Reviewed, UniProtKB/Swiss-Prot Q3UV70 (PDP1_MOUSE)

Names and origin

Protein names

Recommended name:
    [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
      Short name=PDP 1
    EC=3.1.3.43
Alternative name(s):
    Pyruvate dehydrogenase phosphatase, catalytic subunit 1
      Short name=PDPC 1
    Protein phosphatase 2C

Gene names

Name:	Pdp1
Synonyms:	Ppm2c

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	538 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 By similarity.
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 (PDP1) and a regulatory (PDPR) subunit By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Calcium Magnesium Metal-binding
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell protein serine/threonine phosphatase complex Inferred from electronic annotation. Source: InterPro
Molecular function	[pyruvate dehydrogenase (lipoamide)] phosphatase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 71	71	Mitochondrion By similarity
	Chain	72 – 538	467	[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial		PRO_0000045808
Sites
	Metal binding	144	1	Magnesium 1 By similarity
	Metal binding	144	1	Magnesium 2 By similarity
	Metal binding	145	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	418	1	Magnesium 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3UV70-1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: A32049DED0FC58EE	FASTA	538	61,180
	10 20 30 40 50 60 MPAPTQLFFP LVRNCELSRI YGTACYCHHK HLCCSPPYIP QNRLRYTPHP AYATFCRPRE 70 80 90 100 110 120 NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSIL GFDSNQLPAN 130 140 150 160 170 180 APIEDRRSAA TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV 190 200 210 220 230 240 ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESADI DVKEALINAF 250 260 270 280 290 300 KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE 310 320 330 340 350 360 EDGSWSAVTL SNDHNAQNER ELERLKLEHP KNEAKSVVKQ DRLLGLLMPF RAFGDVKFKW 370 380 390 400 410 420 SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE VTYHRLRPQD KFLVLATDGL 430 440 450 460 470 480 WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRAKMS SVFEDQNAAT 490 500 510 520 530 HLIRHAVGNN EFGAVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ

References

[1]

"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK137550 mRNA. Translation: BAE23403.1.
IPI	IPI00672824.
RefSeq	NP_001028625.1. NP_001091700.1. NP_001091701.1.
UniGene	Mm.331489
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q3UV70.
Genome annotation databases
Ensembl	ENSMUSG00000049225. Mus musculus. [Contig view]
GeneID	381511.
KEGG	mmu:381511.
Organism-specific databases
MGI	MGI:2685870. Ppm2c.
Phylogenomic databases
HOGENOM	Q3UV70.
HOVERGEN	Q3UV70.
Enzyme and pathway databases
BRENDA	3.1.3.43. 244.
Gene expression databases
ArrayExpress	Q3UV70.
Bgee	Q3UV70.
GermOnline	ENSMUSG00000049225. Mus musculus.
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	402166.
SOURCE	Search...

Entry information

Entry name

PDP1_MOUSE

Accession

Primary (citable) accession number: Q3UV70

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	October 11, 2005
Last modified:	February 10, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)