PDP2_HUMAN
ID PDP2_HUMAN Reviewed; 529 AA.
AC Q9P2J9; A8K924;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
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; Synonyms=KIAA1348;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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. {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 subunit and a FAD protein of
CC unknown function. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB037769; BAA92586.1; ALT_INIT; mRNA.
DR EMBL; AK292539; BAF85228.1; -; mRNA.
DR EMBL; CH471092; EAW83048.1; -; Genomic_DNA.
DR EMBL; BC028030; AAH28030.1; -; mRNA.
DR CCDS; CCDS10822.1; -.
DR RefSeq; NP_001316857.1; NM_001329928.1.
DR RefSeq; NP_001316858.1; NM_001329929.1.
DR RefSeq; NP_001316859.1; NM_001329930.1.
DR RefSeq; NP_001316860.1; NM_001329931.1.
DR RefSeq; NP_001316861.1; NM_001329932.1.
DR RefSeq; NP_001316862.1; NM_001329933.1.
DR RefSeq; NP_001316863.1; NM_001329934.1.
DR RefSeq; NP_065837.1; NM_020786.3.
DR AlphaFoldDB; Q9P2J9; -.
DR SMR; Q9P2J9; -.
DR BioGRID; 121604; 18.
DR IntAct; Q9P2J9; 11.
DR MINT; Q9P2J9; -.
DR STRING; 9606.ENSP00000309548; -.
DR DEPOD; PDP2; -.
DR iPTMnet; Q9P2J9; -.
DR PhosphoSitePlus; Q9P2J9; -.
DR BioMuta; PDP2; -.
DR DMDM; 12585321; -.
DR EPD; Q9P2J9; -.
DR jPOST; Q9P2J9; -.
DR MassIVE; Q9P2J9; -.
DR MaxQB; Q9P2J9; -.
DR PaxDb; Q9P2J9; -.
DR PeptideAtlas; Q9P2J9; -.
DR PRIDE; Q9P2J9; -.
DR ProteomicsDB; 83825; -.
DR Antibodypedia; 15590; 147 antibodies from 25 providers.
DR DNASU; 57546; -.
DR Ensembl; ENST00000311765.4; ENSP00000309548.2; ENSG00000172840.7.
DR GeneID; 57546; -.
DR KEGG; hsa:57546; -.
DR MANE-Select; ENST00000311765.4; ENSP00000309548.2; NM_020786.4; NP_065837.1.
DR UCSC; uc002eqk.3; human.
DR CTD; 57546; -.
DR DisGeNET; 57546; -.
DR GeneCards; PDP2; -.
DR HGNC; HGNC:30263; PDP2.
DR HPA; ENSG00000172840; Low tissue specificity.
DR MIM; 615499; gene.
DR neXtProt; NX_Q9P2J9; -.
DR OpenTargets; ENSG00000172840; -.
DR PharmGKB; PA165450460; -.
DR VEuPathDB; HostDB:ENSG00000172840; -.
DR eggNOG; KOG0700; Eukaryota.
DR GeneTree; ENSGT00940000160687; -.
DR HOGENOM; CLU_021928_0_0_1; -.
DR InParanoid; Q9P2J9; -.
DR OMA; DHNAWNP; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q9P2J9; -.
DR TreeFam; TF313505; -.
DR BRENDA; 3.1.3.43; 2681.
DR PathwayCommons; Q9P2J9; -.
DR Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR SignaLink; Q9P2J9; -.
DR SIGNOR; Q9P2J9; -.
DR BioGRID-ORCS; 57546; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; PDP2; human.
DR GenomeRNAi; 57546; -.
DR Pharos; Q9P2J9; Tbio.
DR PRO; PR:Q9P2J9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9P2J9; protein.
DR Bgee; ENSG00000172840; Expressed in ileal mucosa and 164 other tissues.
DR ExpressionAtlas; Q9P2J9; baseline and differential.
DR Genevisible; Q9P2J9; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..66
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 67..529
FT /note="[Pyruvate dehydrogenase [acetyl-transferring]]-
FT phosphatase 2, mitochondrial"
FT /id="PRO_0000025421"
FT DOMAIN 106..517
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 529 AA; 59978 MW; 252CAEBCDAF61A5C CRC64;
MSSTVSYWIL NSTRNSIATL QGGRRLYSRY VSNRNKLKWR LFSRVPPTLN SSPCGGFTLC
KAYRHTSTEE DDFHLQLSPE QINEVLRAGE TTHKILDLES RVPNSVLRFE SNQLAANSPV
EDRRGVASCL QTNGLMFGIF DGHGGHACAQ AVSERLFYYV AVSLMSHQTL EHMEGAMESM
KPLLPILHWL KHPGDSIYKD VTSVHLDHLR VYWQELLDLH MEMGLSIEEA LMYSFQRLDS
DISLEIQAPL EDEVTRNLSL QVAFSGATAC MAHVDGIHLH VANAGDCRAI LGVQEDNGMW
SCLPLTRDHN AWNQAELSRL KREHPESEDR TIIMEDRLLG VLIPCRAFGD VQLKWSKELQ
RSILERGFNT EALNIYQFTP PHYYTPPYLT AEPEVTYHRL RPQDKFLVLA SDGLWDMLSN
EDVVRLVVGH LAEADWHKTD LAQRPANLGL MQSLLLQRKA SGLHEADQNA ATRLIRHAIG
NNEYGEMEAE RLAAMLTLPE DLARMYRDDI TVTVVYFNSE SIGAYYKGG
