PP2B_SCHPO
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 03-AUG-2022, entry version 167.
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; 4896.SPBP4H10.04.1; -.
DR iPTMnet; Q12705; -.
DR MaxQB; Q12705; -.
DR PaxDb; Q12705; -.
DR PRIDE; Q12705; -.
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; MESFCCL; -.
DR PhylomeDB; Q12705; -.
DR Reactome; R-SPO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-SPO-4086398; Ca2+ pathway.
DR Reactome; R-SPO-5607763; CLEC7A (Dectin-1) induces NFAT activation.
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:0006874; P:cellular calcium ion homeostasis; IC:ComplexPortal.
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: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; PTHR45673; 1.
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 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
