ID   PDP1_MOUSE              Reviewed;         538 AA.
AC   Q3UV70;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   10-FEB-2009, entry version 30.
DE   RecName: Full=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial;
DE            Short=PDP 1;
DE            EC=3.1.3.43;
DE   AltName: Full=Pyruvate dehydrogenase phosphatase, catalytic subunit 1;
DE            Short=PDPC 1;
DE   AltName: Full=Protein phosphatase 2C;
DE   Flags: Precursor;
GN   Name=Pdp1; Synonyms=Ppm2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Catalyzes the dephosphorylation and concomitant
CC       reactivation of the alpha subunit of the E1 component of the
CC       pyruvate dehydrogenase complex (By similarity).
CC   -!- CATALYTIC ACTIVITY: [Pyruvate dehydrogenase (acetyl-transferring)]
CC       phosphate + H(2)O = [pyruvate dehydrogenase (acetyl-transferring)]
CC       + phosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC       subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the PP2C family.
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DR   EMBL; AK137550; BAE23403.1; -; mRNA.
DR   IPI; IPI00672824; -.
DR   RefSeq; NP_001028625.1; -.
DR   RefSeq; NP_001091700.1; -.
DR   RefSeq; NP_001091701.1; -.
DR   UniGene; Mm.331489; -.
DR   PhosphoSite; Q3UV70; -.
DR   Ensembl; ENSMUSG00000049225; Mus musculus.
DR   GeneID; 381511; -.
DR   KEGG; mmu:381511; -.
DR   MGI; MGI:2685870; Ppm2c.
DR   HOGENOM; Q3UV70; -.
DR   HOVERGEN; Q3UV70; -.
DR   BRENDA; 3.1.3.43; 244.
DR   NextBio; 402166; -.
DR   ArrayExpress; Q3UV70; -.
DR   Bgee; Q3UV70; -.
DR   GermOnline; ENSMUSG00000049225; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; IEA:InterPro.
DR   GO; GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosph...; IEA:EC.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR001932; PP2C-related.
DR   InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR   InterPro; IPR014045; PP2C_N.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 1.
DR   PANTHER; PTHR13832; PP2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   PROSITE; PS01032; PP2C; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Hydrolase; Magnesium; Metal-binding; Mitochondrion;
KW   Protein phosphatase; Transit peptide.
FT   TRANSIT       1     71       Mitochondrion (By similarity).
FT   CHAIN        72    538       [Pyruvate dehydrogenase [acetyl-
FT                                transferring]]-phosphatase 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000045808.
FT   METAL       144    144       Magnesium 1 (By similarity).
FT   METAL       144    144       Magnesium 2 (By similarity).
FT   METAL       145    145       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       418    418       Magnesium 2 (By similarity).
SQ   SEQUENCE   538 AA;  61180 MW;  A32049DED0FC58EE CRC64;
     MPAPTQLFFP LVRNCELSRI YGTACYCHHK HLCCSPPYIP QNRLRYTPHP AYATFCRPRE
     NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSIL GFDSNQLPAN
     APIEDRRSAA TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV
     ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESADI DVKEALINAF
     KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
     EDGSWSAVTL SNDHNAQNER ELERLKLEHP KNEAKSVVKQ DRLLGLLMPF RAFGDVKFKW
     SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE VTYHRLRPQD KFLVLATDGL
     WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRAKMS SVFEDQNAAT
     HLIRHAVGNN EFGAVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ
//