PDP2_RAT
ID PDP2_RAT Reviewed; 530 AA.
AC O88484; Q6IN27;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial;
DE Short=PDP 2;
DE EC=3.1.3.43;
DE AltName: Full=Pyruvate dehydrogenase phosphatase catalytic subunit 2;
DE Short=PDPC 2;
DE Flags: Precursor;
GN Name=Pdp2;
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=Liver;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and a FAD protein of
CC unknown function. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AF062741; AAC40168.1; -; mRNA.
DR EMBL; BC072485; AAH72485.1; -; mRNA.
DR RefSeq; NP_659559.2; NM_145091.4.
DR RefSeq; XP_006255110.1; XM_006255048.3.
DR AlphaFoldDB; O88484; -.
DR SMR; O88484; -.
DR STRING; 10116.ENSRNOP00000016462; -.
DR PaxDb; O88484; -.
DR PRIDE; O88484; -.
DR GeneID; 246311; -.
DR KEGG; rno:246311; -.
DR UCSC; RGD:628812; rat.
DR CTD; 57546; -.
DR RGD; 628812; Pdp2.
DR eggNOG; KOG0700; Eukaryota.
DR InParanoid; O88484; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; O88484; -.
DR TreeFam; TF313505; -.
DR BRENDA; 3.1.3.43; 5301.
DR Reactome; R-RNO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR PRO; PR:O88484; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
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 GO; GO:0042594; P:response to starvation; IEP:RGD.
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 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..67
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 68..530
FT /note="[Pyruvate dehydrogenase [acetyl-transferring]]-
FT phosphatase 2, mitochondrial"
FT /id="PRO_0000025422"
FT DOMAIN 107..518
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 137
FT /note="V -> M (in Ref. 2; AAH72485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 59654 MW; 5AB688FAC78AD9CD CRC64;
MSSTASYRIF NFARNRIAVL RGGRRLYSRA ATSRNQVKWR LFSPASLAVN DSSPHGGFAL
RKAYRHTSTE EEDFHLQLSP EQVSDLLRAG ESSHKVLDFN SGVPNSVLRF ESNQLAANSP
VEDRQGVASC VQTRGTVFGI FDGHGGHACA QAVSERLFYY MAVSLMSHKT LEQMEEAMEN
MKPLLPILQW LKHPGDSIYK DITSVHLDHL RVYWQELLDL HMETGLSTEE ALMYSFQRLD
SDISLEIQAP LEDEVTKNLS LQVAFSGATA CMAHVDGVHL HIANAGDCRA ILGVQGDNGA
WSCLPLTCDH NAWNEAELSR LKREHPESED RTLIIDDRLL GVLLPCRAFG DVQLKWSKEL
QRNVLERGFD TEALNIYQFT PPHYHTPPYL TAKPEVTYHR LRPQDKFLVL ASDGLWDMLD
NEDVVRLVVG HLSKVGHQKP ALDQRPANLG HMQSLLLQRK ASGLHAADQN AATHLIRHAI
GSNEYGEMEP ERLAAMLTLP EDVARMYRDD ITVMVVFFNS ESIDTYFKEG
