PPP6_DROME
ID PPP6_DROME Reviewed; 303 AA.
AC Q27884; Q5BIJ4; Q8MRZ7; Q9W3Z8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Serine/threonine-protein phosphatase 6 catalytic subunit;
DE Short=PP6C;
DE EC=3.1.3.16;
DE AltName: Full=Phosphatase V;
DE Short=PP-V;
GN Name=PpV; Synonyms=PPPV6A; ORFNames=CG12217;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Eye imaginal disk, and Head;
RX PubMed=8223492; DOI=10.1002/j.1460-2075.1993.tb06173.x;
RA Mann D.J., Dombradi V., Cohen P.T.W.;
RT "Drosophila protein phosphatase V functionally complements a SIT4 mutant in
RT Saccharomyces cerevisiae and its amino-terminal region can confer this
RT complementation to a heterologous phosphatase catalytic domain.";
RL EMBO J. 12:4833-4842(1993).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-303.
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).
CC -!- FUNCTION: May be involved in controlling cellularization or in
CC regulating transcription of the genes involved in this process.
CC {ECO:0000269|PubMed:8223492}.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8223492}.
CC -!- DEVELOPMENTAL STAGE: Expressed at highest levels in 2-4 hours embryos.
CC {ECO:0000269|PubMed:8223492}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V)
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM51039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X75980; CAA53588.1; -; mRNA.
DR EMBL; AE014298; AAF46163.1; -; Genomic_DNA.
DR EMBL; BT021230; AAX33378.1; -; mRNA.
DR EMBL; AY119179; AAM51039.1; ALT_INIT; mRNA.
DR PIR; S39611; S39611.
DR RefSeq; NP_001259272.1; NM_001272343.1.
DR RefSeq; NP_001259273.1; NM_001272344.1.
DR RefSeq; NP_001259274.1; NM_001272345.1.
DR RefSeq; NP_511061.1; NM_078506.3.
DR AlphaFoldDB; Q27884; -.
DR SMR; Q27884; -.
DR BioGRID; 58069; 6.
DR DIP; DIP-20494N; -.
DR IntAct; Q27884; 3.
DR STRING; 7227.FBpp0070883; -.
DR PaxDb; Q27884; -.
DR PRIDE; Q27884; -.
DR DNASU; 31582; -.
DR EnsemblMetazoa; FBtr0070921; FBpp0070883; FBgn0003139.
DR EnsemblMetazoa; FBtr0331430; FBpp0303847; FBgn0003139.
DR EnsemblMetazoa; FBtr0331431; FBpp0303848; FBgn0003139.
DR EnsemblMetazoa; FBtr0331432; FBpp0303849; FBgn0003139.
DR GeneID; 31582; -.
DR KEGG; dme:Dmel_CG12217; -.
DR CTD; 31582; -.
DR FlyBase; FBgn0003139; PpV.
DR VEuPathDB; VectorBase:FBgn0003139; -.
DR eggNOG; KOG0373; Eukaryota.
DR GeneTree; ENSGT00550000074961; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q27884; -.
DR OMA; CQNKYGN; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q27884; -.
DR SignaLink; Q27884; -.
DR BioGRID-ORCS; 31582; 0 hits in 3 CRISPR screens.
DR ChiTaRS; PpV; fly.
DR GenomeRNAi; 31582; -.
DR PRO; PR:Q27884; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003139; Expressed in cleaving embryo and 26 other tissues.
DR ExpressionAtlas; Q27884; baseline and differential.
DR Genevisible; Q27884; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISM:FlyBase.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; ISM: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 Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..303
FT /note="Serine/threonine-protein phosphatase 6 catalytic
FT subunit"
FT /id="PRO_0000058880"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 34759 MW; 5269F971416E55EC CRC64;
MGDVDKWIED VKKCKYLPEN ELKKLCEMVC DILLEETNIL PVSTPVTVCG DIHGQFYDLE
QLFRTGGQVP HTNYIFMGDF VDRGYYSLET FTRLLTLKAR YPSRITLLRG NHETRQITKV
YGFFDECFSK YGNANGWKYC CKVFDLLTIA AIIDEEVLCV HGGLSPEIIT LDQIRTIDRN
GEIPYKGAFC DLVWSDPEDM EYWGQSPRGA GWLFGHNVTK DFMAINNLNL ICRAHQLVNE
GIKYMFDGKL VTVWSAPNYC YRCGNVAAIL SFETAEKRQT KIFLAVPDAE RVIPKQNTTP
YFL
