PP2C1_SCHPO
ID PP2C1_SCHPO Reviewed; 347 AA.
AC P40371;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein phosphatase 2C homolog 1;
DE Short=PP2C-1;
DE EC=3.1.3.16;
GN Name=ptc1; ORFNames=SPCC4F11.02;
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 [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8196617; DOI=10.1128/mcb.14.6.3742-3751.1994;
RA Shiozaki K., Akhavan-Niaki H., McGowan C.H., Russell P.;
RT "Protein phosphatase 2C, encoded by ptc1+, is important in the heat shock
RT response of Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 14:3742-3751(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: It has a serine and threonine phosphatase activity. Has a
CC specialized role in the heat shock response. May be responsible for the
CC dephosphorylation of hsp90. Also has a role in maintaining osmotic
CC stability.
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 -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; L26970; AAA35327.1; -; mRNA.
DR EMBL; CU329672; CAB55768.1; -; Genomic_DNA.
DR PIR; A56058; A56058.
DR RefSeq; NP_588401.1; NM_001023392.2.
DR AlphaFoldDB; P40371; -.
DR SMR; P40371; -.
DR BioGRID; 276058; 323.
DR IntAct; P40371; 6.
DR STRING; 4896.SPCC4F11.02.1; -.
DR iPTMnet; P40371; -.
DR MaxQB; P40371; -.
DR PaxDb; P40371; -.
DR PRIDE; P40371; -.
DR EnsemblFungi; SPCC4F11.02.1; SPCC4F11.02.1:pep; SPCC4F11.02.
DR GeneID; 2539495; -.
DR KEGG; spo:SPCC4F11.02; -.
DR PomBase; SPCC4F11.02; ptc1.
DR VEuPathDB; FungiDB:SPCC4F11.02; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_1_1_1; -.
DR InParanoid; P40371; -.
DR OMA; ASKWCGS; -.
DR PhylomeDB; P40371; -.
DR PRO; PR:P40371; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:1990439; F:MAP kinase serine/threonine phosphatase 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; IMP:PomBase.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:PomBase.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:PomBase.
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; IPR000222; PP2C_BS.
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; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome; Stress response.
FT CHAIN 1..347
FT /note="Protein phosphatase 2C homolog 1"
FT /id="PRO_0000057770"
FT DOMAIN 71..323
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 38676 MW; 50675A545502403B CRC64;
MKGSHPNAGS LLEPLHKLNP FSENSTSGHR KNASDHSADG ETRPIAIEMK DSKGNTVPVG
NSRPSKASNW LAGLMEDKNQ RWRRSMEDTH ICLYDFGGNQ DDGFVAVYDG HAGIQASDYC
QKNLHKVLLE KVRNEPDRLV TDLMDETFVE VNSKIAKATH NDICGCTAAV AFFRYEKNRT
RRVLYTANAG DARIVLCRDG KAIRLSYDHK GSDANESRRV TQLGGLMVQN RINGVLAVTR
ALGDTYLKEL VSAHPFTTET RIWNGHDEFF IIACDGLWDV VSDQEAVDFV RNFVSPREAA
VRLVEFALKR LSTDNITCIV VNLTRNPGDL DDSGLTADND SYSNDYY
