PP11_SCHPO
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 03-AUG-2022, entry version 184.
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).
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 -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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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; 102.
DR DIP; DIP-61473N; -.
DR IntAct; P13681; 10.
DR STRING; 4896.SPBC776.02c.1; -.
DR iPTMnet; P13681; -.
DR MaxQB; P13681; -.
DR PaxDb; P13681; -.
DR PRIDE; P13681; -.
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:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA: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:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:PomBase.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IGI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:PomBase.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP: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 GO; GO:1904594; P:regulation of termination of RNA polymerase II transcription; IMP: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 InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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; 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
