.1; -; mRNA.
DR EMBL; AE014298; AAF48622.1; -; Genomic_DNA.
DR EMBL; BT010083; AAQ22552.1; -; mRNA.
DR PIR; S41743; S41743.
DR PIR; S70551; S70551.
DR RefSeq; NP_001245715.1; NM_001258786.3.
DR RefSeq; NP_001245716.1; NM_001258787.2.
DR RefSeq; NP_523373.2; NM_078649.4.
DR AlphaFoldDB; Q27889; -.
DR BMRB; Q27889; -.
DR SMR; Q27889; -.
DR BioGRID; 58962; 41.
DR DIP; DIP-17529N; -.
DR IntAct; Q27889; 22.
DR STRING; 7227.FBpp0301546; -.
DR PaxDb; Q27889; -.
DR PRIDE; Q27889; -.
DR DNASU; 32624; -.
DR EnsemblMetazoa; FBtr0074294; FBpp0074069; FBgn0011826.
DR EnsemblMetazoa; FBtr0305593; FBpp0294044; FBgn0011826.
DR EnsemblMetazoa; FBtr0309793; FBpp0301546; FBgn0011826.
DR GeneID; 32624; -.
DR KEGG; dme:Dmel_CG9842; -.
DR CTD; 32624; -.
DR FlyBase; FBgn0011826; Pp2B-14D.
DR VEuPathDB; VectorBase:FBgn0011826; -.
DR eggNOG; KOG0375; Eukaryota.
DR GeneTree; ENSGT00940000154115; -.
DR HOGENOM; CLU_004962_6_0_1; -.
DR InParanoid; Q27889; -.
DR OMA; MESFCCL; -.
DR OrthoDB; 463522at2759; -.
DR PhylomeDB; Q27889; -.
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; Q27889; -.
DR BioGRID-ORCS; 32624; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32624; -.
DR PRO; PR:Q27889; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0011826; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; Q27889; baseline and differential.
DR Genevisible; Q27889; DM.
DR GO; GO:0005955; C:calcineurin complex; ISS:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; ISS:FlyBase.
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:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0051321; P:meiotic cell cycle; IGI:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:FlyBase.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:FlyBase.
DR GO; GO:0030431; P:sleep; IDA:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP: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 Protein phosphatase; Reference proteome; Zinc.
FT CHAIN 1..570
FT /note="Serine/threonine-protein phosphatase 2B catalytic
FT subunit 2"
FT /id="PRO_0000058831"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 111
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="D -> E (in Ref. 1; CAA54807)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="A -> Q (in Ref. 1; CAA54807 and 2; AAB29893)"
FT /evidence="ECO:0000305"
FT CONFLICT 323..333
FT /note="SYFYSYAACCD -> CY (in Ref. 1; CAA54807)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="Y -> I (in Ref. 1; CAA54807)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="L -> V (in Ref. 1; CAA54807)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="Missing (in Ref. 1; CAA54807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 63101 MW; 4A5429A620C0C275 CRC64;
MSSNNQSSSV AQAATSARTV SAGSAEATDA NSTASNNNNN SSSTAAAGNN SDNSSPTTGT
GTGASTGKLH GGHTAVNTKE RVVDSVPFPP SHKLTLAEVF DQRTGKPNHE LLKQHFILEG
RIEEAPALKI IQDGAALLRQ EKTMIDIEAP VTVCGDIHGQ FYDLMKLFEV GGSPASTKYL
FLGDYVDRGY FSIECVLYLW SLKITYPQTL FLLRGNHECR HLTEYFTFKQ ECKIKYSERV
YDACMDAFDC LPLAALMNQQ FLCVHGGLSP EIHELEDIRR LDRFKEPPAF GPMCDLLWSD
PLEDFGNEKN SDFYTHNSVR GCSYFYSYAA CCDFLQNNNL LSIIRAHEAQ DAGYRMYRKS
QTTGFPSLIT IFSAPNYLDV YNNKAAVLKY ENNVMNIRQF NCSPHPYWLP NFMDVFTWSL
PFVGEKVTEM LVNVLNICSD DELMTEESEE PLSDDEAALR KEVIRNKIRA IGKMARVFSV
LREESESVLQ LKGLTPTGAL PLGALSGGKQ SLKNAMQGFS PNHKITSFAE AKGLDAVNER
MPPRRDQPPT PSEDPNQHSQ QGGKNGAGHG
