Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot O88483 (PDP1_RAT)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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):
    Pyruvate dehydrogenase phosphatase, catalytic subunit 1
      Short name=PDPC 1
    Protein phosphatase 2C
Gene names
Name: Pdp1
Synonyms: Ppm2c
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

Protein attributes

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

Hide | Top

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 (PDP1) and a regulatory (PDPR) subunit By similarity.

Subcellular location

Mitochondrion matrix.

Tissue specificity

Highly expressed in skeletal muscle.

Sequence similarities

Belongs to the PP2C family.

Hide | Top

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_0000025420

Sites

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

Secondary structure

1 ................................................................. 538
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
O88483-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D546096229B73564

FASTA53861,207
        10         20         30         40         50         60 
MPAPTQLFFP LVRNCELSRI YGTACYCHHK HLCCSPPYIP QNRLRYTPHP AYATFCRPRE 

        70         80         90        100        110        120 
NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSIL GFDSNRLPAN 

       130        140        150        160        170        180 
APIEDRRSAT TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV 

       190        200        210        220        230        240 
ESGRALLPIL QWHKHPNDYF SKEASKLYFN GLRTYWQELI DLNTGESADI DVKEALINAF 

       250        260        270        280        290        300 
KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE 

       310        320        330        340        350        360 
EDGSWSAVTL SNDHNAQNER ELQRLKLEHP 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

Hide | Top

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: Heart.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

AF062740 mRNA. Translation: AAC40167.1.
IPIIPI00209752.
UniGeneRn.31799

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2PNQX-ray1.81A/B72-538[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000016180. Rattus norvegicus. [Contig view]

Organism-specific databases

RGD620393. Ppm2c.

Phylogenomic databases

HOVERGENO88483.

Enzyme and pathway databases

BRENDA3.1.3.43. 248.

Gene expression databases

ArrayExpressO88483.
GermOnlineENSRNOG00000016180. Rattus norvegicus.

Family and domain databases

InterProIPR015655. PP2C.
IPR001932. PP2C-related.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR014045. PP2C_N.
[Graphical view]
Gene3DG3DSA:3.60.40.10. PP2C-related. 1 hit.
PANTHERPTHR13832. PP2C. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry namePDP1_RAT
AccessionPrimary (citable) accession number: O88483
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents