ID PPIG_XENTR Reviewed; 323 AA. AC Q6NVU2; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit {ECO:0000250|UniProtKB:P36873}; DE Short=PP-1G {ECO:0000250|UniProtKB:P36873}; DE EC=3.1.3.16; GN Name=ppp1cc {ECO:0000312|EMBL:AAH67911.1}; ORFNames=TEgg061c20.1; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] {ECO:0000312|EMBL:CAJ81429.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Egg {ECO:0000312|EMBL:CAJ81429.1}; RG Sanger Xenopus tropicalis EST/cDNA project; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000312|EMBL:CAJ81429.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo {ECO:0000312|EMBL:AAH67911.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protein phosphatase 1 (PP1) is essential for cell division, CC and participates in the regulation of glycogen metabolism, muscle CC contractility and protein synthesis. Promotes nuclear envelope CC reassembly by targeting nuclear membrane vesicles to chromatin at the CC end of mitosis. Acts by dephosphorylating membrane proteins such as CC lamin B receptor (lbr) to regulate the binding of membrane proteins to CC chromatin (By similarity). {ECO:0000250}. 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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: PP1 comprises a catalytic subunit, ppp1c1, ppp1cb or ppp1cc, CC which is folded into its native form by inhibitor 2 and glycogen CC synthetase kinase 3, and then is complexed to one or several targeting CC or regulatory subunits. {ECO:0000250|UniProtKB:P63088}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36874}. Nucleus CC {ECO:0000250}. Cleavage furrow {ECO:0000250}. Nucleus, nucleolus CC {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, CC centromere, kinetochore {ECO:0000250}. Nucleus speckle {ECO:0000250}. CC Midbody {ECO:0000250}. Mitochondrion {ECO:0000250}. Cytoplasm, CC cytoskeleton, microtubule organizing center CC {ECO:0000250|UniProtKB:P36873}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC {ECO:0000255}. 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; CR761289; CAJ81429.1; -; mRNA. DR EMBL; BC067911; AAH67911.1; -; mRNA. DR RefSeq; NP_998835.1; NM_213670.2. DR AlphaFoldDB; Q6NVU2; -. DR SMR; Q6NVU2; -. DR STRING; 8364.ENSXETP00000037289; -. DR PaxDb; 8364-ENSXETP00000052896; -. DR DNASU; 407879; -. DR Ensembl; ENSXETT00000052896; ENSXETP00000052896; ENSXETG00000024480. DR GeneID; 407879; -. DR KEGG; xtr:407879; -. DR AGR; Xenbase:XB-GENE-967934; -. DR CTD; 5501; -. DR Xenbase; XB-GENE-967934; ppp1cc. DR eggNOG; KOG0374; Eukaryota. DR HOGENOM; CLU_004962_0_0_1; -. DR InParanoid; Q6NVU2; -. DR OMA; EEHEIRY; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; Q6NVU2; -. DR TreeFam; TF354243; -. DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. DR Reactome; R-XTR-2467813; Separation of Sister Chromatids. DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins. DR Reactome; R-XTR-68877; Mitotic Prometaphase. DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation. DR Proteomes; UP000008143; Chromosome 1. DR Bgee; ENSXETG00000024480; Expressed in egg cell and 16 other cell types or tissues. DR ExpressionAtlas; Q6NVU2; differential. DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW. DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell. DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. 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; ISS:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB. DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB. DR CDD; cd07414; MPP_PP1_PPKL; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR InterPro; IPR031675; STPPase_N. DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF204; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF16891; STPPase_N; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Cell cycle; Cell division; Centromere; Chromosome; KW Cytoplasm; Cytoskeleton; Glycogen metabolism; Hydrolase; Kinetochore; KW Manganese; Metal-binding; Mitochondrion; Mitosis; Nucleus; KW Protein phosphatase; Reference proteome. FT CHAIN 1..323 FT /note="Serine/threonine-protein phosphatase PP1-gamma FT catalytic subunit" FT /id="PRO_0000365636" FT REGION 300..323 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 125 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 64 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 66 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="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 124 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 173 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 248 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 323 AA; 36956 MW; 8CD4C5DE036A8C2B CRC64; MADVDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE KKKPNASRPV TPPRGMITKQ AKK //