Reviewed, UniProtKB/Swiss-Prot P62138 (PP1A_RAT)

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)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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 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.
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, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen. PPP1R15A and PPP1R15B 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 By similarity. Interacts with PPP1R9A, PPP1R9B and PPP1R7. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5 Interacts with NOM1 and PPP1R8 By similarity.
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
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	Direct protein sequencing
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 amino acid dephosphorylation Inferred from direct assay. Source: RGD regulation of glycogen biosynthetic process Inferred from direct assay. Source: RGD regulation of glycogen catabolic process Inferred from direct assay. Source: RGD
Cellular component	cytosol Inferred from Experiment. Source: Reactome dendritic spine Inferred from direct assay. Source: RGD glycogen granule Inferred from direct assay. Source: RGD perikaryon Inferred from direct assay. Source: RGD protein phosphatase type 1 complex Inferred from direct assay. Source: RGD
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine phosphatase activity Inferred from Experiment. Source: Reactome ribonucleoprotein binding Inferred from physical interaction. 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)
	P62138-1 [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: 1650776] [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: 2177460] [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: 7751917] [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: 15489334] [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: 10504266] [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: 17890166] [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
EMBLGenBankDDBJ	D00859 mRNA. Translation: BAA00732.1. D90163 mRNA. Translation: BAA14194.1. BC070517 mRNA. Translation: AAH70517.1.
IPI	IPI00208265.
PIR	JX0157.
RefSeq	NP_113715.1.
UniGene	Rn.2024
3D structure databases
SMR	P62138. Positions 7-300.
ModBase	Search...
Protein-protein interaction databases
STRING	P62138.
PTM databases
PhosphoSite	P62138.
Genome annotation databases
Ensembl	ENSRNOT00000025282; ENSRNOP00000025282; ENSRNOG00000018708; Rattus norvegicus. [Genome view]
GeneID	24668.
KEGG	rno:24668.
UCSC	NM_031527. rat.
Organism-specific databases
CTD	24668.
RGD	3375. Ppp1ca.
Phylogenomic databases
HOVERGEN	P62138.
OMA	LTPHCAP
Enzyme and pathway databases
BRENDA	3.1.3.16. 248.
Gene expression databases
ArrayExpress	P62138.
Genevestigator	P62138.
GermOnline	ENSRNOG00000018708. Rattus norvegicus.
Family and domain databases
InterPro	IPR004843. M-pesterase. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
PANTHER	PTHR11668. T_phtase_apaH. 1 hit.
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 Resources
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:	November 24, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)