Reviewed, UniProtKB/Swiss-Prot O88484 (PDP2_RAT)

Names and origin

Protein names

Recommended name:
    [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial
      Short name=PDP 2
    EC=3.1.3.43
Alternative name(s):
    Pyruvate dehydrogenase phosphatase, catalytic subunit 2
      Short name=PDPC 2

Gene names

Name:

Pdp2

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

General annotation (Comments)

Function	Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.
Catalytic activity	[Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Subunit structure	Heterodimer of a catalytic subunit and a FAD protein of unknown function By similarity.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Highly expressed in liver.
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological process	carbohydrate utilization Ref.1 Traceable author statement. Source: RGD protein amino acid dephosphorylation Inferred from direct assay. Source: RGD
Cellular component	mitochondrial pyruvate dehydrogenase (lipoamide) phosphatase complex Ref.1 Traceable author statement. Source: RGD protein serine/threonine phosphatase complex Inferred from electronic annotation. Source: InterPro
Molecular function	[pyruvate dehydrogenase (lipoamide)] phosphatase activity Ref.1 Inferred from direct assay. Source: RGD magnesium ion binding Inferred by curator. Source: RGD magnesium-dependent protein serine/threonine phosphatase activity Inferred from direct assay. Source: RGD manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 67	67	Mitochondrion Potential
	Chain	68 – 530	463	[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial		PRO_0000025422
Sites
	Metal binding	142	1	Manganese 1 By similarity
	Metal binding	142	1	Manganese 2 By similarity
	Metal binding	143	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	413	1	Manganese 2 By similarity
Experimental info
	Sequence conflict	137	1	V → M in AAH72485. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O88484-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 5AB688FAC78AD9CD	FASTA	530	59,654
	10 20 30 40 50 60 MSSTASYRIF NFARNRIAVL RGGRRLYSRA ATSRNQVKWR LFSPASLAVN DSSPHGGFAL 70 80 90 100 110 120 RKAYRHTSTE EEDFHLQLSP EQVSDLLRAG ESSHKVLDFN SGVPNSVLRF ESNQLAANSP 130 140 150 160 170 180 VEDRQGVASC VQTRGTVFGI FDGHGGHACA QAVSERLFYY MAVSLMSHKT LEQMEEAMEN 190 200 210 220 230 240 MKPLLPILQW LKHPGDSIYK DITSVHLDHL RVYWQELLDL HMETGLSTEE ALMYSFQRLD 250 260 270 280 290 300 SDISLEIQAP LEDEVTKNLS LQVAFSGATA CMAHVDGVHL HIANAGDCRA ILGVQGDNGA 310 320 330 340 350 360 WSCLPLTCDH NAWNEAELSR LKREHPESED RTLIIDDRLL GVLLPCRAFG DVQLKWSKEL 370 380 390 400 410 420 QRNVLERGFD TEALNIYQFT PPHYHTPPYL TAKPEVTYHR LRPQDKFLVL ASDGLWDMLD 430 440 450 460 470 480 NEDVVRLVVG HLSKVGHQKP ALDQRPANLG HMQSLLLQRK ASGLHAADQN AATHLIRHAI 490 500 510 520 530 GSNEYGEMEP ERLAAMLTLP EDVARMYRDD ITVMVVFFNS ESIDTYFKEG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression, and regulation." Huang B., Gudi R., Wu P., Harris R.A., Hamilton J., Popov K.M. J. Biol. Chem. 273:17680-17688(1998) [PubMed: 9651365] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF062741 mRNA. Translation: AAC40168.1. BC072485 mRNA. Translation: AAH72485.1.
IPI	IPI00209753.
RefSeq	NP_659559.2.
UniGene	Rn.220381
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000012343. Rattus norvegicus. [Contig view]
GeneID	246311.
KEGG	rno:246311.
Organism-specific databases
RGD	628812. Pdp2.
Phylogenomic databases
HOVERGEN	O88484.
Enzyme and pathway databases
BRENDA	3.1.3.43. 248.
Gene expression databases
ArrayExpress	O88484.
GermOnline	ENSRNOG00000012343. Rattus norvegicus.
Family and domain databases
InterPro	IPR015655. PP2C. IPR001932. PP2C-related. IPR000222. PP2C_Mn2_Asp60_BS. IPR014045. PP2C_N. [Graphical view]
Gene3D	G3DSA:3.60.40.10. PP2C-related. 1 hit.
PANTHER	PTHR13832. PP2C. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	623736.

Entry information

Entry name

PDP2_RAT

Accession

Primary (citable) accession number: O88484
Secondary accession number(s): Q6IN27

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)