MPIP_SCHPO
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 03-AUG-2022, entry version 175.
DE RecName: Full=M-phase inducer phosphatase;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:P30303};
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.
RX DOI=10.1007/BF00435510;
RA Grallert B., Sipiczki M.;
RT "Initiation of the second meiotic division in Schizosaccharomyces pombe
RT shares common functions with that of mitosis.";
RL Curr. Genet. 15:231-233(1989).
RN [4]
RP FUNCTION.
RX PubMed=7498766; DOI=10.1093/genetics/140.4.1235;
RA Iino Y., Hiramine Y., Yamamoto M.;
RT "The role of cdc2 and other genes in meiosis in Schizosaccharomyces
RT pombe.";
RL Genetics 140:1235-1245(1995).
RN [5]
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 [6]
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 and meiotic progression (PubMed:3955656,
CC Ref.3, PubMed:7498766). Directly dephosphorylates cdc2 and stimulates
CC its kinase activity (By similarity). Required for the G2/M transition
CC of the cell cycle (PubMed:15629716). Required for induction of meiosis
CC II (Ref.3, PubMed:7498766). {ECO:0000250|UniProtKB:P30305,
CC ECO:0000269|PubMed:15629716, ECO:0000269|PubMed:3955656,
CC ECO:0000269|Ref.3}.
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:P30303};
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};
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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 AlphaFoldDB; P06652; -.
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; PMNDASH; -.
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-5689880; Ub-specific processing proteases.
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-69656; Cyclin A:Cdk2-associated events at S phase entry.
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: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:0031569; P:mitotic G2 cell size control checkpoint signaling; IMP:PomBase.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0110044; P:regulation of cell cycle switching, mitotic to meiotic cell cycle; IMP:PomBase.
DR GO; GO:0008361; P:regulation of cell size; NAS:PomBase.
DR GO; GO:0072435; P:response to mitotic G2 DNA damage checkpoint signaling; 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 REGION 174..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
