PPE1_SCHPO
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 03-AUG-2022, entry version 169.
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; 4896.SPCC1739.12.1; -.
DR iPTMnet; P36614; -.
DR MaxQB; P36614; -.
DR PaxDb; P36614; -.
DR PRIDE; P36614; -.
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 OMA; CQNKYGN; -.
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:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
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:1903379; P:regulation of mitotic chromosome condensation; IGI:PomBase.
DR GO; GO:1903432; P:regulation of TORC1 signaling; ISO:PomBase.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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
