ID   PP11_DROME              Reviewed;         327 AA.
AC   P48461; Q5U0Y2; Q9VC69;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 195.
DE   RecName: Full=Serine/threonine-protein phosphatase alpha-1 isoform;
DE            EC=3.1.3.16;
GN   Name=Pp1alpha-96A; Synonyms=Pp1-96A; ORFNames=CG6593;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=2176604; DOI=10.1111/j.1432-1033.1990.tb19464.x;
RA   Dombradi V., Axton J.M., Brewis N.D., da Cruz e Silva E.F., Alphey L.,
RA   Cohen P.T.W.;
RT   "Drosophila contains three genes that encode distinct isoforms of protein
RT   phosphatase 1.";
RL   Eur. J. Biochem. 194:739-745(1990).
RN   [2]
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   [3]
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH NOP17L.
RX   PubMed=17007873; DOI=10.1016/j.jmb.2006.08.094;
RA   Bennett D., Lyulcheva E., Alphey L.;
RT   "Towards a comprehensive analysis of the protein phosphatase 1 interactome
RT   in Drosophila.";
RL   J. Mol. Biol. 364:196-212(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, 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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with Nop17l. {ECO:0000269|PubMed:17007873}.
CC   -!- INTERACTION:
CC       P48461; Q9V7W9: NiPp1; NbExp=3; IntAct=EBI-91997, EBI-108894;
CC       P48461; Q0E9G3: Nop17l; NbExp=4; IntAct=EBI-91997, EBI-150380;
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X56438; CAA39820.1; -; mRNA.
DR   EMBL; AE014297; AAF56306.1; -; Genomic_DNA.
DR   EMBL; BT016110; AAV36995.1; -; mRNA.
DR   PIR; S13827; S13827.
DR   RefSeq; NP_001262919.1; NM_001275990.1.
DR   RefSeq; NP_524484.1; NM_079760.3.
DR   AlphaFoldDB; P48461; -.
DR   SMR; P48461; -.
DR   BioGRID; 67848; 39.
DR   DIP; DIP-19812N; -.
DR   FunCoup; P48461; 2447.
DR   IntAct; P48461; 28.
DR   MINT; P48461; -.
DR   STRING; 7227.FBpp0306442; -.
DR   iPTMnet; P48461; -.
DR   PaxDb; 7227-FBpp0306442; -.
DR   PeptideAtlas; P48461; -.
DR   EnsemblMetazoa; FBtr0084642; FBpp0084026; FBgn0003134.
DR   EnsemblMetazoa; FBtr0334334; FBpp0306442; FBgn0003134.
DR   GeneID; 42922; -.
DR   KEGG; dme:Dmel_CG6593; -.
DR   AGR; FB:FBgn0003134; -.
DR   CTD; 42922; -.
DR   FlyBase; FBgn0003134; Pp1alpha-96A.
DR   VEuPathDB; VectorBase:FBgn0003134; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   HOGENOM; CLU_004962_8_3_1; -.
DR   InParanoid; P48461; -.
DR   OMA; SIFICRG; -.
DR   OrthoDB; 1930084at2759; -.
DR   PhylomeDB; P48461; -.
DR   Reactome; R-DME-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-DME-538898; Dephosphorylation of TIM.
DR   Reactome; R-DME-9770562; mRNA Polyadenylation.
DR   BioGRID-ORCS; 42922; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42922; -.
DR   PRO; PR:P48461; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003134; Expressed in fat body cell in male reproductive gland and 280 other cell types or tissues.
DR   ExpressionAtlas; P48461; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:FlyBase.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISM:FlyBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IGI:FlyBase.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:FlyBase.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:FlyBase.
DR   GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISS:FlyBase.
DR   GO; GO:0005981; P:regulation of glycogen catabolic process; ISS:FlyBase.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   FunFam; 3.60.21.10:FF:000004; Serine/threonine-protein phosphatase; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR050341; PP1_catalytic_subunit.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF300; SERINE_THREONINE-PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Metal-binding; Phosphoprotein; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..327
FT                   /note="Serine/threonine-protein phosphatase alpha-1
FT                   isoform"
FT                   /id="PRO_0000058791"
FT   REGION          308..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        123
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         315
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   327 AA;  37370 MW;  372390FBBB3CA8F0 CRC64;
     MSDIMNIDSI ISRLLEVRGA RPGKNVQLSE SEIRSLCLKS REIFLSQPIL LELEAPLKIC
     GDIHGQYYDL LRLFEYGGFP PESNYLFLGD YVDRGKQSLE TICLLLAYKI KYAENFFLLR
     GNHECASINR IYGFYDECKR RYTIKLWKTF TDCFNCLPVA AIVDEKIFCC HGGLSPDLSS
     MEQIRRIMRP TDVPDQGLLC DLLWSDPDKD TMGWGENDRG VSFTFGAEVV GKFLQKHEFD
     LICRAHQVVE DGYEFFAKRQ LVTLFSAPNY CGEFDNAGAM MSVDDTLMCS FQILKPADKR
     RFVYPNFGSS GRPLTPPRGA NNKNKKK
//