ID   PPE1_SCHPO              Reviewed;         305 AA.
AC   P36614;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Serine/threonine-protein phosphatase ppe1;
DE            EC=3.1.3.16;
DE   AltName: Full=Phosphatase esp1;
GN   Name=ppe1; Synonyms=esp1, ppx1; ORFNames=SPCC1739.12;
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].
RC   STRAIN=972 / HM123;
RX   PubMed=8387356; DOI=10.1091/mbc.4.3.303;
RA   Shimanuki M., Kinoshita N., Ohkura H., Yoshida T., Toda T., Yanagida M.;
RT   "Isolation and characterization of the fission yeast protein phosphatase
RT   gene ppe1+ involved in cell shape control and mitosis.";
RL   Mol. Biol. Cell 4:303-313(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8387358; DOI=10.1091/mbc.4.3.337;
RA   Matsumoto T., Beach D.;
RT   "Interaction of the pim1/spi1 mitotic checkpoint with a protein
RT   phosphatase.";
RL   Mol. Biol. Cell 4:337-345(1993).
RN   [3]
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   [4]
RP   FUNCTION, INTERACTION WITH STS5; ECK1 AND MIS12, AND SUBCELLULAR LOCATION.
RX   PubMed=12773390; DOI=10.1093/emboj/cdg266;
RA   Goshima G., Iwasaki O., Obuse C., Yanagida M.;
RT   "The role of Ppe1/PP6 phosphatase for equal chromosome segregation in
RT   fission yeast kinetochore.";
RL   EMBO J. 22:2752-2763(2003).
CC   -!- FUNCTION: Has a role in chromosome segregation. May provide a dynamic
CC       connection between kinetochore microtubules and kinetochore chromatin.
CC       Negatively regulates mis12. {ECO:0000269|PubMed:12773390}.
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   -!- SUBUNIT: Interacts with sts5, ekc1 and mis12.
CC       {ECO:0000269|PubMed:12773390}.
CC   -!- INTERACTION:
CC       P36614; O74511: ekc1; NbExp=2; IntAct=EBI-1153118, EBI-1153096;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773390}.
CC       Note=Associated with chromatin.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D13712; BAA02865.1; -; Genomic_DNA.
DR   EMBL; Z18925; CAA79358.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA20786.1; -; Genomic_DNA.
DR   PIR; A47727; A47727.
DR   RefSeq; NP_588420.1; NM_001023411.2.
DR   AlphaFoldDB; P36614; -.
DR   SMR; P36614; -.
DR   BioGRID; 275341; 35.
DR   IntAct; P36614; 2.
DR   STRING; 284812.P36614; -.
DR   iPTMnet; P36614; -.
DR   MaxQB; P36614; -.
DR   PaxDb; 4896-SPCC1739-12-1; -.
DR   EnsemblFungi; SPCC1739.12.1; SPCC1739.12.1:pep; SPCC1739.12.
DR   GeneID; 2538758; -.
DR   KEGG; spo:SPCC1739.12; -.
DR   PomBase; SPCC1739.12; ppe1.
DR   VEuPathDB; FungiDB:SPCC1739.12; -.
DR   eggNOG; KOG0373; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; P36614; -.
DR   OMA; MEGFKYH; -.
DR   PhylomeDB; P36614; -.
DR   PRO; PR:P36614; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; IPI:PomBase.
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:0004721; F:phosphoprotein phosphatase activity; IGI:PomBase.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:2001211; P:negative regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway; IMP:PomBase.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:1903432; P:regulation of TORC1 signaling; ISO:PomBase.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF10; SERINE_THREONINE-PROTEIN PHOSPHATASE 6 CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell shape; Hydrolase; Manganese; Metal-binding;
KW   Mitosis; Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..305
FT                   /note="Serine/threonine-protein phosphatase ppe1"
FT                   /id="PRO_0000058882"
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   305 AA;  35259 MW;  001980A1CC7646D7 CRC64;
     MFDLDEWIAT VRKCKYLPEH QLKRLCEMVK VILMEESNIQ PVRTPVTVCG DIHGQFYDLL
     ELFRVGGELP STNYIFMGDF VDRGYFSLET FTLFMLLKAR YPDKITLLRG NHESRQITQV
     YGFYDECQTK YGNANVWKYC CQVFDFLTLA AVIDNKILCV HGGLSPEVRT LDQIRILARA
     QEIPHEGSFC DLMWSDPEDI ESWTVSPRGA GWLFGSKVTT EFSQINDLTL IARAHQLVQE
     GYKYHFADKN LVTVWSAPNY CYRCGNVASV MKVDESLEPE FRIFSAVADE DRTVPPSRKR
     SEYFI
//