ODPX_MOUSE
ID ODPX_MOUSE Reviewed; 501 AA.
AC Q8BKZ9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Pyruvate dehydrogenase protein X component, mitochondrial;
DE AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex;
DE AltName: Full=Lipoyl-containing pyruvate dehydrogenase complex component X;
DE Flags: Precursor;
GN Name=Pdhx;
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=Corpus striatum;
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 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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-394, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to
CC the dihydrolipoamide transacetylase (E2) core of the pyruvate
CC dehydrogenase complexes of eukaryotes. This specific binding is
CC essential for a functional PDH complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the inner core of the multimeric pyruvate
CC dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX
CC molecules. This core binds multiple copies of pyruvate dehydrogenase
CC (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase
CC (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). Interacts with SIRT4.
CC Interacts with DLD. {ECO:0000250|UniProtKB:O00330}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD
CC complex activity. {ECO:0000250|UniProtKB:O00330}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AK047670; BAC33120.1; -; mRNA.
DR EMBL; BC061231; AAH61231.1; -; mRNA.
DR CCDS; CCDS16473.1; -.
DR RefSeq; NP_780303.1; NM_175094.5.
DR AlphaFoldDB; Q8BKZ9; -.
DR SMR; Q8BKZ9; -.
DR BioGRID; 205209; 12.
DR IntAct; Q8BKZ9; 9.
DR MINT; Q8BKZ9; -.
DR STRING; 10090.ENSMUSP00000011058; -.
DR iPTMnet; Q8BKZ9; -.
DR PhosphoSitePlus; Q8BKZ9; -.
DR SwissPalm; Q8BKZ9; -.
DR REPRODUCTION-2DPAGE; IPI00222767; -.
DR EPD; Q8BKZ9; -.
DR jPOST; Q8BKZ9; -.
DR MaxQB; Q8BKZ9; -.
DR PaxDb; Q8BKZ9; -.
DR PeptideAtlas; Q8BKZ9; -.
DR PRIDE; Q8BKZ9; -.
DR ProteomicsDB; 289964; -.
DR Antibodypedia; 25893; 303 antibodies from 35 providers.
DR DNASU; 27402; -.
DR Ensembl; ENSMUST00000011058; ENSMUSP00000011058; ENSMUSG00000010914.
DR GeneID; 27402; -.
DR KEGG; mmu:27402; -.
DR UCSC; uc008lil.3; mouse.
DR CTD; 8050; -.
DR MGI; MGI:1351627; Pdhx.
DR VEuPathDB; HostDB:ENSMUSG00000010914; -.
DR eggNOG; KOG0557; Eukaryota.
DR GeneTree; ENSGT00940000156046; -.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; Q8BKZ9; -.
DR OMA; QVTVIKH; -.
DR OrthoDB; 747232at2759; -.
DR PhylomeDB; Q8BKZ9; -.
DR TreeFam; TF332256; -.
DR Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR Reactome; R-MMU-70268; Pyruvate metabolism.
DR BioGRID-ORCS; 27402; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Pdhx; mouse.
DR PRO; PR:Q8BKZ9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BKZ9; protein.
DR Bgee; ENSMUSG00000010914; Expressed in interventricular septum and 222 other tissues.
DR ExpressionAtlas; Q8BKZ9; baseline and differential.
DR Genevisible; Q8BKZ9; MM.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; ISO:MGI.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0034604; F:pyruvate dehydrogenase (NAD+) activity; ISO:MGI.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISO:MGI.
DR GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; ISO:MGI.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; PTHR23151; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lipoyl; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 54..501
FT /note="Pyruvate dehydrogenase protein X component,
FT mitochondrial"
FT /id="PRO_0000020485"
FT DOMAIN 56..132
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 183..220
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 145..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00330"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00330"
FT MOD_RES 394
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 501 AA; 53999 MW; 3FD1FA752EAC5092 CRC64;
MAASWRLHCN QPLLRYLLGF SSRRSLGLAQ GAAAWPVDRG ASWRWFHSTQ LLQADPIKVL
MPSLSPTMEQ GNIVKWLRKE GEAVSAGDSL CEIETDKAVV TLDANDDGIL AKIVVEEGAK
NIQLGSLIAL MVEEGEDWKQ VEIPKDVSAP PPVSKPPAPT QPSPQPQIPC PARKEHKGTA
RFRLSPAARN ILEKHSLDAS QGTATGPRGI FTKEDALKLV ELKQMGKITE SRPASAPPPS
LSASVPPQAT AGPSYPRPMT PPVSIPGQPN AAGTFTEIPA SNIRRVIAKR LTESKSTVPH
AYATADCDLG AVLKVRRDLV KDDIKVSVND FIIRAAAVTL KQMPGVNVTW DGEGPKQLPS
VDISVAVATD KGLITPIIKD AAAKGIQEIA DSVKVLSKKA RDGKLMPEEY QGGSFSISNL
GMFGIDEFAA VINPPQACIL AVGRFRPVLK LTEDEEGNPQ LQQHQLITVT MSSDSRVVDD
ELATRFLETF KANLENPMRL G
