LOCUS       NP_001004072             390 aa            linear   ROD 27-APR-2025
DEFINITION  pyruvate dehydrogenase E1 component subunit alpha, somatic form,
            mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_001004072 XP_343788
VERSION     NP_001004072.2
DBSOURCE    REFSEQ: accession NM_001004072.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Sharkia,I., Hadad Erlich,T., Landolina,N., Assayag,M., Motzik,A.,
            Rachmin,I., Kay,G., Porat,Z., Tshori,S., Berkman,N.,
            Levi-Schaffer,F. and Razin,E.
  TITLE     Pyruvate dehydrogenase has a major role in mast cell function, and
            its activity is regulated by mitochondrial microphthalmia
            transcription factor
  JOURNAL   J Allergy Clin Immunol 140 (1), 204-214 (2017)
   PUBMED   27871875
  REMARK    GeneRIF: The association of mitochondrial microphthalmia-associated
            transcription factor (MITF) with pyruvate dehydrogenase (PDH)
            emerges as an important regulator of mast cell function. Our
            findings indicate that PDH could arise as a new target for the
            manipulation of allergic diseases.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Terzenidou,M.E., Segklia,A., Kano,T., Papastefanaki,F.,
            Karakostas,A., Charalambous,M., Ioakeimidis,F., Papadaki,M.,
            Kloukina,I., Chrysanthou-Piterou,M., Samiotaki,M., Panayotou,G.,
            Matsas,R. and Douni,E.
  TITLE     Novel insights into SLC25A46-related pathologies in a genetic mouse
            model
  JOURNAL   PLoS Genet 13 (4), e1006656 (2017)
   PUBMED   28376086
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Bunik,V.I., Artiukhov,A., Kazantsev,A., Goncalves,R., Daloso,D.,
            Oppermann,H., Kulakovskaya,E., Lukashev,N., Fernie,A., Brand,M. and
            Gaunitz,F.
  TITLE     Specific inhibition by synthetic analogs of pyruvate reveals that
            the pyruvate dehydrogenase reaction is essential for metabolism and
            viability of glioblastoma cells
  JOURNAL   Oncotarget 6 (37), 40036-40052 (2015)
   PUBMED   26503465
  REMARK    GeneRIF: Data indicate that catalytic transformation of pyruvate by
            pyruvate dehydrogenase is essential for the metabolism and
            viability of glioblastoma cell lines.
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Akhmedov,D., De Marchi,U., Wollheim,C.B. and Wiederkehr,A.
  TITLE     Pyruvate dehydrogenase E1alpha phosphorylation is induced by
            glucose but does not control metabolism-secretion coupling in
            INS-1E clonal beta-cells
  JOURNAL   Biochim Biophys Acta 1823 (10), 1815-1824 (2012)
   PUBMED   22809973
  REMARK    GeneRIF: Although glucose stimulates E1alpha phosphorylation and
            therefore inhibits PDH activity, this control mechanism by itself
            does not alter metabolism-secretion coupling in INS-1E clonal
            beta-cells.
REFERENCE   5  (residues 1 to 390)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Johnson,M.T., Mahmood,S., Hyatt,S.L., Yang,H.S., Soloway,P.D.,
            Hanson,R.W. and Patel,M.S.
  TITLE     Inactivation of the murine pyruvate dehydrogenase (Pdha1) gene and
            its effect on early embryonic development
  JOURNAL   Mol Genet Metab 74 (3), 293-302 (2001)
   PUBMED   11708858
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Lissens,W., De Meirleir,L., Seneca,S., Liebaers,I., Brown,G.K.,
            Brown,R.M., Ito,M., Naito,E., Kuroda,Y., Kerr,D.S., Wexler,I.D.,
            Patel,M.S., Robinson,B.H. and Seyda,A.
  TITLE     Mutations in the X-linked pyruvate dehydrogenase (E1) alpha subunit
            gene (PDHA1) in patients with a pyruvate dehydrogenase complex
            deficiency
  JOURNAL   Hum Mutat 15 (3), 209-219 (2000)
   PUBMED   10679936
  REMARK    Review article
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Maury,J., Kerbey,A.L., Priestman,D.A., Patel,M.S., Girard,J. and
            Ferre,P.
