ID   PP2B_SCHPO              Reviewed;         554 AA.
AC   Q12705; Q9P7E4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit;
DE            EC=3.1.3.16;
GN   Name=ppb1; ORFNames=SPBC1346.01c, SPBP4H10.04;
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].
RX   PubMed=7983142; DOI=10.1242/jcs.107.7.1725;
RA   Yoshida T., Toda T., Yanagida M.;
RT   "A calcineurin-like gene ppb1+ in fission yeast: mutant defects in
RT   cytokinesis, cell polarity, mating and spindle pole body positioning.";
RL   J. Cell Sci. 107:1725-1735(1994).
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).
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase.
CC       This subunit may have a role in the calmodulin activation of
CC       calcineurin. Appears to be involved in cytokinesis, mating, transport,
CC       nuclear and spindle pole body positioning, and cell shape.
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=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Composed of two components (A and B), the A component is the
CC       catalytic subunit and the B component confers calcium sensitivity.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D28955; BAA06081.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB83162.1; -; Genomic_DNA.
DR   PIR; T45137; T45137.
DR   PIR; T50310; T50310.
DR   RefSeq; NP_596178.1; NM_001022097.2.
DR   AlphaFoldDB; Q12705; -.
DR   SMR; Q12705; -.
DR   BioGRID; 276568; 46.
DR   ComplexPortal; CPX-597; Calcineurin complex.
DR   STRING; 284812.Q12705; -.
DR   iPTMnet; Q12705; -.
DR   MaxQB; Q12705; -.
DR   PaxDb; 4896-SPBP4H10-04-1; -.
DR   EnsemblFungi; SPBP4H10.04.1; SPBP4H10.04.1:pep; SPBP4H10.04.
DR   GeneID; 2540024; -.
DR   KEGG; spo:SPBP4H10.04; -.
DR   PomBase; SPBP4H10.04; ppb1.
DR   VEuPathDB; FungiDB:SPBP4H10.04; -.
DR   eggNOG; KOG0375; Eukaryota.
DR   HOGENOM; CLU_004962_6_0_1; -.
DR   InParanoid; Q12705; -.
DR   OMA; YPAACNF; -.
DR   PhylomeDB; Q12705; -.
DR   PRO; PR:Q12705; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005955; C:calcineurin complex; IPI:ComplexPortal.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR   GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR   GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; IMP:PomBase.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IBA:GO_Central.
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; IDA:PomBase.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IMP:PomBase.
DR   GO; GO:0071277; P:cellular response to calcium ion; IMP:PomBase.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IGI:PomBase.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; NAS:ComplexPortal.
DR   GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IMP:PomBase.
DR   GO; GO:1903473; P:positive regulation of mitotic actomyosin contractile ring contraction; IMP:PomBase.
DR   GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IGI:PomBase.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IMP:ComplexPortal.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0030100; P:regulation of endocytosis; ISO:PomBase.
DR   CDD; cd07416; MPP_PP2B; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041751; MPP_PP2B.
DR   InterPro; IPR043360; PP2B.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR   PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 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   3: Inferred from homology;
KW   Calmodulin-binding; Cell shape; Hydrolase; Iron; Manganese; Metal-binding;
KW   Protein phosphatase; Reference proteome; Zinc.
FT   CHAIN           1..554
FT                   /note="Serine/threonine-protein phosphatase 2B catalytic
FT                   subunit"
FT                   /id="PRO_0000058835"
FT   REGION          411..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        12
FT                   /note="I -> T (in Ref. 1; BAA06081)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129..130
FT                   /note="KL -> EI (in Ref. 1; BAA06081)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   554 AA;  63714 MW;  D27ACA21AE2F3E19 CRC64;
     MTSGPHNLED PIVRAIRQKN QAPSHDFTIF VQEDGSSVST LDRVVKNVQA PATYIPTDVE
     FFDINEPDKP DLHFLRNHFI REGRLSEEQT LYIIKKATEI LKSEDNLIEV DAPVTVCGDI
     HGQYYDLMKL FEVGGNPANT QYLFLGDYVD RGYFSIECLL YLWALKIWYP KTLWLLRGNH
     ECAHLTDYFT FKLECTHKYN IKVYEACLQS FNALPLAAIM NKQFLCVHGG LSPELHTLND
     IRMINRFCEP PTHGLMCDLL WSDPLEDFGS EKSNKHFIHN NVRGCSYFYS YQAVCTFLEN
     NNLLSVIRAH EAQDVGYRMY RKTKTTGFPS LMTIFSAPNY LDVYNNKAAV LKYENNVMNI
     RQFNCSPHPY WLPNFMDVFT WSLPFVGEKV SEMLISMLNI CSKEELYETD LKESAPTQHK
     QPAPSENENK ADQEIDIEAR RQIIKNKIMA IGRISRVFSV LREERESVSE LKNVSGTQRL
     PAGTLMLGAE GIKNAINSFD DARKLDIQNE RLPPSNSRRR STDLKAFEEV MNSSEDDTSI
     DHLVERFADK KSSL
//