ID PP1B_XENTR Reviewed; 327 AA. AC Q5I085; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit; DE Short=PP-1B; DE EC=3.1.3.16; GN Name=ppp1cb; ORFNames=TEgg049h05.1; 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Egg; RG Sanger Xenopus tropicalis EST/cDNA project; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Neurula; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (DEC-2004) 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 (PP1) is essential CC for cell division, it participates in the regulation of glycogen CC metabolism, muscle contractility and protein synthesis. Involved in CC regulation of ionic conductances and long-term synaptic plasticity (By CC 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. 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; CR760533; CAJ81891.1; -; mRNA. DR EMBL; BC088594; AAH88594.1; -; mRNA. DR RefSeq; NP_001011467.1; NM_001011467.1. DR AlphaFoldDB; Q5I085; -. DR SMR; Q5I085; -. DR STRING; 8364.ENSXETP00000010716; -. DR PaxDb; 8364-ENSXETP00000021336; -. DR Ensembl; ENSXETT00000098265; ENSXETP00000077905; ENSXETG00000010214. DR GeneID; 496958; -. DR KEGG; xtr:496958; -. DR AGR; Xenbase:XB-GENE-961670; -. DR CTD; 5500; -. DR Xenbase; XB-GENE-961670; ppp1cb. DR InParanoid; Q5I085; -. DR OMA; FGEFDNA; -. DR OrthoDB; 19833at2759; -. DR Reactome; R-XTR-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-XTR-5625740; RHO GTPases activate PKNs. DR Proteomes; UP000008143; Chromosome 5. DR Bgee; ENSXETG00000010214; Expressed in skeletal muscle tissue and 17 other cell types or tissues. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB. 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:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. DR GO; GO:0030155; P:regulation of cell adhesion; 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:SF472; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-BETA 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 Acetylation; Carbohydrate metabolism; Cell cycle; Cell division; Cytoplasm; KW Glycogen metabolism; Hydrolase; Manganese; Metal-binding; Nucleus; KW Protein phosphatase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..327 FT /note="Serine/threonine-protein phosphatase PP1-beta FT catalytic subunit" FT /id="PRO_0000293480" FT REGION 305..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 124 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 63 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 123 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 172 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 247 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250" SQ SEQUENCE 327 AA; 37173 MW; F337A83332B89705 CRC64; MADGELNVDS LISRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK KAKYQYGGLN SGRPVTPPRT ANPPKKR //