  TITLE     Pretranslational regulation of pyruvate dehydrogenase complex
            subunits in white adipose tissue during the suckling-weaning
            transition in the rat
  JOURNAL   Biochem J 311 (Pt 2) (Pt 2), 531-535 (1995)
   PUBMED   7487891
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Cullingford,T.E., Clark,J.B. and Phillips,I.R.
  TITLE     The pyruvate dehydrogenase complex: cloning of the rat somatic E1
            alpha subunit and its coordinate expression with the mRNAs for the
            E1 beta, E2, and E3 catalytic subunits in developing rat brain
  JOURNAL   J Neurochem 62 (5), 1682-1690 (1994)
   PUBMED   8158120
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Matuda,S., Nakano,K., Ohta,S., Saheki,T., Kawanishi,Y. and
            Miyata,T.
  TITLE     The alpha-ketoacid dehydrogenase complexes. Sequence similarity of
            rat pyruvate dehydrogenase with Escherichia coli and Azotobacter
            vinelandii alpha-ketoglutarate dehydrogenase
  JOURNAL   Biochim Biophys Acta 1089 (1), 1-7 (1991)
   PUBMED   2025639
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC098897.1.
            
            On Feb 3, 2007 this sequence version replaced NP_001004072.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098897.1, BC079369.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq14"
     Protein         1..390
                     /product="pyruvate dehydrogenase E1 component subunit
                     alpha, somatic form, mitochondrial precursor"
                     /EC_number="1.2.4.1"
                     /note="pyruvate dehydrogenase E1 component subunit alpha,
                     somatic form, mitochondrial; PDHE1-A type I; pyruvate
                     dehydrogenase E1alpha subunit; pyruvate dehydrogenase
                     (lipoamide) alpha 1; pyruvate dehydrogenase alpha 1;
                     pyruvate dehydrogenase E1 alpha 1 subunit"
                     /calculated_mol_wt=40181
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P26284.2)"
                     /calculated_mol_wt=3053
     mat_peptide     30..390
                     /product="Pyruvate dehydrogenase E1 component subunit
                     alpha, somatic form, mitochondrial. /id=PRO_0000020445"
                     /note="propagated from UniProtKB/Swiss-Prot (P26284.2)"
                     /calculated_mol_wt=40181
     Region          58..370
                     /region_name="PDH_E1_alph_y"
                     /note="pyruvate dehydrogenase E1 component, alpha subunit;
                     TIGR03182"
                     /db_xref="CDD:274473"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            order(88,140,165..166,197,199..202,205,209,213,228..231,
                     245,296,300)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238958"
     Site            order(118..119,165,167,195..198,225,227,292)
                     /site_type="other"
                     /note="TPP-binding site [chemical binding]"
                     /db_xref="CDD:238958"
     Site            order(160,162,164,169,172..173,176..177,179..180,183,
                     202..203,209..210,213)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:238958"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDK1.
                     /evidence=ECO:0000269|PubMed:19341700; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            order(287..293,295..305,314..316)
                     /site_type="phosphorylation"
                     /note="phosphorylation loop region [posttranslational
                     modification]"
                     /db_xref="CDD:238958"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDK1, PDK2, PDK3 and PDK4.
                     /evidence=ECO:0000269|PubMed:19341700; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDK1, PDK2, PDK3 and PDK4.
                     /evidence=ECO:0000269|PubMed:19341700; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            313
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08559; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            336
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     CDS             1..390
                     /gene="Pdha1"
                     /coded_by="NM_001004072.2:39..1211"
                     /db_xref="GeneID:29554"
                     /db_xref="RGD:3286"
ORIGIN      
        1 mrkmlaavsr vlagaaqkpa srvlvasrnf andatfeikk cdlhrleegp pvttvltred
       61 glkyyrmmqt vrrmelkadq lykqkiirgf chlcdgqeac cvgleaginp tdhlitayra
      121 hgftftrglp vrailaeltg rrggcakgkg gsmhmyaknf yggngivgaq vplgagiala
      181 ckyngkdevc ltlygdgaan qgqifeaynm aalwklpcif icennrygmg tsveraaast
      241 dyykrgdfip glrvdgmdil cvreatkfaa aycrsgkgpi lmelqtyryh ghsmsdpgvs
      301 yrtreeiqev rsksdpimll kdrmvnsnla sveelkeidv evrkeiedaa qfatadpepp
      361 leelgyhiys sdppfevrga nqwikfksvs
//
