ID   PP11_SCHPO              Reviewed;         327 AA.
AC   P13681;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1-1;
DE            EC=3.1.3.16;
GN   Name=dis2; Synonyms=bws1; ORFNames=SPBC776.02c;
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=SP557;
RX   PubMed=2544292; DOI=10.1016/0092-8674(89)90339-5;
RA   Booher R., Beach D.;
RT   "Involvement of a type 1 protein phosphatase encoded by bws1+ in fission
RT   yeast mitotic control.";
RL   Cell 57:1009-1016(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2544298; DOI=10.1016/0092-8674(89)90338-3;
RA   Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.;
RT   "The fission yeast dis2+ gene required for chromosome disjoining encodes
RT   one of two putative type 1 protein phosphatases.";
RL   Cell 57:997-1007(1989).
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   MUTANT CS.
RC   STRAIN=972 / HM123;
RX   PubMed=2170029; DOI=10.1016/0092-8674(90)90173-c;
RA   Kinoshita N., Ohkura H., Yanagida M.;
RT   "Distinct, essential roles of type 1 and 2A protein phosphatases in the
RT   control of the fission yeast cell division cycle.";
RL   Cell 63:405-415(1990).
RN   [5]
RP   PHOSPHORYLATION AT THR-316.
RX   PubMed=7957097; DOI=10.1002/j.1460-2075.1994.tb06865.x;
RA   Yamano H., Ishii K., Yanagida M.;
RT   "Phosphorylation of dis2 protein phosphatase at the C-terminal cdc2
RT   consensus and its potential role in cell cycle regulation.";
RL   EMBO J. 13:5310-5318(1994).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=22375062; DOI=10.1242/jcs.096826;
RA   Buttrick G.J., Lancaster T.C., Meadows J.C., Millar J.B.;
RT   "Plo1 phosphorylates Dam1 to promote chromosome bi-orientation in fission
RT   yeast.";
RL   J. Cell Sci. 125:1645-1651(2012).
CC   -!- FUNCTION: Essential role in cell cycle control. PP1 is perhaps required
CC       for exit from mitosis.
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: Oligomer.
CC   -!- INTERACTION:
CC       P13681; Q9UT08: paa1; NbExp=10; IntAct=EBI-4320127, EBI-16132377;
CC       P13681; Q12702: pab1; NbExp=9; IntAct=EBI-4320127, EBI-16132256;
CC       P13681; Q10428: par1; NbExp=12; IntAct=EBI-4320127, EBI-989357;
CC       P13681; P22194: sds22; NbExp=3; IntAct=EBI-4320127, EBI-16132213;
CC       P13681; O60132: tea4; NbExp=2; IntAct=EBI-4320127, EBI-1099982;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DISRUPTION PHENOTYPE: Simultaneous knockout of dam1 results in
CC       inviability. {ECO:0000269|PubMed:22375062}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {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; M27075; AAA74731.1; -; Genomic_DNA.
DR   EMBL; M27068; AAA89197.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA22875.1; -; Genomic_DNA.
DR   PIR; A32550; A32550.
DR   RefSeq; NP_596317.1; NM_001022239.2.
DR   AlphaFoldDB; P13681; -.
DR   SMR; P13681; -.
DR   BioGRID; 277707; 104.
DR   DIP; DIP-61473N; -.
DR   IntAct; P13681; 10.
DR   STRING; 284812.P13681; -.
DR   iPTMnet; P13681; -.
DR   MaxQB; P13681; -.
DR   PaxDb; 4896-SPBC776-02c-1; -.
DR   EnsemblFungi; SPBC776.02c.1; SPBC776.02c.1:pep; SPBC776.02c.
DR   GeneID; 2541193; -.
DR   KEGG; spo:SPBC776.02c; -.
DR   PomBase; SPBC776.02c; dis2.
DR   VEuPathDB; FungiDB:SPBC776.02c; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   HOGENOM; CLU_004962_8_3_1; -.
DR   InParanoid; P13681; -.
DR   OMA; EEHEIRY; -.
DR   PhylomeDB; P13681; -.
DR   PRO; PR:P13681; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:1902716; C:cell cortex of growing cell tip; IDA:PomBase.
DR   GO; GO:0140472; C:cell cortex of non-growing cell tip; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0051286; C:cell tip; IDA:PomBase.
DR   GO; GO:0061638; C:CENP-A containing chromatin; IDA:PomBase.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:1990567; C:DPS complex; IDA:PomBase.
DR   GO; GO:0000791; C:euchromatin; EXP:PomBase.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IPI:PomBase.
DR   GO; GO:0072357; C:PTW/PP1 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:0004722; F:protein serine/threonine phosphatase activity; IDA:PomBase.
DR   GO; GO:0180005; F:RNA polymerase II CTD heptapeptide repeat T4 phosphatase activity; EXP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR   GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; IC:PomBase.
DR   GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:PomBase.
DR   GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IGI:PomBase.
DR   GO; GO:2000784; P:positive regulation of establishment of cell polarity regulating cell shape; EXP:PomBase.
DR   GO; GO:0031536; P:positive regulation of exit from mitosis; EXP:PomBase.
DR   GO; GO:1903068; P:positive regulation of protein localization to cell tip; EXP:PomBase.
DR   GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IMP:PomBase.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; EXP:PomBase.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
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   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF300; SERINE_THREONINE-PROTEIN PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 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; Hydrolase; Manganese; Metal-binding; Mitosis;
KW   Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..327
FT                   /note="Serine/threonine-protein phosphatase PP1-1"
FT                   /id="PRO_0000058818"
FT   REGION          305..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         316
FT                   /note="Phosphothreonine; by CDC2"
FT                   /evidence="ECO:0000269|PubMed:7957097"
FT   MUTAGEN         245
FT                   /note="R->Q: Cold-sensitive phenotype."
FT   CONFLICT        17
FT                   /note="E -> EGE (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   327 AA;  37636 MW;  1106BB9C7D6FDCFB CRC64;
     MSNPDVDLDS IIDRLLEVRG SRPGRQVQLS EDEIRFLCNK AREIFISQPI LLELEAPLKI
     CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL EVICLLLAYK IKYPENFFIL
     RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN
     SMDQIQRIMR PTDVPDTGLL CDLLWSDPDK DLTGWGDNDR GVSFTFGPDV VSRFLHKHDM
     DLVCRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK
     KQRYGYQGSS QNWHMTPPRK NKTGNSK
//