ID PP1GA_XENLA Reviewed; 323 AA. AC P36874; Q5EAX1; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 2. DT 27-MAR-2024, entry version 128. DE RecName: Full=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A; DE Short=PP-1G-A; DE Short=xPP1-gamma1; DE EC=3.1.3.16; GN Name=ppp1cc-a; Synonyms=ppp1cc; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR RP LOCATION. RC TISSUE=Oocyte; RX PubMed=17448463; DOI=10.1016/j.yexcr.2007.03.015; RA Ito H., Koyama Y., Takano M., Ishii K., Maeno M., Furukawa K., Horigome T.; RT "Nuclear envelope precursor vesicle targeting to chromatin is stimulated by RT protein phosphatase 1 in Xenopus egg extracts."; RL Exp. Cell Res. 313:1897-1910(2007). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Walker D.H., Rempel R., Maller J.L.; RT "The C-terminus of Xenopus protein phosphatase 1-gamma1 determines its cell RT cycle-dependent regulation and phosphorylation."; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Egg; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protein phosphatase that associates with over 200 regulatory CC proteins to form highly specific holoenzymes which dephosphorylate CC hundreds of biological targets. Protein phosphatase 1 (PP1) is CC essential for cell division, and participates in the regulation of CC glycogen metabolism, muscle contractility and protein synthesis (By CC similarity). Promotes nuclear envelope reassembly by targeting nuclear CC membrane vesicles to chromatin at the end of mitosis. Acts by CC dephosphorylating membrane proteins such as lamin B receptor (lbr) to CC regulate the binding of membrane proteins to chromatin. {ECO:0000250, CC ECO:0000269|PubMed:17448463}. 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 Evidence={ECO:0000269|PubMed:17448463}; 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 Evidence={ECO:0000269|PubMed:17448463}; 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}. CC -!- INTERACTION: CC P36874; Q9IB67: casp2.L; NbExp=2; IntAct=EBI-2908704, EBI-7207360; CC P36874; O42263: cenpe.S; NbExp=2; IntAct=EBI-2908704, EBI-2607221; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17448463}. Nucleus CC {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cleavage furrow CC {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, CC centromere, kinetochore {ECO:0000250}. Nucleus speckle {ECO:0000250}. CC Midbody {ECO:0000250}. Mitochondrion {ECO:0000250}. Membrane CC {ECO:0000269|PubMed:17448463}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC {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; AB106881; BAF51554.1; -; mRNA. DR EMBL; L17039; AAA49934.1; -; mRNA. DR EMBL; BC090213; AAH90213.1; -; mRNA. DR RefSeq; NP_001081308.1; NM_001087839.1. DR AlphaFoldDB; P36874; -. DR SMR; P36874; -. DR IntAct; P36874; 2. DR MINT; P36874; -. DR DNASU; 397767; -. DR GeneID; 397767; -. DR KEGG; xla:397767; -. DR AGR; Xenbase:XB-GENE-967940; -. DR CTD; 397767; -. DR Xenbase; XB-GENE-967940; ppp1cc.L. DR OMA; EEHEIRY; -. DR OrthoDB; 19833at2759; -. DR Proteomes; UP000186698; Chromosome 1L. DR Bgee; 397767; Expressed in egg cell and 19 other cell types or tissues. DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. 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; IDA: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; IMP:UniProtKB. DR GO; GO:0006470; P:protein dephosphorylation; IDA: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 1: Evidence at protein level; KW Carbohydrate metabolism; Cell cycle; Cell division; Centromere; Chromosome; KW Cytoplasm; Glycogen metabolism; Hydrolase; Kinetochore; Manganese; KW Membrane; 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 A" FT /id="PRO_0000058790" 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" 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" FT CONFLICT 213 FT /note="V -> I (in Ref. 2; AAA49934)" FT /evidence="ECO:0000305" FT CONFLICT 220 FT /note="D -> Y (in Ref. 2; AAA49934)" FT /evidence="ECO:0000305" 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 //