PP4R3_DROME
ID PP4R3_DROME Reviewed; 980 AA.
AC Q9VFS5; Q8MSX6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 4.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3;
DE Short=PP4R3;
DE AltName: Full=Protein falafel;
GN Name=flfl; ORFNames=CG9351;
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM D).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16085932; DOI=10.1074/mcp.m500231-mcp200;
RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R., Fields S.,
RA Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT "A novel, evolutionarily conserved protein phosphatase complex involved in
RT cisplatin sensitivity.";
RL Mol. Cell. Proteomics 4:1725-1740(2005).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19204120; DOI=10.1101/gad.1723609;
RA Sousa-Nunes R., Chia W., Somers W.G.;
RT "Protein phosphatase 4 mediates localization of the Miranda complex during
RT Drosophila neuroblast asymmetric divisions.";
RL Genes Dev. 23:359-372(2009).
RN [6]
RP PROBABLE COMPONENT OF A COMPLEX WITH PP4-19C AND PPP4R2R, 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: Regulatory subunit of serine/threonine-protein phosphatase 4.
CC The probable PP4 complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is
CC required to prevent caspase induced cell death (in vitro). May be
CC involved in DNA damage repair. Key mediator specific for the
CC localization of mira and associated cell fate determinants during both
CC interphase and mitosis. Nuclear Flfl is required to exclude mira/pros
CC from the nucleus when inefficiently bound to the cytoskeleton/cortex,
CC whereas cytosolic or membrane-associated flfl is required for the
CC cortical association and asymmetric localization of mira/pros/brat/stau
CC at metaphase and anaphase. {ECO:0000269|PubMed:16085932,
CC ECO:0000269|PubMed:18487071, ECO:0000269|PubMed:19204120}.
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. Interacts with mira.
CC {ECO:0000269|PubMed:19204120}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19204120}. Membrane
CC {ECO:0000269|PubMed:19204120}. Cytoplasm {ECO:0000269|PubMed:19204120}.
CC Note=Predominantly nuclear during interphase/prophase and cytoplasmic
CC after nuclear envelope breakdown.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q9VFS5-1; Sequence=Displayed;
CC Name=D;
CC IsoId=Q9VFS5-2; Sequence=VSP_037302;
CC -!- TISSUE SPECIFICITY: Expressed in neuroblasts.
CC {ECO:0000269|PubMed:19204120}.
CC -!- DISRUPTION PHENOTYPE: Mutant larvae exhibit hypersensitivity to the
CC anticancer drug cisplatin. {ECO:0000269|PubMed:16085932}.
CC -!- SIMILARITY: Belongs to the SMEK family. {ECO:0000305}.
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DR EMBL; AE014297; AAF54974.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13587.2; -; Genomic_DNA.
DR EMBL; AY118508; AAM49877.1; -; mRNA.
DR RefSeq; NP_650304.2; NM_142047.4. [Q9VFS5-2]
DR RefSeq; NP_731849.2; NM_169548.3. [Q9VFS5-1]
DR RefSeq; NP_731850.2; NM_169549.2. [Q9VFS5-1]
DR PDB; 4WSF; X-ray; 1.50 A; A=2-123.
DR PDBsum; 4WSF; -.
DR AlphaFoldDB; Q9VFS5; -.
DR SMR; Q9VFS5; -.
DR BioGRID; 66755; 11.
DR STRING; 7227.FBpp0082285; -.
DR PaxDb; Q9VFS5; -.
DR PRIDE; Q9VFS5; -.
DR DNASU; 41675; -.
DR EnsemblMetazoa; FBtr0082817; FBpp0082285; FBgn0024555. [Q9VFS5-1]
DR EnsemblMetazoa; FBtr0114604; FBpp0113096; FBgn0024555. [Q9VFS5-2]
DR EnsemblMetazoa; FBtr0344783; FBpp0311112; FBgn0024555. [Q9VFS5-1]
DR GeneID; 41675; -.
DR KEGG; dme:Dmel_CG9351; -.
DR UCSC; CG9351-RB; d. melanogaster. [Q9VFS5-1]
DR UCSC; CG9351-RD; d. melanogaster.
