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 27-MAR-2024, entry version 159. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9913-ENSBTAP00000026003; -. DR Ensembl; ENSBTAT00000026003.4; ENSBTAP00000026003.3; ENSBTAG00000019522.4. 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; RYGQNCI; -. DR OrthoDB; 11028at2759; -. DR TreeFam; TF354280; -. DR Proteomes; UP000009136; Chromosome 11. DR Bgee; ENSBTAG00000019522; Expressed in spermatid and 107 other cell types or 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:0051726; P:regulation of cell cycle; IEA:Ensembl. DR CDD; cd00143; PP2Cc; 2. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1. DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1. DR Pfam; PF00481; PP2C; 2. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 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 //