PP1B_BOVIN
ID PP1B_BOVIN Reviewed; 327 AA.
AC Q3SWW9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-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 (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 Component of the PTW/PP1 phosphatase complex, which plays a role in the
CC control of chromatin structure and cell cycle progression during the
CC transition from mitosis into interphase. In balance with CSNK1D and
CC CSNK1E, determines the circadian period length, through the regulation
CC of the speed and rhythmicity of PER1 and PER2 phosphorylation. May
CC dephosphorylate CSNK1D and CSNK1E (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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
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 (in skeletal muscle), PPP1R3B (in liver),
CC PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen.
CC PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex
CC containing PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R7 and
CC PPP1R12C. Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase
CC complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB
CC or PPP1CC. Interacts with PPP1R8. Interacts with PPP1R12A and NUAK1;
CC the interaction is direct. Interacts with TRIM28; the interaction is
CC weak. Interacts with FOXP3. Interacts with RRP1B. Interacts with
CC SERPINE1. Interacts with LZTR1 (By similarity).
CC {ECO:0000250|UniProtKB:P62140, ECO:0000250|UniProtKB:P62141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus
CC {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P62140}. Note=Highly mobile in cells and can be
CC relocalized through interaction with targeting subunits. In the
CC presence of PPP1R8 relocalizes from the nucleus to nuclear speckles.
CC {ECO:0000250|UniProtKB:P62140}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget - Issue
CC 32 of March 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/032";
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DR EMBL; BC104628; AAI04629.1; -; mRNA.
DR RefSeq; NP_001029825.1; NM_001034653.1.
DR AlphaFoldDB; Q3SWW9; -.
DR SMR; Q3SWW9; -.
DR STRING; 9913.ENSBTAP00000016514; -.
DR PaxDb; Q3SWW9; -.
DR PeptideAtlas; Q3SWW9; -.
DR PRIDE; Q3SWW9; -.
DR Ensembl; ENSBTAT00000016514; ENSBTAP00000016514; ENSBTAG00000012447.
DR GeneID; 538829; -.
DR KEGG; bta:538829; -.
DR CTD; 5500; -.
DR VEuPathDB; HostDB:ENSBTAG00000012447; -.
DR VGNC; VGNC:33220; PPP1CB.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000154644; -.
DR InParanoid; Q3SWW9; -.
DR OMA; TVQMSEN; -.
DR OrthoDB; 766640at2759; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000012447; Expressed in semitendinosus and 102 other tissues.
DR ExpressionAtlas; Q3SWW9; baseline and differential.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
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 Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Biological rhythms; Carbohydrate metabolism; Cell cycle;
KW Cell division; Cytoplasm; Glycogen metabolism; Hydrolase; Manganese;
KW Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62140"
FT CHAIN 2..327
FT /note="Serine/threonine-protein phosphatase PP1-beta
FT catalytic subunit"
FT /id="PRO_0000283052"
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|UniProtKB:P62140"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62140"
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
