ID   PP4C_DROME              Reviewed;         307 AA.
AC   O76932; Q9VR98;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE            Short=PP4C;
DE            EC=3.1.3.16;
GN   Name=Pp4-19C; Synonyms=pp4; ORFNames=CG32505;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=Oregon-R;
RX   PubMed=9570751; DOI=10.1242/jcs.111.10.1331;
RA   Helps N.R., Brewis N.D., Lineruth K., Davis T., Kaiser K., Cohen P.T.W.;
RT   "Protein phosphatase 4 is an essential enzyme required for organisation of
RT   microtubules at centrosomes in Drosophila embryos.";
RL   J. Cell Sci. 111:1331-1340(1998).
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;
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   [5]
RP   PROBABLE COMPONENT OF A COMPLEX WITH PPP4R2R AND FLFL, AND FUNCTION.
RX   PubMed=18487071; DOI=10.1016/j.biocel.2008.03.021;
RA   Martin-Granados C., Philp A., Oxenham S.K., Prescott A.R., Cohen P.T.W.;
RT   "Depletion of protein phosphatase 4 in human cells reveals essential roles
RT   in centrosome maturation, cell migration and the regulation of Rho
RT   GTPases.";
RL   Int. J. Biochem. Cell Biol. 40:2315-2332(2008).
CC   -!- FUNCTION: Protein phosphatase that regulates many processes such as
CC       microtubule organization at centrosomes. The probable PP4 complex Pp4-
CC       19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase-
CC       induced cell death (in vitro). {ECO:0000269|PubMed:18487071,
CC       ECO:0000269|PubMed:9570751}.
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   -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC       different assemblies of the catalytic and one or more regulatory
CC       subunits (By similarity). Probably part of a PP4 PPP4C-PPP4R2-PPP4R3
CC       complex containing Pp4-19C, PPP4R2r and flfl. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9570751}. Nucleus
CC       {ECO:0000269|PubMed:9570751}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000269|PubMed:9570751}.
CC   -!- PTM: Reversibly methyl esterified on Leu-307 by leucine carboxyl
CC       methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1
CC       (PPME1). Carboxyl methylation influences the affinity of the catalytic
CC       subunit for the different regulatory subunits, thereby modulating the
CC       PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC       localization (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; Y14213; CAA74606.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAF50905.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09547.1; -; Genomic_DNA.
DR   EMBL; AY113503; AAM29508.1; -; mRNA.
DR   RefSeq; NP_001285489.1; NM_001298560.1.
DR   RefSeq; NP_001285490.1; NM_001298561.1.
DR   RefSeq; NP_001303570.1; NM_001316641.1.
DR   RefSeq; NP_524803.1; NM_080064.3.
DR   RefSeq; NP_728342.1; NM_167703.4.
DR   AlphaFoldDB; O76932; -.
DR   SMR; O76932; -.
DR   BioGRID; 69445; 17.
DR   IntAct; O76932; 8.
DR   STRING; 7227.FBpp0312200; -.
DR   PaxDb; 7227-FBpp0077016; -.
DR   DNASU; 45031; -.
DR   EnsemblMetazoa; FBtr0077324; FBpp0077016; FBgn0023177.
DR   EnsemblMetazoa; FBtr0077325; FBpp0077017; FBgn0023177.
DR   EnsemblMetazoa; FBtr0345017; FBpp0311268; FBgn0023177.
DR   EnsemblMetazoa; FBtr0346620; FBpp0312200; FBgn0023177.
DR   EnsemblMetazoa; FBtr0445386; FBpp0401522; FBgn0023177.
DR   GeneID; 45031; -.
DR   KEGG; dme:Dmel_CG32505; -.
DR   AGR; FB:FBgn0023177; -.
DR   CTD; 45031; -.
DR   FlyBase; FBgn0023177; Pp4-19C.
DR   VEuPathDB; VectorBase:FBgn0023177; -.
DR   eggNOG; KOG0372; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; O76932; -.
DR   OMA; QSTMPID; -.
DR   OrthoDB; 19833at2759; -.
DR   PhylomeDB; O76932; -.
DR   SignaLink; O76932; -.
DR   BioGRID-ORCS; 45031; 1 hit in 3 CRISPR screens.
DR   GenomeRNAi; 45031; -.
DR   PRO; PR:O76932; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0023177; Expressed in secondary oocyte and 24 other cell types or tissues.
DR   ExpressionAtlas; O76932; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR   GO; GO:0000775; C:chromosome, centromeric region; IPI:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0030289; C:protein phosphatase 4 complex; 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; IMP:FlyBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IMP:FlyBase.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR   GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC SUBUNIT; 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; O76932; DM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Hydrolase; Manganese; Metal-binding; Methylation;
KW   Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..307
FT                   /note="Serine/threonine-protein phosphatase 4 catalytic
FT                   subunit"
FT                   /id="PRO_0000353208"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         307
FT                   /note="Leucine methyl ester"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  35341 MW;  514FCCB93A345E2E CRC64;
     MSDYSDLDRQ IEQLKRCEII KENEVKALCA KAREILVEEG NVQRVDSPVT VCGDIHGQFY
     DLKELFKVGG DVPEKNYLFM GDFVDRGYYS VETFLLLLAL KVRYPDRITL IRGNHESRQI
     TQVYGFYDEC LRKYGSTAVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IQYLDQIRSI
     DRKQEVPHDG PMCDLLWSDP EDQTGWGVSP RGAGYLFGSD VVSQFNRTND IDMICRAHQL
     VMEGFKWHFN ETVLTVWSAP NYCYRCGNVA AILELNEYLH RDFVIFEAAP QESRGIPSKK
     PQADYFL
//