ID MPIP_SCHPO Reviewed; 596 AA. AC P06652; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 07-APR-2021, entry version 170. DE RecName: Full=M-phase inducer phosphatase; DE EC=3.1.3.48; DE AltName: Full=Mitosis initiation protein; DE AltName: Full=P80; GN Name=cdc25 {ECO:0000303|PubMed:3955656, ECO:0000312|PomBase:SPAC24H6.05}; GN ORFNames=SPAC24H6.05 {ECO:0000312|PomBase:SPAC24H6.05}; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=3955656; DOI=10.1016/0092-8674(86)90546-5; RA Russell P., Nurse P.; RT "cdc25+ functions as an inducer in the mitotic control of fission yeast."; RL Cell 45:145-153(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAD24, AND RP PHOSPHORYLATION. RX PubMed=15629716; DOI=10.1016/j.molcel.2004.11.043; RA Lopez-Aviles S., Grande M., Gonzalez M., Helgesen A.L., Alemany V., RA Sanchez-Piris M., Bachs O., Millar J.B., Aligue R.; RT "Inactivation of the Cdc25 phosphatase by the stress-activated Srk1 kinase RT in fission yeast."; RL Mol. Cell 17:49-59(2005). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-178, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). CC -!- FUNCTION: Tyrosine protein phosphatase which functions as a dosage- CC dependent inducer of mitotic progression (PubMed:3955656). Directly CC dephosphorylates cdc2 and stimulates its kinase activity (By CC similarity). Required for the G2/M transition of the cell cycle CC (PubMed:15629716). {ECO:0000250|UniProtKB:P30305, CC ECO:0000269|PubMed:15629716, ECO:0000269|PubMed:3955656}. 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 Evidence={ECO:0000250|UniProtKB:Q8GY31}; CC -!- SUBUNIT: Interacts with rad24 during G2 in a srk1-dependent manner; the CC interaction is increased during osmostress. CC {ECO:0000269|PubMed:15629716}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15629716}. Nucleus CC {ECO:0000269|PubMed:15629716}. Note=Accumulates in the nucleus in CC cycling cells; nuclear localization is the highest in G2. CC {ECO:0000269|PubMed:15629716}. CC -!- PTM: Phosphorylated by srk1 in the N-terminus; phosphorylation promotes CC nuclear exclusion. {ECO:0000269|PubMed:15629716}. CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA35294.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13158; AAA35294.1; ALT_FRAME; Genomic_DNA. DR EMBL; CU329670; CAA90849.1; -; Genomic_DNA. DR PIR; S62407; S62407. DR RefSeq; NP_592947.1; NM_001018348.2. DR SMR; P06652; -. DR BioGRID; 279086; 93. DR IntAct; P06652; 2. DR STRING; 4896.SPAC24H6.05.1; -. DR iPTMnet; P06652; -. DR MaxQB; P06652; -. DR PaxDb; P06652; -. DR PRIDE; P06652; -. DR EnsemblFungi; SPAC24H6.05.1; SPAC24H6.05.1:pep; SPAC24H6.05. DR PomBase; SPAC24H6.05; cdc25. DR VEuPathDB; FungiDB:SPAC24H6.05; -. DR eggNOG; KOG3772; Eukaryota. DR HOGENOM; CLU_017900_0_0_1; -. DR InParanoid; P06652; -. DR OMA; LSMFESP; -. DR PhylomeDB; P06652; -. DR Reactome; R-SPO-156711; Polo-like kinase mediated events. DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress. DR Reactome; R-SPO-5625740; RHO GTPases activate PKNs. DR Reactome; R-SPO-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain. DR Reactome; R-SPO-69202; Cyclin E associated events during G1/S transition. DR Reactome; R-SPO-69273; Cyclin A/B1/B2 associated events during G2/M transition. DR Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-SPO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex. DR PRO; PR:P06652; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IDA:PomBase. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:0005634; C:nucleus; IDA:PomBase. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:PomBase. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:PomBase. DR GO; GO:0051728; P:cell cycle switching, mitotic to meiotic cell cycle; IMP:PomBase. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase. DR GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IMP:PomBase. DR GO; GO:0008361; P:regulation of cell size; NAS:PomBase. DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:PomBase. DR GO; GO:0072435; P:response to mitotic G2 DNA damage checkpoint signaling; IMP:PomBase. DR GO; GO:0072428; P:signal transduction involved in intra-S DNA damage checkpoint; IMP:PomBase. 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; Cytoplasm; Hydrolase; Mitosis; Nucleus; KW Phosphoprotein; Protein phosphatase; Reference proteome. FT CHAIN 1..596 FT /note="M-phase inducer phosphatase" FT /id="PRO_0000198661" FT DOMAIN 429..533 FT /note="Rhodanese" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173" FT ACT_SITE 480 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000250|UniProtKB:Q16828" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" SQ SEQUENCE 596 AA; 66566 MW; CF8D430FC7BD38C1 CRC64; MDSPLSSLSF TNTLSGKRNV LRPAARELKL MSDRNANQEL DFFFPKSKHI ASTLVDPFGK TCSTASPASS LAADMSMNMH IDESPALPTP RRTLFRSLSC TVETPLANKT IVSPLPESPS NDALTESYFF RQPASKYSIT QDSPRVSSTI AYSFKPKASI ALNTTKSEAT RSSLSSSSFD SYLRPNVSRS RSSGNAPPFL RSRSSSSYSI NKKKGTSGGQ ATRHLTYALS RTCSQSSNTT SLLESCLTDD TDDFELMSDH EDTFTMGKVA DLPESSVELV EDAASIQRPN SDFGACNDNS LDDLFQASPI KPIDMLPKIN KDIAFPSLKV RSPSPMAFAM QEDAEYDEQD TPVLRRTQSM FLNSTRLGLF KSQDLVCVTP KQSTKESERF ISSHVEDLSL PCFAVKEDSL KRITQETLLG LLDGKFKDIF DKCIIIDCRF EYEYLGGHIS TAVNLNTKQA IVDAFLSKPL THRVALVFHC EHSAHRAPHL ALHFRNTDRR MNSHRYPFLY YPEVYILHGG YKSFYENHKN RCDPINYVPM NDASHVMTCT KAMNNFKRNA TFMRTKSYTF GQSVLASPDV NDSPTAMHSL STLRRF //