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   27-MAR-2024, entry version 163.
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,
RC   Pancreas, 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; 15.
DR   IntAct; Q8BKZ9; 9.
DR   MINT; Q8BKZ9; -.
DR   STRING; 10090.ENSMUSP00000011058; -.
DR   GlyGen; Q8BKZ9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BKZ9; -.
DR   PhosphoSitePlus; Q8BKZ9; -.
DR   SwissPalm; Q8BKZ9; -.
DR   REPRODUCTION-2DPAGE; IPI00222767; -.
DR   EPD; Q8BKZ9; -.
DR   jPOST; Q8BKZ9; -.
DR   MaxQB; Q8BKZ9; -.
DR   PaxDb; 10090-ENSMUSP00000011058; -.
DR   PeptideAtlas; Q8BKZ9; -.
DR   ProteomicsDB; 289964; -.
DR   Pumba; Q8BKZ9; -.
DR   Antibodypedia; 25893; 324 antibodies from 35 providers.
DR   DNASU; 27402; -.
DR   Ensembl; ENSMUST00000011058.9; ENSMUSP00000011058.3; ENSMUSG00000010914.11.
DR   GeneID; 27402; -.
DR   KEGG; mmu:27402; -.
DR   UCSC; uc008lil.3; mouse.
DR   AGR; MGI:1351627; -.
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; TIKQKPW; -.
DR   OrthoDB; 5483022at2759; -.
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; 6 hits in 79 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 225 other cell types or tissues.
DR   ExpressionAtlas; Q8BKZ9; baseline and differential.
DR   GO; GO:1902493; C:acetyltransferase complex; ISO:MGI.
DR   GO; GO:0045240; C:dihydrolipoyl dehydrogenase complex; ISO:MGI.
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; IEA:Ensembl.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISO:MGI.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 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; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF9; PYRUVATE DEHYDROGENASE PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
DR   Genevisible; Q8BKZ9; MM.
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
//