ID   MPIP_YEAST              Reviewed;         554 AA.
AC   P23748; D6VZL1;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   02-SEP-2026, entry version 199.
DE   RecName: Full=M-phase inducer phosphatase;
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:P30303};
DE   AltName: Full=Mitosis initiation protein MIH1;
DE   AltName: Full=Mitotic inducer homolog;
GN   Name=MIH1; OrderedLocusNames=YMR036C {ECO:0000312|SGD:S000004639};
GN   ORFNames=YM9532.01C, YM9973.10C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2649252; DOI=10.1016/0092-8674(89)90967-7;
RA   Russell P., Moreno S., Reed S.I.;
RT   "Conservation of mitotic controls in fission and budding yeasts.";
RL   Cell 57:295-303(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872; DOI=10.1038/387s090;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Terminates the cell cycle delay. Reverses the CDC28
CC       phosphorylation catalyzed by SWE1.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978; EC=3.1.3.48;
CC         Evidence={ECO:0000250|UniProtKB:P30303};
CC   -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR   EMBL; J04846; AAA57223.1; -; Genomic_DNA.
DR   EMBL; Z48502; CAA88402.1; -; Genomic_DNA.
DR   EMBL; Z49213; CAA89152.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09935.1; -; Genomic_DNA.
DR   PIR; A32386; A32386.
DR   RefSeq; NP_013750.1; NM_001182533.1.
DR   AlphaFoldDB; P23748; -.
DR   SMR; P23748; -.
DR   BioGRID; 35208; 165.
DR   DIP; DIP-2713N; -.
DR   FunCoup; P23748; 370.
DR   IntAct; P23748; 22.
DR   MINT; P23748; -.
DR   STRING; 4932.YMR036C; -.
DR   iPTMnet; P23748; -.
DR   PaxDb; 4932-YMR036C; -.
DR   PeptideAtlas; P23748; -.
DR   EnsemblFungi; YMR036C_mRNA; YMR036C; YMR036C.
DR   GeneID; 855052; -.
DR   KEGG; sce:YMR036C; -.
DR   AGR; SGD:S000004639; -.
DR   SGD; S000004639; MIH1.
DR   VEuPathDB; FungiDB:YMR036C; -.
DR   eggNOG; KOG3772; Eukaryota.
DR   HOGENOM; CLU_036651_0_0_1; -.
DR   InParanoid; P23748; -.
DR   OMA; CESFYNS; -.
DR   OrthoDB; 26523at2759; -.
DR   BioCyc; YEAST:G3O-32741-MONOMER; -.
DR   Reactome; R-SCE-156711; Polo-like kinase mediated events.
DR   Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-SCE-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-SCE-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR   Reactome; R-SCE-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-SCE-69601; Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-SCE-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR   BioGRID-ORCS; 855052; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P23748; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P23748; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
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:0051231; P:spindle elongation; IMP:SGD.
DR   CDD; cd01530; Cdc25; 1.
DR   FunFam; 3.40.250.10:FF:000021; M-phase inducer phosphatase cdc-25.2; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR000751; MPI_Phosphatase.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR   PANTHER; PTHR10828:SF17; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR00716; MPIPHPHTASE.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Hydrolase; Mitosis; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..554
FT                   /note="M-phase inducer phosphatase"
FT                   /id="PRO_0000198662"
FT   DOMAIN          261..373
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          72..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..130
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..171
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..466
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000250"
FT   CONFLICT        238..239
FT                   /note="ND -> MT (in Ref. 1; AAA57223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241..248
FT                   /note="FPRISPET -> SLEFLQKR (in Ref. 1; AAA57223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365..367
FT                   /note="FDN -> LT (in Ref. 1; AAA57223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        475..554
FT                   /note="ILSKSSMSSNSNLSTSHMLLMDGLDTPSYFSFEDERGNHQQVSGDEEQDGDF
FT                   TFVGSDREDLPRPARRSLFPSLETEDKK -> S (in Ref. 1; AAA57223)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   554 AA;  63358 MW;  DBD85D02CF48CA6F CRC64;
     MNNIFHGTED ECANEDVLSF QKISLKSPFG KKKNIFRNVQ TFFKSKSKHS NVDDDLINKE
     NLAFDKSPLL TNHRSKEIDG PSPNIKQLGH RDELDENENE NDDIVLSMHF ASQTLQSPTR
     NSSRRSLTNN RDNDLLSRIK YPGSPQRSSS FSRSRSLSRK PSMNSSSNSS RRVQRQDGKI
     PRSSRKSSQK FSNITQNTLN FTSASSSPLA PNSVGVKCFE SCLAKTQIPY YYDDRNSNDF
     FPRISPETLK NILQNNMCES FYNSCRIIDC RFEYEYTGGH IINSVNIHSR DELEYEFIHK
     VLHSDTSNNN TLPTLLIIHC EFSSHRGPSL ASHLRNCDRI INQDHYPKLF YPDILILDGG
     YKAVFDNFPE LCYPRQYVGM NSQENLLNCE QEMDKFRRES KRFATKNNSF RKLASPSNPN
     FFYRDSHQSS TTMASSALSF RFEPPPKLSL NHRRVSSGSS LNSSESTGDE NFFPILSKSS
     MSSNSNLSTS HMLLMDGLDT PSYFSFEDER GNHQQVSGDE EQDGDFTFVG SDREDLPRPA
     RRSLFPSLET EDKK
//