P62138 (PP1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Short name=PP-1A
EC=3.1.3.16

Gene names

Name:	Ppp1ca
Synonyms:	Ppp1a

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	330 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 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development By similarity.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit 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. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts with RPSA only in the presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS. Interacts with PPP1R39. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site By similarity. Interacts with PPP1R9A, PPP1R9B and YLPM1. Interacts with NEK2. Interacts with PHACTR4; which acts as an activator of PP1 activity. Interacts with FER; this promotes phosphorylation at Thr-320 By similarity. Ref.5 Ref.7
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Nucleus › nucleoplasm By similarity. Nucleus › nucleolus By similarity. Note: Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting it to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles By similarity.
Tissue specificity	Widely expressed. Ref.3
Post-translational modification	Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation By similarity.
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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	branching morphogenesis of an epithelial tube Inferred from electronic annotation. Source: Compara 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 lung development Inferred from electronic annotation. Source: Compara protein dephosphorylation Inferred from direct assay PubMed 7720853. Source: RGD regulation of glycogen biosynthetic process Inferred from direct assay PubMed 7720853. Source: RGD regulation of glycogen catabolic process Inferred from direct assay PubMed 7720853. Source: RGD
Cellular_component	MLL5-L complex Inferred from electronic annotation. Source: Compara PTW/PP1 phosphatase complex Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome dendritic spine Inferred from direct assay PubMed 7724573. Source: RGD glycogen granule Inferred from direct assay PubMed 7720853. Source: RGD nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 7724573. Source: RGD perikaryon Inferred from direct assay PubMed 7724573. Source: RGD protein phosphatase type 1 complex Inferred from direct assay PubMed 7720853. Source: RGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from direct assay PubMed 7720853. Source: RGD protein serine/threonine phosphatase activity Inferred from electronic annotation. Source: Compara ribonucleoprotein complex binding Inferred from physical interaction PubMed 12065664. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 330	329	Serine/threonine-protein phosphatase PP1-alpha catalytic subunit		PRO_0000058777
Sites
	Active site	125	1	Proton donor By similarity
	Metal binding	64	1	Iron By similarity
	Metal binding	66	1	Iron By similarity
	Metal binding	92	1	Iron By similarity
	Metal binding	92	1	Manganese By similarity
	Metal binding	124	1	Manganese By similarity
	Metal binding	173	1	Manganese By similarity
	Metal binding	248	1	Manganese By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	306	1	Phosphotyrosine By similarity
	Modified residue	320	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62138 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: 60C37E1AD9831DAC	FASTA	330	37,512
	10 20 30 40 50 60 MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK 70 80 90 100 110 120 ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL 130 140 150 160 170 180 LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL 190 200 210 220 230 240 QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD 250 260 270 280 290 300 LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD 310 320 330 KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of cDNA for the catalytic subunit 1 alpha of rat kidney type 1 protein phosphatase, and detection of the gene expression at high levels in hepatoma cells and regenerating livers as compared to rat livers." Kitamura K., Mizuno Y., Sasaki A., Yasui A., Tsuiki S., Kikuchi K. J. Biochem. 109:307-310(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Identification of members of the protein phosphatase 1 gene family in the rat and enhanced expression of protein phosphatase 1 alpha gene in rat hepatocellular carcinomas." Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M. Jpn. J. Cancer Res. 81:1272-1280(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Differential expression of protein phosphatase 1 isoforms in mammalian brain." da Cruz e Silva E.F., Fox C.A., Ouimet C.C., Gustafson E., Watson S.J., Greengard P. J. Neurosci. 15:3375-3389(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Brain.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[5]	"Regulation of neurabin I interaction with protein phosphatase 1 by phosphorylation." McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y., Greengard P., Nairn A.C., Hemmings H.C. Jr. Biochemistry 38:12943-12949(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 7-26 AND 212-234, INTERACTION WITH PPP1R9A AND PPP1R9B. Strain: Sprague-Dawley.
[6]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 44-60 AND 112-122, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
[7]	"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G." Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G. Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YLPM1.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00859 mRNA. Translation: BAA00732.1. D90163 mRNA. Translation: BAA14194.1. BC070517 mRNA. Translation: AAH70517.1.
IPI	IPI00208265.
PIR	JX0157.
RefSeq	NP_113715.1. NM_031527.1.
UniGene	Rn.2024.
3D structure databases
ProteinModelPortal	P62138.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62138. 1 interaction.
PTM databases
PhosphoSite	P62138.
Proteomic databases
PaxDb	P62138.
PRIDE	P62138.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000025282; ENSRNOP00000025282; ENSRNOG00000018708.
GeneID	24668.
KEGG	rno:24668.
UCSC	RGD:3375. rat.
Organism-specific databases
CTD	5499.
RGD	3375. Ppp1ca.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000062911.
HOGENOM	HOG000172697.
HOVERGEN	HBG000216.
InParanoid	P62138.
KO	K06269.
OMA	APNYCNE.
OrthoDB	EOG49GKGT.
Enzyme and pathway databases
Reactome	REACT_113568. Metabolism.
Gene expression databases
ArrayExpress	P62138.
Genevestigator	P62138.
GermOnline	ENSRNOG00000018708. Rattus norvegicus.
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	P62138.
NextBio	604034.

Entry information

Entry name

PP1A_RAT

Accession

Primary (citable) accession number: P62138
Secondary accession number(s): P08129, P20653, P22802

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	June 21, 2004
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program