PP1B_CHICK
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 03-AUG-2022, entry version 131.
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}.
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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; P62207; -.
DR Ensembl; ENSGALT00000031908; ENSGALP00000031272; ENSGALG00000010026.
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; TVQMSEN; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P62207; -.
DR TreeFam; TF354243; -.
DR BRENDA; 3.1.3.16; 1306.
DR EvolutionaryTrace; P62207; -.
DR PRO; PR:P62207; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000010026; Expressed in ovary and 12 other 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 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 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
