LOCUS       NP_446446                391 aa            linear   ROD 02-JUN-2024
DEFINITION  pyruvate dehydrogenase E1 component subunit alpha, testis-specific
            form, mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_446446 XP_346644
VERSION     NP_446446.1
DBSOURCE    REFSEQ: accession NM_053994.2
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 391)
  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   2  (residues 1 to 391)
  AUTHORS   Korotchkina,L.G., Sidhu,S. and Patel,M.S.
  TITLE     Characterization of testis-specific isoenzyme of human pyruvate
            dehydrogenase
  JOURNAL   J Biol Chem 281 (14), 9688-9696 (2006)
   PUBMED   16436377
REFERENCE   3  (residues 1 to 391)
  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   4  (residues 1 to 391)
  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   5  (residues 1 to 391)
  AUTHORS   Cullingford,T.E., Clark,J.B. and Phillips,I.R.
  TITLE     Characterization of cDNAs encoding the rat testis-specific E1 alpha
            subunit of the pyruvate dehydrogenase complex: comparison of
            expression of the corresponding mRNA with that of the somatic E1
            alpha subunit
  JOURNAL   Biochim Biophys Acta 1216 (1), 149-153 (1993)
   PUBMED   7916643
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Fitzgerald,J., Hutchison,W.M. and Dahl,H.H.
  TITLE     Isolation and characterisation of the mouse pyruvate dehydrogenase
            E1 alpha genes
  JOURNAL   Biochim Biophys Acta 1131 (1), 83-90 (1992)
   PUBMED   1581363
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078757.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346644.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC078757.1 [ECO:0000345]
            ##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..391
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q44"
     Protein         1..391
                     /product="pyruvate dehydrogenase E1 component subunit
                     alpha, testis-specific form, mitochondrial precursor"
                     /EC_number="1.2.4.1"
                     /note="pyruvate dehydrogenase E1 component subunit alpha,
                     testis-specific form, mitochondrial; PDHE1-A type II;
                     pyruvate dehydrogenase (lipoamide) alpha 2; pyruvate
                     dehydrogenase alpha 2; pyruvate dehydrogenase E1 alpha 2
                     subunit"
                     /calculated_mol_wt=40120
     transit_peptide 1..30
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q06437.1)"
                     /calculated_mol_wt=3291
     mat_peptide     31..391
                     /product="Pyruvate dehydrogenase E1 component subunit
                     alpha, testis-specific form, mitochondrial.
                     /id=PRO_0000020449"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06437.1)"
                     /calculated_mol_wt=40120
     Region          59..371
                     /region_name="PDH_E1_alph_y"
                     /note="pyruvate dehydrogenase E1 component, alpha subunit;
                     TIGR03182"
                     /db_xref="CDD:274473"
     Site            order(89,141,166..167,198,200..203,206,210,214,229..232,
                     246,249,297,301)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238958"
     Site            order(119..120,166,168,196..199,226,228,293)
                     /site_type="other"
                     /note="TPP-binding site [chemical binding]"
                     /db_xref="CDD:238958"
     Site            order(161,163,165,170,173..174,177..178,180..181,184,
                     203..204,210..211,214)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:238958"
     Site            order(288..294,296..306,315..317)
                     /site_type="phosphorylation"
                     /note="phosphorylation loop region [posttranslational
                     modification]"
                     /db_xref="CDD:238958"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q06437.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29803; propagated from
                     UniProtKB/Swiss-Prot (Q06437.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDK3.
                     /evidence=ECO:0000250|UniProtKB:P29803; propagated from
                     UniProtKB/Swiss-Prot (Q06437.1)"
     CDS             1..391
                     /gene="Pdha2"
                     /gene_synonym="Pdhal"
                     /coded_by="NM_053994.2:41..1216"
                     /db_xref="GeneID:117098"
                     /db_xref="RGD:620095"
ORIGIN      
        1 mrkmlatvls qvfsgmvqkp alrgllsslk fsndatcdik kcdlylleqg pptstvltre
       61 ealkyyrnmq virrmelkad qlykqkfirg fchlcdgqea cnvgleagin ptdhiitsyr
      121 ahglcytrgl svksilaelt grkggcakgk ggsmhmyakn fyggngivga qvplgagval
      181 ackylkngqi clalygdgaa nqgqvfeayn msalwklpcv ficennrygm gtaiersaas
      241 tdyhkkgfvi pglrvngmdi lsvreatkfa adhcrsgkgp ivmelqtyry hghsmsdpgi
      301 syrtreevqn vrsksdpiml lrermisnnl ssveelkeid advkkeveea aqfattdpep
      361 pledlanyly hqnppfevrg ahkwlkfksv s
//
