PP2C4_SCHPO
ID PP2C4_SCHPO Reviewed; 383 AA.
AC O14156; Q9UR02;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein phosphatase 2C homolog 4;
DE Short=PP2C-4;
DE EC=3.1.3.16;
GN Name=ptc4; ORFNames=SPAC4A8.03c;
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], SUBUNIT, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10436019; DOI=10.1091/mbc.10.8.2647;
RA Gaits F., Russell P.;
RT "Vacuole fusion regulated by protein phosphatase 2C in fission yeast.";
RL Mol. Biol. Cell 10:2647-2654(1999).
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: Has a role in the regulation of vacuole fusion.
CC {ECO:0000269|PubMed:10436019}.
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. {ECO:0000269|PubMed:10436019}.
CC -!- INTERACTION:
CC O14156; Q09892: sty1; NbExp=4; IntAct=EBI-7593590, EBI-3648525;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10436019};
CC Peripheral membrane protein {ECO:0000269|PubMed:10436019}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AF140285; AAD27651.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB58554.1; -; Genomic_DNA.
DR PIR; T38772; T38772.
DR RefSeq; NP_593814.1; NM_001019244.2.
DR AlphaFoldDB; O14156; -.
DR SMR; O14156; -.
DR BioGRID; 279527; 4.
DR IntAct; O14156; 2.
DR MINT; O14156; -.
DR STRING; 4896.SPAC4A8.03c.1; -.
DR iPTMnet; O14156; -.
DR SwissPalm; O14156; -.
DR MaxQB; O14156; -.
DR PaxDb; O14156; -.
DR PRIDE; O14156; -.
DR EnsemblFungi; SPAC4A8.03c.1; SPAC4A8.03c.1:pep; SPAC4A8.03c.
DR GeneID; 2543095; -.
DR KEGG; spo:SPAC4A8.03c; -.
DR PomBase; SPAC4A8.03c; ptc4.
DR VEuPathDB; FungiDB:SPAC4A8.03c; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_021251_0_0_1; -.
DR InParanoid; O14156; -.
DR OMA; HRLTFQH; -.
DR PhylomeDB; O14156; -.
DR PRO; PR:O14156; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:PomBase.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; EXP: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; IDA:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; IMP:PomBase.
DR GO; GO:0061191; P:positive regulation of vacuole fusion, non-autophagic; IMP:PomBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW Protein phosphatase; Reference proteome; Vacuole.
FT CHAIN 1..383
FT /note="Protein phosphatase 2C homolog 4"
FT /id="PRO_0000057773"
FT DOMAIN 51..356
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 383 AA; 43569 MW; 88E00C2BDAE4B9BF CRC64;
MSIRFLKRLR APLYIQNAYC SKNYFYRSFI QYYSPSNGPY LKISMNKAPQ SLGLCTARGD
SPTNQDRMAY GYLNNLKDTT NRDSPFFYGL FDGHGGTECS EFLSTNLGKI IENQDLNDTE
KILKEVHSVG GYMAGLKPPF SLRTVLQSRD EDLLWRARLY YSFLQADMDY LTNYARPSPD
SAVPGAVGTV AIITSKNNLS YWESDSYIIH LAHVGDTRAL LCDSRTGRAH RLTFQHHPAD
VEEARRLRRY NMGFSRDSFG QKRFAWVANT RSFGDGYKLK KLGVVAEPQL TSIHSLRDDW
SFLTLLSDGI TDVVSDDEVV DIIKLSESPQ DAANNIIRYA QNVGAVDDIT CLVVRLPGWK
KRTINDFTKN LRLEKSAYHP RRS