DR CTD; 41675; -.
DR FlyBase; FBgn0024555; flfl.
DR VEuPathDB; VectorBase:FBgn0024555; -.
DR eggNOG; KOG2175; Eukaryota.
DR GeneTree; ENSGT00390000018199; -.
DR InParanoid; Q9VFS5; -.
DR OMA; MMRGYML; -.
DR PhylomeDB; Q9VFS5; -.
DR BioGRID-ORCS; 41675; 0 hits in 3 CRISPR screens.
DR ChiTaRS; flfl; fly.
DR GenomeRNAi; 41675; -.
DR PRO; PR:Q9VFS5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0024555; Expressed in wing disc and 37 other tissues.
DR ExpressionAtlas; Q9VFS5; baseline and differential.
DR Genevisible; Q9VFS5; DM.
DR GO; GO:0000775; C:chromosome, centromeric region; IPI:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:UniProtKB.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR GO; GO:0045175; P:basal protein localization; IMP:FlyBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006887; DUF625.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF04802; SMK-1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Membrane; Nucleus;
KW Reference proteome.
FT CHAIN 1..980
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 3"
FT /id="PRO_0000355974"
FT DOMAIN 1..105
FT /note="WH1"
FT REGION 640..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 651..657
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_037302"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:4WSF"
FT STRAND 20..33
FT /evidence="ECO:0007829|PDB:4WSF"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4WSF"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:4WSF"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:4WSF"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4WSF"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4WSF"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4WSF"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:4WSF"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:4WSF"
FT HELIX 88..102
FT /evidence="ECO:0007829|PDB:4WSF"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4WSF"
SQ SEQUENCE 980 AA; 109295 MW; ACD1835AB3CF3481 CRC64;
MTTDTRRRVK LYALNAERQW DDRGTGHVSS TYVERLKGIS LLVRAESDGS LLLESKIQPD
TAYQKQQDTL IVWSEGDNFD LALSFQEKAG CDEIWEKICQ VQGKDPSVEI TQDIVEESED
ERFEDMSDTA PPIELPPCEL SRLEDISETI QSCLSTPLRK EKLSMALESE SYIKKLLNLF
HVCEDLDNTE GLHHLFEIFK NIFLLNKNAL FEIMFADDTI FDVVGCLEYD PSVSQPKKHR
QYLKQLAKFR EAVPIKNLDL LAKIHQTFRV QYIQDIILPT PSVFVEDNML NTLSSFIFFN
KVEIVTMIQD DERYLLDVFA VLTDPTTGDA KRRDTVLFLK EFCNYAQNLQ PQGKDSFYKT
LTCLGILQAL ELTLVMNDKK TKSASIDILT AIVEFSPLVV RNYTLNQANR PEVERMLLNI
AIEQMLNDSE PELGIAVQLM GIVKILLEPE NMLTEKGDFL NFFYKYSVQT LVAPVILNTI
GDRPQNEDYQ TAQLLGIVLD ILSFCVEHHS YHIKNFLLQK DLLKRILVLM KSTHTFLVLG
ALRLLRKIIA LKDEFYNRHI VKCNLFAPVV DAFIRNNGRY NLLESAILEL FEFIKLEDIR
TLCVYFVENF SKIFDEIEYV QTFKYLKNRY DQYQDRLKDR DKMENRTDGG LPIIRSGGRF
RRDQRQMEEE EEMWFNEEDD FTEEIDTYNN VMKSVSEKNG PQTQNQQKSS PPHSTSPHSG
LLGSLSTTAS STATSATSGA PVASGSSSPE AISADEQTQA AVHLAAAALQ HHQQQQQQQQ
QNPFQQQTQP EIAELQQQLS SVEAPQSQEL ELSQSAAASA SPTSSSSSLE ASTSSSSASS
SSSSSSSSSP PGSSAAASLC DSATVAAVAA SQFLSTIATA MAASVTAAAA TNSSPSISPA
PAVSSPDIEN ADAQLPPSDD ASSPASGEQD ANSTEGTSSE ADKTTAKKGL VDYESDSGED
DYEEDEYSEG PQAQKRARQA
