P62207 (PP1B_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Short name=PP-1B
EC=3.1.3.16
EC=3.1.3.53

Gene names

Name:

PPP1CB

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 phosphoprotein + H2O = a protein + phosphate. Ref.3 [Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate. Ref.3
Cofactor	Binds 1 iron ion per subunit By similarity. Ref.4 Binds 1 manganese ion per subunit. Ref.4
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.
Subunit structure	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. Ref.3 Ref.4
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Tissue specificity	Detected in gizzard (at protein level). Ref.4
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism
Cellular component	Cytoplasm Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein dephosphorylation Inferred from electronic annotation. Source: Compara regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	MLL5-L complex Inferred from electronic annotation. Source: Compara PTW/PP1 phosphatase complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin phosphatase activity Inferred from direct assay Ref.3. Source: UniProtKB myosin-light-chain-phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 327

326

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

PRO_0000058784

Sites

Active site

124

1

Proton donor By similarity

Metal binding

63

1

Iron or manganese

Metal binding

65

1

Iron or manganese

Metal binding

91

1

Iron or manganese

Metal binding

91

1

Manganese By similarity

Metal binding

123

1

Manganese By similarity

Metal binding

172

1

Manganese By similarity

Metal binding

247

1

Manganese By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.2

Secondary structure

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327

Helix Strand Turn

Details...

Helix

8 – 16

9

Turn

17 – 20

4

Helix

31 – 45

15

Beta strand

50 – 54

5

Beta strand

56 – 61

6

Helix

68 – 78

11

Beta strand

86 – 88

3

Beta strand

93 – 97

5

Helix

99 – 112

14

Turn

114 – 116

3

Beta strand

117 – 119

3

Helix

127 – 130

4

Helix

135 – 142

8

Helix

145 – 155

11

Beta strand

161 – 164

4

Turn

165 – 167

3

Beta strand

168 – 170

3

Helix

183 – 186

4

Beta strand

196 – 198

3

Helix

199 – 205

7

Beta strand

213 – 217

5

Beta strand

221 – 226

6

Helix

228 – 238

11

Beta strand

241 – 245

5

Beta strand

252 – 257

6

Turn

258 – 261

4

Beta strand

262 – 266

5

Helix

271 – 273

3

Beta strand

282 – 284

3

Beta strand

289 – 292

4

Sequences

	Sequence		Length	Mass (Da)
	P62207 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E8356022E9B94ECD	FASTA	327	37,187
	10 20 30 40 50 60 MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI 70 80 90 100 110 120 CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL 130 140 150 160 170 180 RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ 190 200 210 220 230 240 SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL 250 260 270 280 290 300 DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 310 320 KAKYQYGGLN SGRPVTPPRT ANPPKKR

References

[1]	"Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase." Shimizu H., Ito M., Miyahara M., Ichikawa K., Okubo S., Konishi T., Naka M., Tanaka T., Hirano K., Hartshorne D.J., Nakano T. J. Biol. Chem. 269:30407-30411(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Gizzard.
[2]	Bienvenut W.V., Black E.J., Gillespie D.A. Submitted (JAN-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14 AND 111-121, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[3]	"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." Alessi D., MacDougall L.K., Sola M.M., Ikebe M., Cohen P. Eur. J. Biochem. 210:1023-1035(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 147-149; 168-185; 221-233; 246-259 AND 304-319, CATALYTIC ACTIVITY, SUBUNIT. Tissue: Gizzard.
[4]	"Structural basis of protein phosphatase 1 regulation." Terrak M., Kerff F., Langsetmo K., Tao T., Dominguez R. Nature 429:780-784(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND PPP1R12A, COFACTOR, TISSUE SPECIFICITY, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D37987 mRNA. Translation: BAA07203.1.

IPI

IPI00594959.

RefSeq

NP_990453.1. NM_205122.1.

UniGene

Gga.1250.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1S70	X-ray	2.70	A	1-327	[»]

ProteinModelPortal

P62207.

ModBase

Search...

Proteomic databases

PaxDb

P62207.

PRIDE

P62207.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSGALT00000031908; ENSGALP00000031272; ENSGALG00000010026.

GeneID

396019.

KEGG

gga:396019.

Organism-specific databases

CTD

5500.

Phylogenomic databases

eggNOG

COG0639.

GeneTree

ENSGT00530000062911.

HOGENOM

HOG000172697.

HOVERGEN

HBG000216.

InParanoid

P62207.

KO

K06269.

OMA

PDLQGME.

OrthoDB

EOG4MKNGK.

Enzyme and pathway databases

BRENDA

3.1.3.16. 1306.

Family and domain databases

InterPro

IPR004843. Metallo_PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]

Pfam

PF00149. Metallophos. 1 hit.
[Graphical view]

PRINTS

PR00114. STPHPHTASE.

SMART

SM00156. PP2Ac. 1 hit.
[Graphical view]

PROSITE

PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P62207.

EvolutionaryTrace

P62207.

NextBio

20816081.

Entry information

Entry name

PP1B_CHICK

Accession

Primary (citable) accession number: P62207
Secondary accession number(s): P37140

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program