PPM1G_CAEEL
ID PPM1G_CAEEL Reviewed; 491 AA.
AC P49595; Q8MNS3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein phosphatase ppm-1.G {ECO:0000305};
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2C isoform gamma homolog {ECO:0000305};
DE Short=PP2C-gamma {ECO:0000305};
DE AltName: Full=Protein phosphatase magnesium-dependent 1 gamma homolog {ECO:0000305};
GN Name=ppm-1.G {ECO:0000312|WormBase:F42G9.1a};
GN ORFNames=F42G9.1 {ECO:0000312|WormBase:F42G9.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F42G9.1a};
CC IsoId=P49595-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F42G9.1b};
CC IsoId=P49595-2; Sequence=VSP_060334;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; BX284603; CCD61882.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD61883.1; -; Genomic_DNA.
DR PIR; T16354; T16354.
DR RefSeq; NP_741086.1; NM_171075.4. [P49595-1]
DR RefSeq; NP_741087.1; NM_171076.3.
DR AlphaFoldDB; P49595; -.
DR SMR; P49595; -.
DR BioGRID; 40503; 3.
DR IntAct; P49595; 2.
DR STRING; 6239.F42G9.1a; -.
DR iPTMnet; P49595; -.
DR EPD; P49595; -.
DR PaxDb; P49595; -.
DR PeptideAtlas; P49595; -.
DR EnsemblMetazoa; F42G9.1a.1; F42G9.1a.1; WBGene00018362. [P49595-1]
DR EnsemblMetazoa; F42G9.1b.1; F42G9.1b.1; WBGene00018362. [P49595-2]
DR GeneID; 175233; -.
DR KEGG; cel:CELE_F42G9.1; -.
DR UCSC; F42G9.1a; c. elegans.
DR CTD; 175233; -.
DR WormBase; F42G9.1a; CE07231; WBGene00018362; ppm-1.G. [P49595-1]
DR WormBase; F42G9.1b; CE30788; WBGene00018362; ppm-1.G. [P49595-2]
DR eggNOG; KOG0699; Eukaryota.
DR GeneTree; ENSGT00940000165923; -.
DR HOGENOM; CLU_013173_13_1_1; -.
DR InParanoid; P49595; -.
DR OMA; DAHIATP; -.
DR OrthoDB; 957254at2759; -.
DR PhylomeDB; P49595; -.
DR PRO; PR:P49595; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00018362; Expressed in adult organism and 5 other tissues.
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:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 2.
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; 2.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..491
FT /note="Protein phosphatase ppm-1.G"
FT /id="PRO_0000057762"
FT DOMAIN 23..486
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 112..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..293
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..37
FT /note="MGAYLNKPIIEKEKEEGSGNGLSYACTTMQGWRVNQE -> MDFKNVEYFYL
FT KNFQ (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060334"
SQ SEQUENCE 491 AA; 53142 MW; F110D12E343953D6 CRC64;
MGAYLNKPII EKEKEEGSGN GLSYACTTMQ GWRVNQEDAH NCVVDLHTDW HMFGVYDGHG
GTEVSKFTSA KLPDFLKERK FWEADDVAEC LQKAFVDFDD FIRAEESMKE LKDIGDEGKP
KKAGGEADSE DEADRIDTIE EASVPLAELL KRYGGAGVGK SLLSAFLAKG DVSDDSEDED
EDEEEAEEQD DTEEKKENED ASAEVVIENA EDKEEEEGSP KKKGQKRCQK SPIQSEAKKS
KSETDAETAP SSSSGVDGVA TEEEDEDDSD KEFVADEEED DEDAEDEQSD EEMVDGSLAP
LLLGSGGAEV PGEDSGTTAC VCLVGKDKVI VANAGDSRAV LCRNGKAVDL SVDHKPEDEV
ETNRIHAAGG QIEDGRVNGG LNLSRAFGDH AYKKNQELGL KEQMITALPD VKIEALTPED
EFIVVACDGI WNSMESQQVV DFVRDLLAKG SSCAEVCDAL CDACLADSTD GDGTGCDNMT
VICTTFDRKS K
