ID PP1B_CHICK Reviewed; 327 AA. AC P62207; P37140; DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 137. DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit; DE Short=PP-1B; DE EC=3.1.3.16; DE EC=3.1.3.53; GN Name=PPP1CB; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Gizzard; RX PubMed=7982954; DOI=10.1016/s0021-9258(18)43828-8; RA Shimizu H., Ito M., Miyahara M., Ichikawa K., Okubo S., Konishi T., RA Naka M., Tanaka T., Hirano K., Hartshorne D.J., Nakano T.; RT "Characterization of the myosin-binding subunit of smooth muscle myosin RT phosphatase."; RL J. Biol. Chem. 269:30407-30411(1994). RN [2] RP PROTEIN SEQUENCE OF 2-14 AND 111-121, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V., Black E.J., Gillespie D.A.; RL Submitted (JAN-2007) to UniProtKB. RN [3] RP PROTEIN SEQUENCE OF 147-149; 168-185; 221-233; 246-259 AND 304-319, RP CATALYTIC ACTIVITY, AND SUBUNIT. RC TISSUE=Gizzard; RX PubMed=1336455; DOI=10.1111/j.1432-1033.1992.tb17508.x; RA Alessi D., MacDougall L.K., Sola M.M., Ikebe M., Cohen P.; RT "The control of protein phosphatase-1 by targetting subunits. The major RT myosin phosphatase in avian smooth muscle is a novel form of protein RT phosphatase-1."; RL Eur. J. Biochem. 210:1023-1035(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND RP PPP1R12A, COFACTOR, TISSUE SPECIFICITY, AND SUBUNIT. RX PubMed=15164081; DOI=10.1038/nature02582; RA Terrak M., Kerff F., Langsetmo K., Tao T., Dominguez R.; RT "Structural basis of protein phosphatase 1 regulation."; RL Nature 429:780-784(2004). 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. 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:1336455}; 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:1336455}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[myosin light chain] = L-seryl-[myosin CC light chain] + phosphate; Xref=Rhea:RHEA:12849, Rhea:RHEA-COMP:13684, CC Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.53; CC Evidence={ECO:0000269|PubMed:1336455}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[myosin light chain] = L-threonyl- CC [myosin light chain] + phosphate; Xref=Rhea:RHEA:53988, Rhea:RHEA- CC COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.53; CC Evidence={ECO:0000269|PubMed:1336455}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:15164081}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:15164081}; CC -!- ACTIVITY REGULATION: Inhibited by the toxins okadaic acid, tautomycin CC and microcystin Leu-Arg. The phosphatase activity of the PPP1R15A-PP1 CC complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug CC that protects cells from endoplasmic reticulum stress (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, CC which is folded into its native form by inhibitor 2 and glycogen CC synthetase kinase 3, and then complexed to one or several targeting or CC regulatory subunits. The targeting or regulatory subunits determine the CC substrate specificity of PP1. PPP1R12A, PPP1R12B and PPP1R12C mediate CC binding to myosin. PPP1R3A, PPP1R3B, PPP1R3C and PPP1R3D mediate CC binding to glycogen (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Detected in gizzard (at protein level). CC {ECO:0000269|PubMed:15164081}. 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; D37987; BAA07203.1; -; mRNA. DR RefSeq; NP_990453.1; NM_205122.1. DR PDB; 1S70; X-ray; 2.70 A; A=1-327. DR PDBsum; 1S70; -. DR AlphaFoldDB; P62207; -. DR SMR; P62207; -. DR BioGRID; 676289; 2. DR ELM; P62207; -. DR STRING; 9031.ENSGALP00000031272; -. DR PaxDb; 9031-ENSGALP00000031272; -. DR Ensembl; ENSGALT00000144038; ENSGALP00000079649; ENSGALG00000010026. DR Ensembl; ENSGALT00010048228.1; ENSGALP00010028439.1; ENSGALG00010019972.1. DR Ensembl; ENSGALT00015038176; ENSGALP00015022393; ENSGALG00015015663. DR GeneID; 396019; -. DR KEGG; gga:396019; -. DR CTD; 5500; -. DR VEuPathDB; HostDB:geneid_396019; -. DR eggNOG; KOG0374; Eukaryota. DR GeneTree; ENSGT00940000154644; -. DR HOGENOM; CLU_004962_0_0_1; -. DR InParanoid; P62207; -. DR OMA; FGEFDNA; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; P62207; -. DR TreeFam; TF354243; -. DR BRENDA; 3.1.3.16; 1306. DR Reactome; R-GGA-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-GGA-5627123; RHO GTPases activate PAKs. DR Reactome; R-GGA-5673000; RAF activation. DR EvolutionaryTrace; P62207; -. DR PRO; PR:P62207; -. DR Proteomes; UP000000539; Chromosome 3. DR Bgee; ENSGALG00000010026; Expressed in ovary and 12 other cell types or tissues. DR ExpressionAtlas; P62207; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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; IDA:UniProtKB. DR GO; GO:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central. DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Carbohydrate metabolism; Cell cycle; KW Cell division; Cytoplasm; Direct protein sequencing; Glycogen metabolism; KW Hydrolase; Manganese; Metal-binding; Nucleus; Phosphoprotein; KW Protein phosphatase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.2" FT CHAIN 2..327 FT /note="Serine/threonine-protein phosphatase PP1-beta FT catalytic subunit" FT /id="PRO_0000058784" 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 BINDING 65 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT BINDING 91 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT BINDING 91 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT BINDING 123 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT BINDING 172 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT BINDING 247 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.2" FT HELIX 8..16 FT /evidence="ECO:0007829|PDB:1S70" FT TURN 17..20 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 31..45 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 68..78 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 99..112 FT /evidence="ECO:0007829|PDB:1S70" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 135..142 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 145..155 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:1S70" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 183..186 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 199..205 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 228..238 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 241..245 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 252..257 FT /evidence="ECO:0007829|PDB:1S70" FT TURN 258..261 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 262..266 FT /evidence="ECO:0007829|PDB:1S70" FT HELIX 271..273 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:1S70" FT STRAND 289..292 FT /evidence="ECO:0007829|PDB:1S70" SQ SEQUENCE 327 AA; 37187 MW; E8356022E9B94ECD CRC64; MADGELNVDS LITRLLEVRG 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 //