LOCUS       NP_001100051             415 aa            linear   ROD 28-MAR-2024
DEFINITION  pyruvate dehydrogenase kinase, isozyme 3 [Rattus norvegicus].
ACCESSION   NP_001100051 XP_001056460 XP_038955496 XP_216091
VERSION     NP_001100051.1
DBSOURCE    REFSEQ: accession NM_001106581.2
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 415)
  AUTHORS   Tian,L., Wu,D., Dasgupta,A., Chen,K.H., Mewburn,J., Potus,F.,
            Lima,P.D.A., Hong,Z., Zhao,Y.Y., Hindmarch,C.C.T., Kutty,S.,
            Provencher,S., Bonnet,S., Sutendra,G. and Archer,S.L.
  TITLE     Epigenetic Metabolic Reprogramming of Right Ventricular Fibroblasts
            in Pulmonary Arterial Hypertension: A Pyruvate Dehydrogenase
            Kinase-Dependent Shift in Mitochondrial Metabolism Promotes Right
            Ventricular Fibrosis
  JOURNAL   Circ Res 126 (12), 1723-1745 (2020)
   PUBMED   32216531
  REMARK    GeneRIF: Epigenetic Metabolic Reprogramming of Right Ventricular
            Fibroblasts in Pulmonary Arterial Hypertension: A Pyruvate
            Dehydrogenase Kinase-Dependent Shift in Mitochondrial Metabolism
            Promotes Right Ventricular Fibrosis.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Kluza,J., Corazao-Rozas,P., Touil,Y., Jendoubi,M., Maire,C.,
            Guerreschi,P., Jonneaux,A., Ballot,C., Balayssac,S., Valable,S.,
            Corroyer-Dulmont,A., Bernaudin,M., Malet-Martino,M., de
            Lassalle,E.M., Maboudou,P., Formstecher,P., Polakowska,R.,
            Mortier,L. and Marchetti,P.
  TITLE     Inactivation of the HIF-1alpha/PDK3 signaling axis drives melanoma
            toward mitochondrial oxidative metabolism and potentiates the
            therapeutic activity of pro-oxidants
  JOURNAL   Cancer Res 72 (19), 5035-5047 (2012)
   PUBMED   22865452
REFERENCE   3  (residues 1 to 415)
  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
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Blouin,J.M., Penot,G., Collinet,M., Nacfer,M., Forest,C.,
            Laurent-Puig,P., Coumoul,X., Barouki,R., Benelli,C. and Bortoli,S.
  TITLE     Butyrate elicits a metabolic switch in human colon cancer cells by
            targeting the pyruvate dehydrogenase complex
  JOURNAL   Int J Cancer 128 (11), 2591-2601 (2011)
   PUBMED   20715114
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Lu,C.W., Lin,S.C., Chen,K.F., Lai,Y.Y. and Tsai,S.J.
  TITLE     Induction of pyruvate dehydrogenase kinase-3 by hypoxia-inducible
            factor-1 promotes metabolic switch and drug resistance
  JOURNAL   J Biol Chem 283 (42), 28106-28114 (2008)
   PUBMED   18718909
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Patel,M.S. and Korotchkina,L.G.
  TITLE     Regulation of mammalian pyruvate dehydrogenase complex by
            phosphorylation: complexity of multiple phosphorylation sites and
            kinases
  JOURNAL   Exp Mol Med 33 (4), 191-197 (2001)
   PUBMED   11795479
  REMARK    Review article
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Korotchkina,L.G. and Patel,M.S.
  TITLE     Site specificity of four pyruvate dehydrogenase kinase isoenzymes
            toward the three phosphorylation sites of human pyruvate
            dehydrogenase
  JOURNAL   J Biol Chem 276 (40), 37223-37229 (2001)
   PUBMED   11486000
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Kolobova,E., Tuganova,A., Boulatnikov,I. and Popov,K.M.
  TITLE     Regulation of pyruvate dehydrogenase activity through
            phosphorylation at multiple sites
  JOURNAL   Biochem J 358 (Pt 1), 69-77 (2001)
   PUBMED   11485553
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Baker,J.C., Yan,X., Peng,T., Kasten,S. and Roche,T.E.
  TITLE     Marked differences between two isoforms of human pyruvate
            dehydrogenase kinase
  JOURNAL   J Biol Chem 275 (21), 15773-15781 (2000)
   PUBMED   10748134
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On or before Jun 3, 2021 this sequence version replaced
            XP_038955496.1, XP_216091.3, XP_001056460.1.
            
            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 :: BC169078.1, SRR26643289.44861.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##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..415
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..415
                     /product="pyruvate dehydrogenase kinase, isozyme 3"
                     /EC_number="2.7.11.2"
                     /note="pyruvate dehydrogenase kinase, isoenzyme 3;
                     [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3,
                     mitochondrial"
                     /calculated_mol_wt=47813
     Region          26..188
                     /region_name="BCDHK_Adom3"
                     /note="Mitochondrial branched-chain alpha-ketoacid
                     dehydrogenase kinase; pfam10436"
                     /db_xref="CDD:463093"
     Region          192..359
                     /region_name="HATPase_PDK-like"
                     /note="Histidine kinase-like ATPase domain of pyruvate
                     dehydrogenase kinase, branched-chain alpha-ketoacid
                     dehydrogenase kinase and related domains; cd16929"
                     /db_xref="CDD:340406"
     Site            order(221,273,275,277..280,282..284,288,293..295,344,
                     346..350,353,357)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340406"
     Site            order(247,251..252,254..255,285,287,289,291..292,300,
                     322..329,345,347,351..352,354)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340406"
     Site            order(301,328)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340406"
     CDS             1..415
                     /gene="Pdk3"
                     /coded_by="NM_001106581.2:194..1441"
                     /db_xref="GeneID:296849"
                     /db_xref="RGD:1593276"
ORIGIN      
        1 mrlfyrllkq pvpkqierys rfspsplsik qfldfgrdna cektsymflr kelpvrlant
       61 mrevnllpdn llnrpsvglv qswymqsfle lleyenkspe dprvldnflh vlinirnrhn
      121 dvvptmaqgv ieykekfgfd pfissniqyf ldrfytnris frmlinqhtl lfggdtnpah
      181 pkhigsidpt cnvadvvkda yetakmlceq yylvapelev eefnakapnk piqvvyvpsh
      241 lfhmlfelfk nsmratvely edkkegypav ktlvtlgked lsikisdlgg gvplrkidrl
      301 fnymystapr psleptraap lagfgyglpi srlyaryfqg dlklysmegv gtdaviylka
      361 lssesferlp vfnksawrhy kttpeaddws npsseprdas kykakqdkik snktf
//
