PP2C5_SCHPO
ID PP2C5_SCHPO Reviewed; 444 AA.
AC O14189; O42655;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 4.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein phosphatase 2C homolog C10F6.17c;
DE EC=3.1.3.16;
DE AltName: Full=Pyruvate dehydrogenase (Lipoamide) phosphatase C10F6.17c;
GN ORFNames=SPAC10F6.17c;
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 [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 [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in regulation of pyruvate dehydrogenase activity.
CC {ECO:0000250}.
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=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; CU329670; CAA15730.2; -; Genomic_DNA.
DR RefSeq; NP_593268.2; NM_001018665.2.
DR AlphaFoldDB; O14189; -.
DR SMR; O14189; -.
DR BioGRID; 279440; 1.
DR STRING; 4896.SPAC10F6.17c.1; -.
DR iPTMnet; O14189; -.
DR MaxQB; O14189; -.
DR PaxDb; O14189; -.
DR EnsemblFungi; SPAC10F6.17c.1; SPAC10F6.17c.1:pep; SPAC10F6.17c.
DR GeneID; 2543002; -.
DR KEGG; spo:SPAC10F6.17c; -.
DR PomBase; SPAC10F6.17c; -.
DR VEuPathDB; FungiDB:SPAC10F6.17c; -.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_021928_1_0_1; -.
DR InParanoid; O14189; -.
DR OMA; SHFRYAP; -.
DR PhylomeDB; O14189; -.
DR PRO; PR:O14189; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosphatase activity; ISO: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:0006091; P:generation of precursor metabolites and energy; NAS:PomBase.
DR GO; GO:1904184; P:positive regulation of pyruvate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..444
FT /note="Protein phosphatase 2C homolog C10F6.17c"
FT /id="PRO_0000352809"
FT DOMAIN 85..439
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 49741 MW; CF52B91186DB64E8 CRC64;
MNFFTSAVGS KVFKRNNFKY VAIAASSIGL AAYHIRKDAI ALDIPNSTYQ HVSKNRVPPT
DGDGITKRLK EFERTVTVNK DGIFRYDFNQ VASNDPCEDD HVEVIDRNID EGNWYFWGIF
DGHSGWNTSL FLRQHLVPAV VRELQKCTAS YYHQNACPSS LALDKSISEA FAKVDHQIVH
EHVSHVFNNP ESLQVAASLL LPALSGSCAL LTSYSAKSKS LQVACTGDSR AVLGECTPDG
SWEAIPLSRD QTGMNPDEAS RLEVEHPGEE VLRNNRILGR LMPSRAFGDA RYKWSQEISE
RLHREYFSAS PIPVKTPPYV TAVPEIESIT VNPKKHRFLI MASDGLWDTM SSEQAVQLVG
EWADTVLGKT TNEKNTTQDD KQSWSLFKKT SKVIDDNAAT HLIRHSLGGS DQRISALLTL
TYPISRRYRD DITVTVIFFD EKTL
