PP1B_DROME
ID PP1B_DROME Reviewed; 330 AA.
AC P48462; Q9W2V5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Serine/threonine-protein phosphatase beta isoform;
DE EC=3.1.3.16 {ECO:0000269|PubMed:18412953};
DE AltName: Full=Protein flap wing;
GN Name=flw; Synonyms=PP1-9C, PP1-BETA-9C; ORFNames=CG2096;
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 [MRNA].
RC TISSUE=Embryo;
RX PubMed=2176604; DOI=10.1111/j.1432-1033.1990.tb19464.x;
RA Dombradi V., Axton J.M., Brewis N.D., da Cruz e Silva E.F., Alphey L.,
RA Cohen P.T.W.;
RT "Drosophila contains three genes that encode distinct isoforms of protein
RT phosphatase 1.";
RL Eur. J. Biochem. 194:739-745(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF TYR-133 AND
RP VAL-284.
RX PubMed=10712908; DOI=10.1016/s0960-9822(00)00364-x;
RA Raghavan S., Williams I., Aslam H., Thomas D., Szoor B., Morgan G.,
RA Gross S., Turner J., Fernandes J., VijayRaghavan K., Alphey L.;
RT "Protein phosphatase 1beta is required for the maintenance of muscle
RT attachments.";
RL Curr. Biol. 10:269-272(2000).
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH NOP17L.
RX PubMed=17007873; DOI=10.1016/j.jmb.2006.08.094;
RA Bennett D., Lyulcheva E., Alphey L.;
RT "Towards a comprehensive analysis of the protein phosphatase 1 interactome
RT in Drosophila.";
RL J. Mol. Biol. 364:196-212(2006).
RN [6]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH URI.
RX PubMed=18412953; DOI=10.1186/1471-2199-9-36;
RA Kirchner J., Vissi E., Gross S., Szoor B., Rudenko A., Alphey L.,
RA White-Cooper H.;
RT "Drosophila Uri, a PP1alpha binding protein, is essential for viability,
RT maintenance of DNA integrity and normal transcriptional activity.";
RL BMC Mol. Biol. 9:36-36(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315 AND THR-316, AND
RP 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: Required for cell adhesion in non-muscle tissues and in
CC maintenance of muscle attachment. Vital for larval development.
CC {ECO:0000269|PubMed:10712908}.
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 Evidence={ECO:0000269|PubMed:18412953};
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 Evidence={ECO:0000269|PubMed:18412953};
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: Interacts with Nop17l (PubMed:17007873). Interacts with uri;
CC uri inhibits flw phosphatase activity (PubMed:18412953).
CC {ECO:0000269|PubMed:17007873, ECO:0000269|PubMed:18412953}.
CC -!- INTERACTION:
CC P48462; Q0E9G3: Nop17l; NbExp=3; IntAct=EBI-869621, EBI-150380;
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X56439; CAA39821.1; -; mRNA.
DR EMBL; AJ249214; CAB59732.1; -; Genomic_DNA.
DR EMBL; AJ249215; CAB59732.1; JOINED; Genomic_DNA.
DR EMBL; AE014298; AAF46583.2; -; Genomic_DNA.
DR PIR; S13828; S13828.
DR RefSeq; NP_001259407.1; NM_001272478.1.
DR RefSeq; NP_524738.1; NM_079999.3.
DR AlphaFoldDB; P48462; -.
DR SMR; P48462; -.
DR BioGRID; 68952; 133.
DR IntAct; P48462; 28.
DR STRING; 7227.FBpp0071381; -.
DR iPTMnet; P48462; -.
DR PaxDb; P48462; -.
DR PRIDE; P48462; -.
DR DNASU; 44289; -.
DR EnsemblMetazoa; FBtr0071447; FBpp0071382; FBgn0000711.
DR EnsemblMetazoa; FBtr0333305; FBpp0305497; FBgn0000711.
DR GeneID; 44289; -.
DR KEGG; dme:Dmel_CG2096; -.
DR CTD; 44289; -.
DR FlyBase; FBgn0000711; flw.
DR VEuPathDB; VectorBase:FBgn0000711; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000154644; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P48462; -.
DR OMA; TVQMSEN; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P48462; -.
DR Reactome; R-DME-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DME-350416; Regulation of non-muscle Myosin II.
DR Reactome; R-DME-350480; Activation of non-muscle Myosin II.
DR Reactome; R-DME-538898; Dephosphorylation of TIM.
DR Reactome; R-DME-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR SignaLink; P48462; -.
DR BioGRID-ORCS; 44289; 1 hit in 3 CRISPR screens.
DR ChiTaRS; flw; fly.
DR GenomeRNAi; 44289; -.
DR PRO; PR:P48462; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000711; Expressed in second segment of antenna (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P48462; baseline and differential.
DR Genevisible; P48462; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IDA:FlyBase.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:FlyBase.
DR GO; GO:1904886; P:beta-catenin destruction complex disassembly; ISS:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR GO; GO:0007301; P:female germline ring canal formation; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; NAS:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IGI:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:FlyBase.
DR GO; GO:0007312; P:oocyte nucleus migration involved in oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0007300; P:ovarian nurse cell to oocyte transport; IMP:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:FlyBase.
DR GO; GO:0031991; P:regulation of actomyosin contractile ring contraction; IMP:FlyBase.
DR GO; GO:1905330; P:regulation of morphogenesis of an epithelium; IMP:FlyBase.
DR GO; GO:0014706; P:striated muscle tissue development; 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 InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Hydrolase; Manganese; Metal-binding; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..330
FT /note="Serine/threonine-protein phosphatase beta isoform"
FT /id="PRO_0000058794"
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 133
FT /note="Y->F: Semi lethal, adult escapers exhibit muscle and
FT wing mutant phenotype; allele flw-6."
FT /evidence="ECO:0000269|PubMed:10712908"
FT MUTAGEN 284
FT /note="V->A: Muscle and wing mutant phenotype; allele flw-
FT 1."
FT /evidence="ECO:0000269|PubMed:10712908"
SQ SEQUENCE 330 AA; 37740 MW; 9233DFC06EAE17AD CRC64;
MGDFDLNVDS LIQRLLEMRS CRTGKQVQMT EAEVRGLCLK SREIFLQQPI LLELEAPLII
CGDIHGQYTD LLRLFEYGGF PPAANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL
RGNHECASIN RIYGFYDECK RRYNVKLWKT FTDCFNCLPV AAIIDEKIFC CHGGLSPDLQ
GMEQIRRLMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGVDV VSKFLNRHEL
DLICRAHQVV EDGYEFFARR QLVTLFSAPN YCGEFDNAGG MMTVDDTLMC SFQILKPSEK
KAKYLYSGMN SSRPTTPQRS APMLATNKKK
