PP12_DROME
ID PP12_DROME Reviewed; 302 AA.
AC P12982; Q4PIY5; Q9VG75;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Serine/threonine-protein phosphatase alpha-2 isoform;
DE EC=3.1.3.16 {ECO:0000269|PubMed:18412953};
GN Name=Pp1-87B; ORFNames=CG5650;
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=Head;
RX PubMed=2550221; DOI=10.1111/j.1432-1033.1989.tb21089.x;
RA Dombradi V., Axton J.M., Glover D.M., Cohen P.T.W.;
RT "Cloning and chromosomal localization of Drosophila cDNA encoding the
RT catalytic subunit of protein phosphatase 1 alpha. High conservation between
RT mammalian and insect sequences.";
RL Eur. J. Biochem. 183:603-610(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Canton-S;
RX PubMed=1330679; DOI=10.1016/0014-5793(92)81402-8;
RA Dombradi V., Cohen P.T.W.;
RT "Protein phosphorylation is involved in the regulation of chromatin
RT condensation during interphase.";
RL FEBS Lett. 312:21-26(1992).
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 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 [6]
RP FUNCTION.
RX PubMed=2175717; DOI=10.1016/0014-5793(90)81434-p;
RA Dombradi V., Axton J.M., Barker H.M., Cohen P.T.W.;
RT "Protein phosphatase 1 activity in Drosophila mutants with abnormalities in
RT mitosis and chromosome condensation.";
RL FEBS Lett. 275:39-43(1990).
RN [7]
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 [8]
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 [9]
RP INTERACTION WITH RIF1, AND DEVELOPMENTAL STAGE.
RX PubMed=26022086; DOI=10.1038/srep10679;
RA Sreesankar E., Bharathi V., Mishra R.K., Mishra K.;
RT "Drosophila Rif1 is an essential gene and controls late developmental
RT events by direct interaction with PP1-87B.";
RL Sci. Rep. 5:10679-10679(2015).
RN [10]
RP INTERACTION WITH RIF1, AND DEVELOPMENTAL STAGE.
RX PubMed=29746464; DOI=10.1371/journal.pbio.2005687;
RA Seller C.A., O'Farrell P.H.;
RT "Rif1 prolongs the embryonic S phase at the Drosophila mid-blastula
RT transition.";
RL PLoS Biol. 16:E2005687-E2005687(2018).
CC -!- FUNCTION: Is essential for the regulation of mitotic chromosomal
CC segregation as well as regulation of chromatin condensation during
CC interphase. {ECO:0000269|PubMed:1330679, ECO:0000269|PubMed:2175717}.
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 Pp1-87B phosphatase activity (PubMed:18412953). Interacts
CC with Rif1 (PubMed:26022086, PubMed:29746464).
CC {ECO:0000269|PubMed:17007873, ECO:0000269|PubMed:18412953,
CC ECO:0000269|PubMed:26022086, ECO:0000269|PubMed:29746464}.
CC -!- INTERACTION:
CC P12982; Q0E9G3: Nop17l; NbExp=3; IntAct=EBI-152633, EBI-150380;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos and larvae (at protein level).
CC {ECO:0000269|PubMed:26022086, ECO:0000269|PubMed:29746464}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X15583; CAA33609.1; -; mRNA.
DR EMBL; S47852; AAB23957.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54810.1; -; Genomic_DNA.
DR EMBL; AY061063; AAL28611.1; -; mRNA.
DR PIR; S12960; PAFF1A.
DR RefSeq; NP_524937.1; NM_080198.3.
DR AlphaFoldDB; P12982; -.
DR SMR; P12982; -.
DR BioGRID; 72126; 71.
DR DIP; DIP-18465N; -.
DR IntAct; P12982; 42.
DR STRING; 7227.FBpp0082067; -.
DR PaxDb; P12982; -.
DR PRIDE; P12982; -.
DR EnsemblMetazoa; FBtr0082595; FBpp0082067; FBgn0004103.
DR GeneID; 49260; -.
DR KEGG; dme:Dmel_CG5650; -.
DR CTD; 49260; -.
DR FlyBase; FBgn0004103; Pp1-87B.
DR VEuPathDB; VectorBase:FBgn0004103; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000153472; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P12982; -.
DR OMA; YLVMESR; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P12982; -.
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 BioGRID-ORCS; 49260; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Pp1-87B; fly.
DR GenomeRNAi; 49260; -.
DR PRO; PR:P12982; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004103; Expressed in eye disc (Drosophila) and 25 other tissues.
DR Genevisible; P12982; 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:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISS:FlyBase.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IEA:InterPro.
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:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:1904886; P:beta-catenin destruction complex disassembly; ISS:FlyBase.
DR GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR GO; GO:0007611; P:learning or memory; NAS:FlyBase.
DR GO; GO:0040011; P:locomotion; NAS:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:FlyBase.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; HGI:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR GO; GO:0008542; P:visual learning; 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; IPR037979; PPP1CA.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF377; PTHR11668:SF377; 1.
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 Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..302
FT /note="Serine/threonine-protein phosphatase alpha-2
FT isoform"
FT /id="PRO_0000058792"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 302 AA; 34542 MW; 68FE054996C9A062 CRC64;
MGDVMNIDSI ISRLLEVRGA RPGKNVQLSE GEIRGLCLKS REIFLSQPIL LELEAPLKIC
GDIHGQYYDL LRLFEYGGFP PESNYLFLGD YVDRGKQSLE TICLLLAYKI KYSENFFLLR
GNHECASINR IYGFYDECKR RYSIKLWKTF TDCFNCLPVA AIVDEKIFCC HGGLSPDLTS
MEQIRRIMRP TDVPDQGLLC DLLWSDPDKD TMGWGENDRG VSFTFGAEVV AKFLQKHEFD
LICRAHQVVE DGYEFFAKRM LVTLFSAPNY CGEFDNAGAM MSVDDTLMCS FQILKPADKR
KK
