PDP1_MOUSE
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 03-AUG-2022, entry version 126.
DE RecName: Full=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial;
DE Short=PDP 1;
DE EC=3.1.3.43;
DE AltName: Full=Protein phosphatase 2C;
DE AltName: Full=Pyruvate dehydrogenase phosphatase catalytic subunit 1;
DE Short=PDPC 1;
DE Flags: Precursor;
GN Name=Pdp1; Synonyms=Ppm2c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation
CC of the alpha subunit of the E1 component of the pyruvate dehydrogenase
CC complex. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha
CC subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] +
CC phosphate; Xref=Rhea:RHEA:12669, Rhea:RHEA-COMP:13689, Rhea:RHEA-
CC COMP:13690, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.43;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AK137550; BAE23403.1; -; mRNA.
DR CCDS; CCDS38694.1; -.
DR RefSeq; NP_001028625.1; NM_001033453.3.
DR RefSeq; NP_001091700.1; NM_001098230.1.
DR RefSeq; NP_001091701.1; NM_001098231.1.
DR RefSeq; NP_001277316.1; NM_001290387.1.
DR RefSeq; NP_001277320.1; NM_001290391.1.
DR AlphaFoldDB; Q3UV70; -.
DR SMR; Q3UV70; -.
DR BioGRID; 237972; 4.
DR IntAct; Q3UV70; 1.
DR STRING; 10090.ENSMUSP00000103934; -.
DR iPTMnet; Q3UV70; -.
DR PhosphoSitePlus; Q3UV70; -.
DR EPD; Q3UV70; -.
DR MaxQB; Q3UV70; -.
DR PaxDb; Q3UV70; -.
DR PRIDE; Q3UV70; -.
DR ProteomicsDB; 288090; -.
DR Antibodypedia; 12838; 279 antibodies from 32 providers.
DR DNASU; 381511; -.
DR Ensembl; ENSMUST00000056050; ENSMUSP00000050521; ENSMUSG00000049225.
DR Ensembl; ENSMUST00000108297; ENSMUSP00000103932; ENSMUSG00000049225.
DR GeneID; 381511; -.
DR KEGG; mmu:381511; -.
DR UCSC; uc008sab.2; mouse.
DR CTD; 54704; -.
DR MGI; MGI:2685870; Pdp1.
DR VEuPathDB; HostDB:ENSMUSG00000049225; -.
DR eggNOG; KOG0700; Eukaryota.
DR GeneTree; ENSGT00940000156368; -.
DR HOGENOM; CLU_021928_0_0_1; -.
DR InParanoid; Q3UV70; -.
DR OMA; SHFRYAP; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q3UV70; -.
DR Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR BioGRID-ORCS; 381511; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pdp1; mouse.
DR PRO; PR:Q3UV70; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3UV70; protein.
DR Bgee; ENSMUSG00000049225; Expressed in lateral geniculate body and 219 other tissues.
DR ExpressionAtlas; Q3UV70; baseline and differential.
DR Genevisible; Q3UV70; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosphatase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:MGI.
DR GO; GO:1904184; P:positive regulation of pyruvate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Hydrolase; Magnesium; Metal-binding; Mitochondrion;
KW Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..71
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 72..538
FT /note="[Pyruvate dehydrogenase [acetyl-transferring]]-
FT phosphatase 1, mitochondrial"
FT /id="PRO_0000045808"
FT DOMAIN 109..525
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J1"
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
