PP2B1_DROME
ID PP2B1_DROME Reviewed; 622 AA.
AC P48456; Q8MQN3; Q9TY69; Q9VA20;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit 1;
DE EC=3.1.3.16;
DE AltName: Full=Calmodulin-dependent calcineurin A1 subunit;
GN Name=CanA1; Synonyms=CNA1, PpD14; ORFNames=CG1455;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-622.
RX PubMed=1331060; DOI=10.1016/s0021-9258(18)41706-1;
RA Guerini D., Montell C., Klee C.B.;
RT "Molecular cloning and characterization of the genes encoding the two
RT subunits of Drosophila melanogaster calcineurin.";
RL J. Biol. Chem. 267:22542-22549(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-157.
RX PubMed=1321058; DOI=10.1016/0014-5793(92)80836-6;
RA Chen M.X., Chen Y.H., Cohen P.T.W.;
RT "Polymerase chain reactions using Saccharomyces, Drosophila and human DNA
RT predict a large family of protein serine/threonine phosphatases.";
RL FEBS Lett. 306:54-58(1992).
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 -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28410.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF57105.3; -; Genomic_DNA.
DR EMBL; AY128480; AAM75073.1; -; mRNA.
DR EMBL; M97012; AAA28410.1; ALT_INIT; mRNA.
DR EMBL; S39996; AAB22466.1; -; Genomic_DNA.
DR PIR; B44307; B44307.
DR RefSeq; NP_001247378.2; NM_001260449.2.
DR RefSeq; NP_524600.3; NM_079861.4.
DR AlphaFoldDB; P48456; -.
DR SMR; P48456; -.
DR BioGRID; 68520; 15.
DR IntAct; P48456; 5.
DR STRING; 7227.FBpp0085094; -.
DR PaxDb; P48456; -.
DR PRIDE; P48456; -.
DR DNASU; 43670; -.
DR EnsemblMetazoa; FBtr0085732; FBpp0085094; FBgn0010015.
DR EnsemblMetazoa; FBtr0334546; FBpp0306613; FBgn0010015.
DR GeneID; 43670; -.
DR KEGG; dme:Dmel_CG1455; -.
DR CTD; 43670; -.
DR FlyBase; FBgn0010015; CanA1.
DR VEuPathDB; VectorBase:FBgn0010015; -.
DR eggNOG; KOG0375; Eukaryota.
DR GeneTree; ENSGT00940000154115; -.
DR InParanoid; P48456; -.
DR OrthoDB; 463522at2759; -.
DR PhylomeDB; P48456; -.
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 BioGRID-ORCS; 43670; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43670; -.
DR PRO; PR:P48456; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010015; Expressed in crop (Drosophila) and 9 other tissues.
DR ExpressionAtlas; P48456; baseline and differential.
DR Genevisible; P48456; DM.
DR GO; GO:0005955; C:calcineurin complex; ISS:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; NAS:FlyBase.
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; 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:0004722; F:protein serine/threonine phosphatase activity; ISS:FlyBase.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0072375; P:medium-term memory; IDA:FlyBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:FlyBase.
DR GO; GO:0045088; P:regulation of innate immune response; IDA:FlyBase.
DR GO; GO:0071731; P:response to nitric oxide; IDA:FlyBase.
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 2: Evidence at transcript level;
KW Calmodulin-binding; Hydrolase; Iron; Metal-binding; Protein phosphatase;
KW Reference proteome; Zinc.
FT CHAIN 1..622
FT /note="Serine/threonine-protein phosphatase 2B catalytic
FT subunit 1"
FT /id="PRO_0000058830"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 132
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 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 459
FT /note="L -> V (in Ref. 4; AAA28410)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="P -> S (in Ref. 4; AAA28410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 69133 MW; FAD967D2123EFAE9 CRC64;
MSATSTRSSV TRKSSLSKSS SSDKSAKSSS NSSKSPTAAS GNKQKMQYTK TRERMVDDVP
LPPTHKLTMS EVYDDPKTGK PNFDALRQHF LLEGRIEEAV ALRIITEGAA LLREEKNMID
VEAPITVCGD IHGQFFDLVK LFEVGGPPAT TRYLFLGDYV DRGYFSIECV LYLWSLKITY
PTTLSLLRGN HECRHLTEYF TFKQECIIKY SESIYDACME AFDCLPLAAL LNQQFLCIHG
GLSPEIFTLD DIKTLNRFRE PPAYGPMCDL LWSDPLEDFG NEKTNEFFSH NSVRGCSYFF
SYSACCEFLQ KNNLLSIVRA HEAQDAGYRM YRKNQVTGFP SLITIFSAPN YLDVYNNKAA
VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK VTEMLVNILN ICSDDELVAG
PDDELEEELR KKIVLVPANA SNNNNNNNTP SKPASMSALR KEIIRNKIRA IGKMSRVFSI
LREESESVLQ LKGLTPTGAL PVGALSGGRD SLKEALQGLT ASSHIHSFAE AKGLDAVNER
MPPRRPLLMS ASSSSITTVT RSSSSSSNNN NNNSNTSSTT TTKDISNTSS NDTATVTKTS
RTTVKSATTS NVRAGFTAKK FP
