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Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)

 PP1B_CHICK              Reviewed;         327 AA.
P62207; P37140;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 110.
RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
Short=PP-1B;
EC=3.1.3.16;
EC=3.1.3.53;
Name=PPP1CB;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Gizzard;
PubMed=7982954;
Shimizu H., Ito M., Miyahara M., Ichikawa K., Okubo S., Konishi T.,
Naka M., Tanaka T., Hirano K., Hartshorne D.J., Nakano T.;
"Characterization of the myosin-binding subunit of smooth muscle
myosin phosphatase.";
J. Biol. Chem. 269:30407-30411(1994).
[2]
PROTEIN SEQUENCE OF 2-14 AND 111-121, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Black E.J., Gillespie D.A.;
Submitted (JAN-2007) to UniProtKB.
[3]
PROTEIN SEQUENCE OF 147-149; 168-185; 221-233; 246-259 AND 304-319,
CATALYTIC ACTIVITY, AND SUBUNIT.
TISSUE=Gizzard;
PubMed=1336455; DOI=10.1111/j.1432-1033.1992.tb17508.x;
Alessi D., MacDougall L.K., Sola M.M., Ikebe M., Cohen P.;
"The control of protein phosphatase-1 by targetting subunits. The
major myosin phosphatase in avian smooth muscle is a novel form of
protein phosphatase-1.";
Eur. J. Biochem. 210:1023-1035(1992).
[4]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS
AND PPP1R12A, COFACTOR, TISSUE SPECIFICITY, AND SUBUNIT.
PubMed=15164081; DOI=10.1038/nature02582;
Terrak M., Kerff F., Langsetmo K., Tao T., Dominguez R.;
"Structural basis of protein phosphatase 1 regulation.";
Nature 429:780-784(2004).
-!- FUNCTION: Protein phosphatase that associates with over 200
regulatory proteins to form highly specific holoenzymes which
dephosphorylate hundreds of biological targets. Protein
phosphatase (PP1) is essential for cell division, it participates
in the regulation of glycogen metabolism, muscle contractility and
protein synthesis. Involved in regulation of ionic conductances
and long-term synaptic plasticity.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:1336455}.
-!- CATALYTIC ACTIVITY: [Myosin light-chain] phosphate + H(2)O =
[myosin light-chain] + phosphate. {ECO:0000269|PubMed:1336455}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15164081};
Note=Binds 2 manganese ions per subunit.
{ECO:0000269|PubMed:15164081};
-!- ENZYME REGULATION: Inhibited by the toxins okadaic acid,
tautomycin and microcystin Leu-Arg. The phosphatase activity of
the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited
by Salubrinal, a drug that protects cells from endoplasmic
reticulum stress (By similarity). {ECO:0000250}.
-!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
PPP1CC, which is folded into its native form by inhibitor 2 and
glycogen synthetase kinase 3, and then complexed to one or several
targeting or regulatory subunits. The targeting or regulatory
subunits determine the substrate specificity of PP1. PPP1R12A,
PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A, PPP1R3B,
PPP1R3C and PPP1R3D mediate binding to glycogen (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in gizzard (at protein level).
{ECO:0000269|PubMed:15164081}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
{ECO:0000305}.
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EMBL; D37987; BAA07203.1; -; mRNA.
RefSeq; NP_990453.1; NM_205122.1.
UniGene; Gga.1250; -.
PDB; 1S70; X-ray; 2.70 A; A=1-327.
PDBsum; 1S70; -.
ProteinModelPortal; P62207; -.
SMR; P62207; -.
BioGrid; 676289; 2.
ELM; P62207; -.
STRING; 9031.ENSGALP00000031272; -.
PaxDb; P62207; -.
GeneID; 396019; -.
KEGG; gga:396019; -.
CTD; 5500; -.
eggNOG; ENOG410IN85; Eukaryota.
eggNOG; ENOG410XPVF; LUCA.
HOGENOM; HOG000172697; -.
HOVERGEN; HBG000216; -.
InParanoid; P62207; -.
KO; K06269; -.
OMA; DHQEADI; -.
OrthoDB; EOG091G0EKF; -.
PhylomeDB; P62207; -.
TreeFam; TF354243; -.
BRENDA; 3.1.3.16; 1306.
Reactome; R-GGA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-GGA-5627123; RHO GTPases activate PAKs.
EvolutionaryTrace; P62207; -.
PRO; PR:P62207; -.
Proteomes; UP000000539; Unplaced.
Bgee; ENSGALG00000010026; -.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017018; F:myosin phosphatase activity; IDA:UniProtKB.
GO; GO:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR037979; PPP1CA/PPP1CB.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR031675; STPPase_N.
PANTHER; PTHR11668:SF377; PTHR11668:SF377; 1.
Pfam; PF00149; Metallophos; 1.
Pfam; PF16891; STPPase_N; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Carbohydrate metabolism; Cell cycle;
Cell division; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycogen metabolism; Hydrolase; Manganese;
Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.2}.
CHAIN 2 327 Serine/threonine-protein phosphatase PP1-
beta catalytic subunit.
/FTId=PRO_0000058784.
ACT_SITE 124 124 Proton donor. {ECO:0000250}.
METAL 63 63 Manganese 1.
METAL 65 65 Manganese 1.
METAL 91 91 Manganese 1.
METAL 91 91 Manganese 2.
METAL 123 123 Manganese 2.
METAL 172 172 Manganese 2.
METAL 247 247 Manganese 2.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.2}.
HELIX 8 16 {ECO:0000244|PDB:1S70}.
TURN 17 20 {ECO:0000244|PDB:1S70}.
HELIX 31 45 {ECO:0000244|PDB:1S70}.
STRAND 50 54 {ECO:0000244|PDB:1S70}.
STRAND 56 61 {ECO:0000244|PDB:1S70}.
HELIX 68 78 {ECO:0000244|PDB:1S70}.
STRAND 86 88 {ECO:0000244|PDB:1S70}.
STRAND 93 97 {ECO:0000244|PDB:1S70}.
HELIX 99 112 {ECO:0000244|PDB:1S70}.
TURN 114 116 {ECO:0000244|PDB:1S70}.
STRAND 117 119 {ECO:0000244|PDB:1S70}.
HELIX 127 130 {ECO:0000244|PDB:1S70}.
HELIX 135 142 {ECO:0000244|PDB:1S70}.
HELIX 145 155 {ECO:0000244|PDB:1S70}.
STRAND 161 164 {ECO:0000244|PDB:1S70}.
TURN 165 167 {ECO:0000244|PDB:1S70}.
STRAND 168 170 {ECO:0000244|PDB:1S70}.
HELIX 183 186 {ECO:0000244|PDB:1S70}.
STRAND 196 198 {ECO:0000244|PDB:1S70}.
HELIX 199 205 {ECO:0000244|PDB:1S70}.
STRAND 213 217 {ECO:0000244|PDB:1S70}.
STRAND 221 226 {ECO:0000244|PDB:1S70}.
HELIX 228 238 {ECO:0000244|PDB:1S70}.
STRAND 241 245 {ECO:0000244|PDB:1S70}.
STRAND 252 257 {ECO:0000244|PDB:1S70}.
TURN 258 261 {ECO:0000244|PDB:1S70}.
STRAND 262 266 {ECO:0000244|PDB:1S70}.
HELIX 271 273 {ECO:0000244|PDB:1S70}.
STRAND 282 284 {ECO:0000244|PDB:1S70}.
STRAND 289 292 {ECO:0000244|PDB:1S70}.
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


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