MPIP_DROME
ID MPIP_DROME Reviewed; 479 AA.
AC P20483; Q9VAL9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=M-phase inducer phosphatase;
DE EC=3.1.3.48;
DE AltName: Full=Cdc25-like protein;
DE AltName: Full=Protein string;
GN Name=stg; Synonyms=cdc25; ORFNames=CG1395;
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].
RX PubMed=2702688; DOI=10.1016/0092-8674(89)90183-9;
RA Edgar B.A., O'Farrell P.H.;
RT "Genetic control of cell division patterns in the Drosophila embryo.";
RL Cell 57:177-187(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2120044; DOI=10.1002/j.1460-2075.1990.tb07567.x;
RA Jimenez J., Alphey L., Nurse P., Glover D.M.;
RT "Complementation of fission yeast cdc2ts and cdc25ts mutants identifies two
RT cell cycle genes from Drosophila: a cdc2 homologue and string.";
RL EMBO J. 9:3565-3571(1990).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP 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: This protein functions as a dosage-dependent inducer in
CC mitotic control. It is a tyrosine protein phosphatase required for
CC progression of the cell cycle. It may directly dephosphorylate Cdk1 and
CC activate the Cdk1 activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR EMBL; M24909; AAA28916.1; -; mRNA.
DR EMBL; X57495; CAA40732.1; -; mRNA.
DR EMBL; AE014297; AAF56885.1; -; Genomic_DNA.
DR EMBL; AY069704; AAL39849.1; -; mRNA.
DR PIR; A32290; A32290.
DR RefSeq; NP_001263066.1; NM_001276137.1.
DR RefSeq; NP_524547.1; NM_079823.4.
DR AlphaFoldDB; P20483; -.
DR SMR; P20483; -.
DR BioGRID; 68333; 38.
DR DIP; DIP-19931N; -.
DR IntAct; P20483; 2.
DR STRING; 7227.FBpp0084766; -.
DR iPTMnet; P20483; -.
DR PaxDb; P20483; -.
DR DNASU; 43466; -.
DR EnsemblMetazoa; FBtr0085397; FBpp0084766; FBgn0003525.
DR EnsemblMetazoa; FBtr0334867; FBpp0306890; FBgn0003525.
DR GeneID; 43466; -.
DR KEGG; dme:Dmel_CG1395; -.
DR CTD; 43466; -.
DR FlyBase; FBgn0003525; stg.
DR VEuPathDB; VectorBase:FBgn0003525; -.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000166659; -.
DR HOGENOM; CLU_014464_3_1_1; -.
DR InParanoid; P20483; -.
DR OMA; KRHRCAA; -.
DR OrthoDB; 1423329at2759; -.
DR PhylomeDB; P20483; -.
DR Reactome; R-DME-156711; Polo-like kinase mediated events.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DME-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DME-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR SignaLink; P20483; -.
DR BioGRID-ORCS; 43466; 0 hits in 3 CRISPR screens.
DR ChiTaRS; stg; fly.
DR GenomeRNAi; 43466; -.
DR PRO; PR:P20483; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003525; Expressed in cleaving embryo and 36 other tissues.
DR ExpressionAtlas; P20483; baseline and differential.
DR Genevisible; P20483; DM.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IMP:FlyBase.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007369; P:gastrulation; IMP:FlyBase.
DR GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR GO; GO:0007488; P:histoblast morphogenesis; IMP:FlyBase.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR CDD; cd01530; Cdc25; 1.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000751; MPI_Phosphatase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Hydrolase; Mitosis; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..479
FT /note="M-phase inducer phosphatase"
FT /id="PRO_0000198658"
FT DOMAIN 316..432
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 182..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /evidence="ECO:0000250"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 228
FT /note="A -> T (in Ref. 1; AAA28916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 54095 MW; 68483F3A285962CC CRC64;
MLWETIVEEN NCSMDCNISN NTSSSSSINK MSGSRRARRS LELMSMDQEE LSFYDDDVVP
QDQQRSASPE LMGLLSPEGS PQRFQIVRQP KILPAMGVSS DHTPARSFRI FNSLSSTCSM
ESSMDDEYME LFEMESQSQQ TALGFPSGLN SLISGQIKEQ PAAKSPAGLS MRRPSVRRCL
SMTESNTNST TTPPPKTPET ARDCFKRPEP PASANCSPIQ SKRHRCAAVE KENCPAPSPL
SQVTISHPPP LRKCMSLNDA EIMSALARSE NRNEPELIGD FSKAYALPLM EGRHRDLKSI
SSETVARLLK GEFSDKVASY RIIDCRYPYE FEGGHIEGAK NLYTTEQILD EFLTVQQTEL
QQQQNAESGH KRNIIIFHCE FSSERGPKMS RFLRNLDRER NTNAYPALHY PEIYLLHNGY
KEFFESHVEL CEPHAYRTML DPAYNEAYRH FRAKSKSWNG DGLGGATGRL KKSRSRLML
