PDP1_RAT
ID PDP1_RAT Reviewed; 538 AA.
AC O88483;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=9651365; DOI=10.1074/jbc.273.28.17680;
RA Huang B., Gudi R., Wu P., Harris R.A., Hamilton J., Popov K.M.;
RT "Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid
RT sequences, expression, and regulation.";
RL J. Biol. Chem. 273:17680-17688(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 72-538, COFACTOR, METAL-BINDING
RP SITES, AND SUBUNIT.
RX PubMed=17532339; DOI=10.1016/j.jmb.2007.05.002;
RA Vassylyev D.G., Symersky J.;
RT "Crystal structure of pyruvate dehydrogenase phosphatase 1 and its
RT functional implications.";
RL J. Mol. Biol. 370:417-426(2007).
CC -!- FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation
CC of the alpha subunit of the E1 component of the pyruvate dehydrogenase
CC complex.
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;
CC Evidence={ECO:0000269|PubMed:17532339};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:17532339};
CC -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC subunit. {ECO:0000269|PubMed:17532339}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AF062740; AAC40167.1; -; mRNA.
DR PDB; 2PNQ; X-ray; 1.81 A; A/B=72-538.
DR PDBsum; 2PNQ; -.
DR AlphaFoldDB; O88483; -.
DR SMR; O88483; -.
DR IntAct; O88483; 5.
DR STRING; 10116.ENSRNOP00000062054; -.
DR iPTMnet; O88483; -.
DR PhosphoSitePlus; O88483; -.
DR PaxDb; O88483; -.
DR PRIDE; O88483; -.
DR UCSC; RGD:620393; rat.
DR RGD; 620393; Pdp1.
DR eggNOG; KOG0700; Eukaryota.
DR InParanoid; O88483; -.
DR PhylomeDB; O88483; -.
DR BRENDA; 3.1.3.43; 5301.
DR Reactome; R-RNO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR SABIO-RK; O88483; -.
DR EvolutionaryTrace; O88483; -.
DR PRO; PR:O88483; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosphatase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IMP:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:RGD.
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 DisProt; DP02657; -.
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 3D-structure; Acetylation; Calcium; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; 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_0000025420"
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 BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 516
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J1"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2PNQ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 125..136
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 138..149
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 150..167
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:2PNQ"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 205..221
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 232..253
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:2PNQ"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:2PNQ"
FT STRAND 518..525
FT /evidence="ECO:0007829|PDB:2PNQ"
FT HELIX 527..535
FT /evidence="ECO:0007829|PDB:2PNQ"
SQ SEQUENCE 538 AA; 61207 MW; D546096229B73564 CRC64;
MPAPTQLFFP LVRNCELSRI YGTACYCHHK HLCCSPPYIP QNRLRYTPHP AYATFCRPRE
NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSIL GFDSNRLPAN
APIEDRRSAT TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV
ESGRALLPIL QWHKHPNDYF SKEASKLYFN GLRTYWQELI DLNTGESADI DVKEALINAF
KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
EDGSWSAVTL SNDHNAQNER ELQRLKLEHP KNEAKSVVKQ DRLLGLLMPF RAFGDVKFKW
SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE VTYHRLRPQD KFLVLATDGL
WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRAKMS SVFEDQNAAT
HLIRHAVGNN EFGAVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ
