PP4R2_DROME
ID PP4R2_DROME Reviewed; 609 AA.
AC Q9W2U4; Q960Z5; Q9NFT0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2;
DE AltName: Full=PPP4R2-related protein;
GN Name=PPP4R2r; ORFNames=CG2890;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-435.
RX PubMed=10769191; DOI=10.1042/bj3470845;
RA Hastie C.J., Carnegie G.K., Morrice N., Cohen P.T.W.;
RT "A novel 50 kDa protein forms complexes with protein phosphatase 4 and is
RT located at centrosomal microtubule organizing centres.";
RL Biochem. J. 347:845-855(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; THR-602 AND SER-603, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PROBABLE COMPONENT OF A COMPLEX WITH PP4-19C 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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-223; SER-226 AND
RP SER-252, AND IDENTIFICATION BY 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 -!- FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4
CC (PP4) (By similarity). The probable PP4 complex Pp4-19C-PPP4R2r-flfl
CC (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase induced cell death
CC (in vitro). {ECO:0000250, ECO:0000269|PubMed:18487071}.
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits. Probably part of a PP4 PPP4C-PPP4R2-PPP4R3 complex containing
CC Pp4-19C, PPP4R2r and flfl.
CC -!- SIMILARITY: Belongs to the PPP4R2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB93523.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF46594.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09262.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65307.1; -; Genomic_DNA.
DR EMBL; AY051757; AAK93181.1; -; mRNA.
DR EMBL; AJ271449; CAB93523.1; ALT_FRAME; mRNA.
DR RefSeq; NP_525083.2; NM_080344.3.
DR RefSeq; NP_727427.1; NM_167232.2.
DR RefSeq; NP_996400.1; NM_206677.2.
DR AlphaFoldDB; Q9W2U4; -.
DR BioGRID; 58407; 3.
DR IntAct; Q9W2U4; 2.
DR STRING; 7227.FBpp0071386; -.
DR iPTMnet; Q9W2U4; -.
DR PaxDb; Q9W2U4; -.
DR PRIDE; Q9W2U4; -.
DR DNASU; 31979; -.
DR EnsemblMetazoa; FBtr0071451; FBpp0071386; FBgn0030208.
DR EnsemblMetazoa; FBtr0071452; FBpp0071387; FBgn0030208.
DR EnsemblMetazoa; FBtr0071453; FBpp0089154; FBgn0030208.
DR GeneID; 31979; -.
DR KEGG; dme:Dmel_CG2890; -.
DR CTD; 31979; -.
DR FlyBase; FBgn0030208; PPP4R2r.
DR VEuPathDB; VectorBase:FBgn0030208; -.
DR eggNOG; KOG3175; Eukaryota.
DR GeneTree; ENSGT00940000162859; -.
DR HOGENOM; CLU_445691_0_0_1; -.
DR InParanoid; Q9W2U4; -.
DR PhylomeDB; Q9W2U4; -.
DR Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
DR SignaLink; Q9W2U4; -.
DR BioGRID-ORCS; 31979; 0 hits in 1 CRISPR screen.
DR ChiTaRS; PPP4R2r; fly.
DR GenomeRNAi; 31979; -.
DR PRO; PR:Q9W2U4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030208; Expressed in wing disc and 24 other tissues.
DR ExpressionAtlas; Q9W2U4; baseline and differential.
DR Genevisible; Q9W2U4; DM.
DR GO; GO:0000775; C:chromosome, centromeric region; IPI:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:FlyBase.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
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; IBA:GO_Central.
DR InterPro; IPR015267; PPP4R2.
DR PANTHER; PTHR16487; PTHR16487; 1.
DR Pfam; PF09184; PPP4R2; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..609
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 2"
FT /id="PRO_0000299375"
FT REGION 175..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 602
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 2
FT /note="V -> A (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="E -> Q (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="N -> H (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="L -> M (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="R -> P (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> Q (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> L (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 164..165
FT /note="SM -> FL (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="E -> Q (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="S -> F (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="P -> S (in Ref. 4; CAB93523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 66809 MW; 316FF8ACDE13B2BE CRC64;
MVTMENSDEI MQILERFTDL KQKEIPKELE EYLQYVAKTG DTIFKWSSLK YLFREKLLSV
IKHFNEDSPR LEEIPNYPNV DPFNYETMKS SLLERLDLFN AAPFTVQRLC ELLIDPRKQY
SRIDKFMRAL EKNILVVSTI DPGRKRTESE NGDSLDSVVN GDLSMEVNID IEMENNNGNA
DEGSSPGAGS AGCAQKASCP RSDDNDQPKA KKAKLEIDGE ERSEASDETD TEVATRVKNE
KDEKNDNDET DSPHEAAEIE EPDEEVDEAD QETKTTKQPA YGSQKEGEQE ESFPSSADDE
AEDPMVSKSI EAEKELVAQE KKREEDKKVA IEPKEEIVKK EEVVESDKPD GKVAQLGDKA
VVKKSTPPAD GENQEPVKVK AENEKEEKKH APIKTEKQDD IDSTETDDAP SAEKPAEEKI
ASSESKPKTK SEDDPEAETK KSQPEKTETE AAEKSVSDEK QAAEPNAESE NRNDLTTSKA
TEAAQESVEK SPVEDASSPA VEDLAAATTP QSPLGAADSA AETPPAETGD DSQASPLVAA
VTPPVLALND QPMEDTPAEE EARVSPSATV EEVVMAESAN AGAMATEEAA KDDPAAMEID
DTSQEVMMQ
