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Q3UV70 (PDP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
Short name=PDP 1
EC=3.1.3.43
Alternative name(s):
Protein phosphatase 2C
Pyruvate dehydrogenase phosphatase catalytic subunit 1
Short name=PDPC 1
Gene names
Name:Pdp1
Synonyms:Ppm2c
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7171Mitochondrion By similarity
Chain72 – 538467[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
PRO_0000045808

Sites

Metal binding1441Magnesium 1 By similarity
Metal binding1441Magnesium 2 By similarity
Metal binding1451Magnesium 1; via carbonyl oxygen By similarity
Metal binding4181Magnesium 2 By similarity

Amino acid modifications

Modified residue2021N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3UV70 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: A32049DED0FC58EE

FASTA53861,180
        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

« Hide

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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK137550 mRNA. Translation: BAE23403.1.
IPIIPI00672824.
RefSeqNP_001028625.1. NM_001033453.3.
NP_001091700.1. NM_001098230.1.
NP_001091701.1. NM_001098231.1.
UniGeneMm.331489.

3D structure databases

ProteinModelPortalQ3UV70.
SMRQ3UV70. Positions 80-538.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3UV70.

PTM databases

PhosphoSiteQ3UV70.

Proteomic databases

PRIDEQ3UV70.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056050; ENSMUSP00000050521; ENSMUSG00000049225.
ENSMUST00000108297; ENSMUSP00000103932; ENSMUSG00000049225.
GeneID381511.
KEGGmmu:381511.

Organism-specific databases

CTD54704.
MGIMGI:2685870. Pdp1.

Phylogenomic databases

GeneTreeENSGT00390000006874.
HOVERGENHBG008162.
InParanoidQ3UV70.
OrthoDBEOG4XD3QP.
PhylomeDBQ3UV70.

Gene expression databases

ArrayExpressQ3UV70.
BgeeQ3UV70.
GenevestigatorQ3UV70.
GermOnlineENSMUSG00000049225. Mus musculus.

Family and domain databases

InterProIPR001932. PP2C-like.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
Gene3DG3DSA:3.60.40.10. PP2C-related. 3 hits.
KOK01102.
PANTHERPTHR13832. PP2C. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. PP2C-related. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio402166.
SOURCESearch...

Entry information

Entry namePDP1_MOUSE
AccessionPrimary (citable) accession number: Q3UV70
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 11, 2005
Last modified: November 16, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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