PPM1G_BOVIN
ID PPM1G_BOVIN Reviewed; 543 AA.
AC P79126; Q3ZBB4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein phosphatase 1G;
DE EC=3.1.3.16;
DE AltName: Full=Magnesium-dependent calcium inhibitable phosphatase;
DE Short=MCPP;
DE AltName: Full=Protein phosphatase 1B;
DE AltName: Full=Protein phosphatase 2C isoform gamma;
DE Short=PP2C-gamma;
DE AltName: Full=Protein phosphatase magnesium-dependent 1 gamma;
GN Name=PPM1G; Synonyms=PPM1C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.Y., Qin K.;
RT "Characteristics of a Mg-dependent, calcium-inhibitable serine/threonine
RT protein phosphatase revealed by its cDNA.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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: Interacts with NOL3; may dephosphorylate NOL3.
CC {ECO:0000250|UniProtKB:F1LNI5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane
CC {ECO:0000250|UniProtKB:O15355}; Lipid-anchor
CC {ECO:0000250|UniProtKB:O15355}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; U81159; AAB39357.1; -; mRNA.
DR EMBL; BC103458; AAI03459.1; -; mRNA.
DR RefSeq; NP_777226.2; NM_174801.4.
DR AlphaFoldDB; P79126; -.
DR SMR; P79126; -.
DR STRING; 9913.ENSBTAP00000026003; -.
DR PaxDb; P79126; -.
DR PRIDE; P79126; -.
DR Ensembl; ENSBTAT00000026003; ENSBTAP00000026003; ENSBTAG00000019522.
DR GeneID; 286880; -.
DR KEGG; bta:286880; -.
DR CTD; 5496; -.
DR VEuPathDB; HostDB:ENSBTAG00000019522; -.
DR VGNC; VGNC:33213; PPM1G.
DR eggNOG; KOG0699; Eukaryota.
DR GeneTree; ENSGT00940000158427; -.
DR HOGENOM; CLU_013173_13_1_1; -.
DR InParanoid; P79126; -.
DR OMA; TPEDEFM; -.
DR OrthoDB; 957254at2759; -.
DR TreeFam; TF354280; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000019522; Expressed in spermatid and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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:0035970; P:peptidyl-threonine dephosphorylation; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR CDD; cd00143; PP2Cc; 2.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Lipoprotein; Magnesium; Manganese;
KW Membrane; Metal-binding; Methylation; Myristate; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT CHAIN 2..543
FT /note="Protein phosphatase 1G"
FT /id="PRO_0000057749"
FT DOMAIN 26..503
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 116..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT MOD_RES 381
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT CONFLICT 47
FT /note="P -> Q (in Ref. 1; AAB39357)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="E -> V (in Ref. 1; AAB39357)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="A -> D (in Ref. 1; AAB39357)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="E -> Y (in Ref. 1; AAB39357)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="E -> Q (in Ref. 1; AAB39357)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="N -> H (in Ref. 1; AAB39357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 58607 MW; DFBDFEDBA2B673A3 CRC64;
MGAYLSQPNT VKCSGDGVGA SRLPLPYGFS AMQGWRVSME DAHNCIPELD SETAMFSVYD
GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALEDAFLA IDAKLTTEEV IKELAQIAGR
PTEDEDEKEK VADEDDVDNE EAALLHEEAT MTIEELLTRY GQNCHKGAPH SKSGAGTGEE
PGSQGLNGEA GPEDPSRETS AEENGPTAKA HTGLSSNSEC GTEAGQGGEP GTPTGEAGPS
CSSASDKLPR VAKSKFFEDS EDESDEAEEE EEDSEECSEE EDGYSSEEAE NEEDEDDTEE
AEEDDEEEEM MVPGMEGKEE PGSDSGTTAV VALIRGKQLI VANAGDSRCV VSEAGKALDM
SYDHKPEDEV ELARIKNAGG KVTMDGRVNG GLNLSRAIGD HFYKRNKNLP PEEQMISALP
DIKVLTLTDD HEFMVIACDG IWNVMSSQEV IDFIQSKISQ RDENGELRLL SSIVEELLDQ
CLAPDTSGDG TGCDNMTCII ICFKPRNTAA PQPESGKRKL EEVLSTEGAE ENGNSDKKKA
KRD
