PP2A2_SCHPO
ID PP2A2_SCHPO Reviewed; 322 AA.
AC P23636;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit;
DE EC=3.1.3.16;
GN Name=ppa2; ORFNames=SPBC16H5.07c;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10407269;
RX DOI=10.1002/(sici)1097-0061(199907)15:10a<893::aid-yea430>3.0.co;2-s;
RA Xiang Z., Lyne M.H., Wood V., Rajandream M.A., Barrell B.G., Aves S.J.;
RT "DNA sequencing and analysis of a 67.4 kb region from the right arm of
RT Schizosaccharomyces pombe chromosome II reveals 28 open reading frames
RT including the genes his5, pol5, ppa2, rip1, rpb8 and skb1.";
RL Yeast 15:893-901(1999).
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).
CC -!- FUNCTION: Essential role in cell cycle control. PP2A may be involved in
CC controlling the entry into mitosis, possibly acting as an inhibitor.
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 -!- MISCELLANEOUS: Retarded cell growth is produced by disruption of ppa2.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC {ECO:0000305}.
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DR EMBL; M58519; AAA63579.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17905.1; -; Genomic_DNA.
DR PIR; B36076; B36076.
DR RefSeq; NP_595940.1; NM_001021848.2.
DR AlphaFoldDB; P23636; -.
DR SMR; P23636; -.
DR BioGRID; 276610; 111.
DR DIP; DIP-61477N; -.
DR IntAct; P23636; 1.
DR STRING; 4896.SPBC16H5.07c.1; -.
DR MaxQB; P23636; -.
DR PaxDb; P23636; -.
DR EnsemblFungi; SPBC16H5.07c.1; SPBC16H5.07c.1:pep; SPBC16H5.07c.
DR GeneID; 2540072; -.
DR KEGG; spo:SPBC16H5.07c; -.
DR PomBase; SPBC16H5.07c; ppa2.
DR VEuPathDB; FungiDB:SPBC16H5.07c; -.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; P23636; -.
DR OMA; EGYNWGQ; -.
DR PhylomeDB; P23636; -.
DR Reactome; R-SPO-198753; ERK/MAPK targets.
DR Reactome; R-SPO-202670; ERKs are inactivated.
DR Reactome; R-SPO-389513; CTLA4 inhibitory signaling.
DR Reactome; R-SPO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-SPO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P23636; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; 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:0004721; F:phosphoprotein phosphatase activity; IMP:PomBase.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990813; P:meiotic centromeric cohesion protection; IMP:PomBase.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS: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 3: Inferred from homology;
KW Cell cycle; Cell division; Hydrolase; Manganese; Metal-binding;
KW Methylation; Mitosis; Protein phosphatase; Reference proteome.
FT CHAIN 1..322
FT /note="Major serine/threonine-protein phosphatase PP2A-2
FT catalytic subunit"
FT /id="PRO_0000058872"
FT ACT_SITE 131
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 322
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 36489 MW; 8709C544FAFEDD85 CRC64;
MSIDPANDSK LAPEANDATL GDVDRWIEQL KKCEPLSEAD VEMLCDKARE VLCQENNVQP
VRNPVTVCGD IHGQFHDLME LFKIGGDVPD MNYLFMGDYV DRGYHSVETV SLLVAMKLRY
PNRITILRGN HESRQITQVY GFYDECLRKY GSANVWKHFT NLFDYFPLTA LIEDRIFCLH
GGLSPSIDSL DHVRTLDRVQ EVPHEGPMCD LLWSDPDDRC GWGISPRGAG YTFGQDISET
FNHANGLSLT ARAHQLVMEG FNWAHDGDVV TIFSAPNYCY RCGNQAAILE VDDTMNQVFL
QFDPAPREGE PVIARRTPDY FL
