PP1B_RABIT
ID PP1B_RABIT Reviewed; 327 AA.
AC P62143; P37140;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white;
RX PubMed=2176604; DOI=10.1111/j.1432-1033.1990.tb19464.x;
RA Dombradi V., Axton J.M., Brewis N.D., da Cruz e Silva E.F., Alphey L.,
RA Cohen P.T.W.;
RT "Drosophila contains three genes that encode distinct isoforms of protein
RT phosphatase 1.";
RL Eur. J. Biochem. 194:739-745(1990).
RN [2]
RP PROTEIN SEQUENCE OF 26-35; 60-73; 147-149; 168-186; 222-232; 246-259 AND
RP 304-319, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX PubMed=1336456; DOI=10.1111/j.1432-1033.1992.tb17509.x;
RA Dent P., MacDougall L.K., MacKintosh C., Campbell D.G., Cohen P.;
RT "A myofibrillar protein phosphatase from rabbit skeletal muscle contains
RT the beta isoform of protein phosphatase-1 complexed to a regulatory subunit
RT which greatly enhances the dephosphorylation of myosin.";
RL Eur. J. Biochem. 210:1037-1044(1992).
RN [3]
RP PROTEIN SEQUENCE OF 43-48; 113-121; 132-140; 150-165; 168-186; 188-204;
RP 246-255 AND 267-286, AND INTERACTION WITH PPP1R12B.
RC TISSUE=Skeletal muscle;
RX PubMed=9827534; DOI=10.1016/s0014-5793(98)01276-9;
RA Moorhead G., Johnson D., Morrice N., Cohen P.;
RT "The major myosin phosphatase in skeletal muscle is a complex between the
RT beta-isoform of protein phosphatase 1 and the MYPT2 gene product.";
RL FEBS Lett. 438:141-144(1998).
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 Evidence={ECO:0000269|PubMed:1336456};
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:1336456};
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:1336456};
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:1336456};
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: 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 Inhibited by the toxins okadaic acid, tautomycin and microcystin Leu-
CC Arg. {ECO:0000250, ECO:0000269|PubMed:1336456}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for phosphorylase {ECO:0000269|PubMed:1336456};
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, and PPP1R12C mediate binding to
CC myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C,
CC PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. PPP1R15A
CC and PPP1R15B mediate binding to EIF2S1. Part of a complex containing
CC PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R7 and PPP1R12C. Interacts
CC with PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed
CC of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
CC Interacts with PPP1R8. Interacts with PPP1R12A and NUAK1; the
CC interaction is direct. Interacts with TRIM28; the interaction
CC dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21
CC promoter site (By similarity). Interacts with PPP1R12B
CC (PubMed:9827534). Interacts with FOXP3 (By similarity). Interacts with
CC RRP1B (By similarity). Interacts with SERPINE1. Interacts with LZTR1
CC (By similarity). {ECO:0000250|UniProtKB:P62140,
CC ECO:0000250|UniProtKB:P62141, ECO:0000269|PubMed:1336456,
CC ECO:0000269|PubMed:9827534}.
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; X61639; CAA43820.1; -; mRNA.
DR PIR; S13829; S13829.
DR RefSeq; NP_001095192.1; NM_001101722.1.
DR AlphaFoldDB; P62143; -.
DR SMR; P62143; -.
DR BioGRID; 1172606; 1.
DR STRING; 9986.ENSOCUP00000000885; -.
DR PRIDE; P62143; -.
DR GeneID; 100009587; -.
DR KEGG; ocu:100009587; -.
DR CTD; 5500; -.
DR eggNOG; KOG0374; Eukaryota.
DR InParanoid; P62143; -.
DR OrthoDB; 766640at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
DR GO; GO:0030145; F:manganese ion binding; IDA:CAFA.
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:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:CAFA.
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; IDA:CAFA.
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 1: Evidence at protein level;
KW Acetylation; Biological rhythms; 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:0000250|UniProtKB:P62140"
FT CHAIN 2..327
FT /note="Serine/threonine-protein phosphatase PP1-beta
FT catalytic subunit"
FT /id="PRO_0000058782"
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
