ID   PPY_DROME               Reviewed;         314 AA.
AC   P11612; Q26247; Q9V8A0;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Serine/threonine-protein phosphatase PP-Y;
DE            EC=3.1.3.16;
GN   Name=PpY-55A; Synonyms=PpD19, PPY; ORFNames=CG10930;
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].
RC   TISSUE=Head;
RX   PubMed=2541022; DOI=10.1016/0014-5793(89)81377-8;
RA   Dombradi V., Axton J.M., Glover D.M., Cohen P.T.W.;
RT   "Molecular cloning and chromosomal localization of a novel Drosophila
RT   protein phosphatase.";
RL   FEBS Lett. 247:391-395(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2166691; DOI=10.1016/0014-5793(90)81285-v;
RA   Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J.;
RT   "Protein serine/threonine phosphatases; an expanding family.";
RL   FEBS Lett. 268:355-359(1990).
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=Testis;
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-87.
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   -!- 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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Y subfamily.
CC       {ECO:0000305}.
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; Y07510; CAA68808.1; -; mRNA.
DR   EMBL; AE013599; AAF57771.1; -; Genomic_DNA.
DR   EMBL; AY075165; AAL68035.1; -; mRNA.
DR   EMBL; S40001; AAB22467.1; -; Genomic_DNA.
DR   PIR; S03963; PAFFY.
DR   RefSeq; NP_001286554.1; NM_001299625.1.
DR   RefSeq; NP_476689.1; NM_057341.4.
DR   AlphaFoldDB; P11612; -.
DR   SMR; P11612; -.
DR   BioGRID; 71474; 1.
DR   STRING; 7227.FBpp0085996; -.
DR   PaxDb; 7227-FBpp0085996; -.
DR   DNASU; 48532; -.
DR   EnsemblMetazoa; FBtr0086817; FBpp0085996; FBgn0003140.
DR   EnsemblMetazoa; FBtr0344898; FBpp0311209; FBgn0003140.
DR   GeneID; 48532; -.
DR   KEGG; dme:Dmel_CG10930; -.
DR   AGR; FB:FBgn0003140; -.
DR   CTD; 48532; -.
DR   FlyBase; FBgn0003140; PpY-55A.
DR   VEuPathDB; VectorBase:FBgn0003140; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   GeneTree; ENSGT00940000153472; -.
DR   HOGENOM; CLU_004962_0_0_1; -.
DR   InParanoid; P11612; -.
DR   OMA; YCGLMNN; -.
DR   OrthoDB; 3507827at2759; -.
DR   PhylomeDB; P11612; -.
DR   BioGRID-ORCS; 48532; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 48532; -.
DR   PRO; PR:P11612; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0003140; Expressed in testis and 9 other cell types or tissues.
DR   ExpressionAtlas; P11612; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
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; IDA:FlyBase.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF300; SERINE_THREONINE-PROTEIN PHOSPHATASE-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; P11612; DM.
PE   2: Evidence at transcript level;
KW   Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..314
FT                   /note="Serine/threonine-protein phosphatase PP-Y"
FT                   /id="PRO_0000058889"
FT   ACT_SITE        121
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
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         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        66
FT                   /note="T -> K (in Ref. 6; AAB22467)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="S -> C (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147
FT                   /note="S -> N (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  35980 MW;  6078CB66571261F0 CRC64;
     MAVLTTHEID CIIKELTSLN GSECTLKEEL IERLIQQTRE VIKWQPMLLE LQAPVNICGD
     IHGQFTDLLR IFKACGFPPK ANYLFLGDYV DRGKQSLETI CLLFAYKVKY PLNFFLLRGN
     HESASINKIY GFYDEIKRRH TVRLWHSFTD CFNWLPVAAL VGERIFCCHG GLSPSLRNLQ
     QINHIQRPTD IPDEGIMCDL LWADLNHTTK GWGHNDRGVS FTFDKVIVRD FLKAFDLQLM
     VRAHEVVEDG YEFFANRQLV TVFSAPNYCG MMNNAGGVMS VSTDLICSFV IILPCHKYKM
     IATDANQMPT NEEE
//