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Serine/threonine-protein phosphatase 4 catalytic subunit (PP4C) (EC 3.1.3.16)

 PP4C_DROME              Reviewed;         307 AA.
O76932; Q9VR98;
04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 134.
RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
Short=PP4C;
EC=3.1.3.16;
Name=Pp4-19C; Synonyms=pp4; ORFNames=CG32505;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=Oregon-R;
PubMed=9570751;
Helps N.R., Brewis N.D., Lineruth K., Davis T., Kaiser K.,
Cohen P.T.W.;
"Protein phosphatase 4 is an essential enzyme required for
organisation of microtubules at centrosomes in Drosophila embryos.";
J. Cell Sci. 111:1331-1340(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
PROBABLE COMPONENT OF A COMPLEX WITH PPP4R2R AND FLFL, AND FUNCTION.
PubMed=18487071; DOI=10.1016/j.biocel.2008.03.021;
Martin-Granados C., Philp A., Oxenham S.K., Prescott A.R.,
Cohen P.T.W.;
"Depletion of protein phosphatase 4 in human cells reveals essential
roles in centrosome maturation, cell migration and the regulation of
Rho GTPases.";
Int. J. Biochem. Cell Biol. 40:2315-2332(2008).
-!- FUNCTION: Protein phosphatase that regulates many processes such
as microtubule organization at centrosomes. The probable PP4
complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to
prevent caspase-induced cell death (in vitro).
{ECO:0000269|PubMed:18487071, ECO:0000269|PubMed:9570751}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
different assemblies of the catalytic and one or more regulatory
subunits (By similarity). Probably part of a PP4 PPP4C-PPP4R2-
PPP4R3 complex containing Pp4-19C, PPP4R2r and flfl.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9570751}.
Nucleus {ECO:0000269|PubMed:9570751}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:9570751}.
-!- PTM: Reversibly methyl esterified on Leu-307 by leucine carboxyl
methyltransferase 1 (LCMT1) and protein phosphatase methylesterase
1 (PPME1). Carboxyl methylation influences the affinity of the
catalytic subunit for the different regulatory subunits, thereby
modulating the PP2A holoenzyme's substrate specificity, enzyme
activity and cellular localization (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y14213; CAA74606.1; -; Genomic_DNA.
EMBL; AE014298; AAF50905.1; -; Genomic_DNA.
EMBL; AE014298; AAN09547.1; -; Genomic_DNA.
EMBL; AY113503; AAM29508.1; -; mRNA.
RefSeq; NP_001285489.1; NM_001298560.1.
RefSeq; NP_001285490.1; NM_001298561.1.
RefSeq; NP_001303570.1; NM_001316641.1.
RefSeq; NP_524803.1; NM_080064.3.
RefSeq; NP_728342.1; NM_167703.4.
UniGene; Dm.1809; -.
ProteinModelPortal; O76932; -.
SMR; O76932; -.
BioGrid; 69445; 17.
IntAct; O76932; 8.
MINT; MINT-1643247; -.
STRING; 7227.FBpp0077016; -.
PaxDb; O76932; -.
PRIDE; O76932; -.
EnsemblMetazoa; FBtr0077324; FBpp0077016; FBgn0023177.
EnsemblMetazoa; FBtr0077325; FBpp0077017; FBgn0023177.
EnsemblMetazoa; FBtr0340403; FBpp0309349; FBgn0023177.
EnsemblMetazoa; FBtr0345017; FBpp0311268; FBgn0023177.
EnsemblMetazoa; FBtr0346620; FBpp0312200; FBgn0023177.
GeneID; 45031; -.
KEGG; dme:Dmel_CG32505; -.
CTD; 45031; -.
FlyBase; FBgn0023177; Pp4-19C.
eggNOG; KOG0371; Eukaryota.
eggNOG; COG0639; LUCA.
InParanoid; O76932; -.
KO; K15423; -.
OMA; PDRMTLI; -.
OrthoDB; EOG091G0B6S; -.
PhylomeDB; O76932; -.
SignaLink; O76932; -.
GenomeRNAi; 45031; -.
PRO; PR:O76932; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0023177; -.
ExpressionAtlas; O76932; differential.
Genevisible; O76932; DM.
GO; GO:0005813; C:centrosome; IDA:FlyBase.
GO; GO:0000775; C:chromosome, centromeric region; IPI:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0030289; C:protein phosphatase 4 complex; IDA:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:FlyBase.
GO; GO:0007017; P:microtubule-based process; IMP:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
GO; GO:0006470; P:protein dephosphorylation; IMP:FlyBase.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
SUPFAM; SSF56300; SSF56300; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Manganese;
Metal-binding; Methylation; Nucleus; Protein phosphatase;
Reference proteome.
CHAIN 1 307 Serine/threonine-protein phosphatase 4
catalytic subunit.
/FTId=PRO_0000353208.
ACT_SITE 115 115 Proton donor. {ECO:0000250}.
METAL 54 54 Manganese 1. {ECO:0000250}.
METAL 56 56 Manganese 1. {ECO:0000250}.
METAL 82 82 Manganese 1. {ECO:0000250}.
METAL 82 82 Manganese 2. {ECO:0000250}.
METAL 114 114 Manganese 2. {ECO:0000250}.
METAL 164 164 Manganese 2. {ECO:0000250}.
METAL 238 238 Manganese 2. {ECO:0000250}.
MOD_RES 307 307 Leucine methyl ester. {ECO:0000250}.
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


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