ID   ODPAT_RAT               Reviewed;         391 AA.
AC   Q06437;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial;
DE            EC=1.2.4.1;
DE   AltName: Full=PDHE1-A type II;
DE   Flags: Precursor;
GN   Name=Pdha2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=7916643; DOI=10.1016/0167-4781(93)90054-h;
RA   Cullingford T.E., Clark J.B., Phillips I.R.;
RT   "Characterization of cDNAs encoding the rat testis-specific E1 alpha
RT   subunit of the pyruvate dehydrogenase complex: comparison of expression of
RT   the corresponding mRNA with that of the somatic E1 alpha subunit.";
RL   Biochim. Biophys. Acta 1216:149-153(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PHOSPHORYLATION,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=9787790; DOI=10.1016/s0305-0491(98)10010-x;
RA   Jeng J., Kallarakal A.T., Kim S.F., Popov K.M., Song B.J.;
RT   "Pyruvate dehydrogenase E1 alpha isoform in rat testis: cDNA cloning,
RT   characterization, and biochemical comparison of the recombinant testis and
RT   liver enzymes.";
RL   Comp. Biochem. Physiol. 120B:205-216(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the
CC       glycolytic pathway to the tricarboxylic cycle.
CC       {ECO:0000269|PubMed:9787790}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC         acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000269|PubMed:9787790};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Pyruvate dehydrogenase activity is inhibited by
CC       phosphorylation of PDHA2; it is reactivated by dephosphorylation.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterotetramer of two PDHA2 and two PDHB subunits. The
CC       heterotetramer interacts with DLAT, and is part of the multimeric
CC       pyruvate dehydrogenase complex that contains multiple copies of
CC       pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT,
CC       E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to
CC       an inner core composed of about 48 DLAT and 12 PDHX molecules (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:9787790}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z18878; CAA79318.1; -; mRNA.
DR   EMBL; U44125; AAB68458.1; -; mRNA.
DR   EMBL; BC078757; AAH78757.1; -; mRNA.
DR   PIR; S31416; S31416.
DR   RefSeq; NP_446446.1; NM_053994.2.
DR   AlphaFoldDB; Q06437; -.
DR   SMR; Q06437; -.
DR   iPTMnet; Q06437; -.
DR   PhosphoSitePlus; Q06437; -.
DR   PRIDE; Q06437; -.
DR   GeneID; 117098; -.
DR   KEGG; rno:117098; -.
DR   CTD; 5161; -.
DR   RGD; 620095; Pdha2.
DR   HOGENOM; CLU_029393_5_2_1; -.
DR   InParanoid; Q06437; -.
DR   OMA; FGMPGVT; -.
DR   OrthoDB; 871160at2759; -.
DR   PhylomeDB; Q06437; -.
DR   Reactome; R-RNO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR   Reactome; R-RNO-70268; Pyruvate metabolism.
DR   SABIO-RK; Q06437; -.
DR   PRO; PR:Q06437; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000016223; Expressed in testis.
DR   Genevisible; Q06437; RN.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:RGD.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IDA:RGD.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:RGD.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glucose metabolism; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Reference proteome; Thiamine pyrophosphate;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..391
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha,
FT                   testis-specific form, mitochondrial"
FT                   /id="PRO_0000020449"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29803"
FT   MOD_RES         301
FT                   /note="Phosphoserine; by PDK3"
FT                   /evidence="ECO:0000250|UniProtKB:P29803"
SQ   SEQUENCE   391 AA;  43393 MW;  5BF049BEE483EF5D CRC64;
     MRKMLATVLS QVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYLLEQG PPTSTVLTRE
     EALKYYRNMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA CNVGLEAGIN PTDHIITSYR
     AHGLCYTRGL SVKSILAELT GRKGGCAKGK GGSMHMYAKN FYGGNGIVGA QVPLGAGVAL
     ACKYLKNGQI CLALYGDGAA NQGQVFEAYN MSALWKLPCV FICENNRYGM GTAIERSAAS
     TDYHKKGFVI PGLRVNGMDI LSVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI
     SYRTREEVQN VRSKSDPIML LRERMISNNL SSVEELKEID ADVKKEVEEA AQFATTDPEP
     PLEDLANYLY HQNPPFEVRG AHKWLKFKSV S