PP4C_DROME
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 03-AUG-2022, entry version 155.
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.FBpp0077016; -.
DR PaxDb; O76932; -.
DR PRIDE; O76932; -.
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 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; HGQFWDM; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; O76932; -.
DR Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
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 tissues.
DR ExpressionAtlas; O76932; baseline and differential.
DR Genevisible; O76932; DM.
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:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
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 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 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
