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 16-JUN-2009, entry version 69. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX MEDLINE=94032478; 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 RT expression of the corresponding mRNA with that of the somatic E1 alpha RT subunit."; RL Biochim. Biophys. Acta 1216:149-153(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Testis; RX MEDLINE=99004058; 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 RT and 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains CC multiple copies of three enzymatic components: pyruvate CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and CC lipoamide dehydrogenase (E3). CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate. CC -!- ENZYME REGULATION: E1 activity is regulated by phosphorylation CC (inactivation) and dephosphorylation (activation) of the alpha CC subunit. CC -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. CC -!- SUBCELLULAR LOCATION: Mitochondrion (Probable). CC -!- TISSUE SPECIFICITY: Testis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z18878; CAA79318.1; -; mRNA. DR EMBL; U44125; AAB68458.1; -; mRNA. DR EMBL; BC078757; AAH78757.1; -; mRNA. DR IPI; IPI00193263; -. DR PIR; S31416; S31416. DR RefSeq; NP_446446.1; -. DR UniGene; Rn.11126; -. DR HSSP; P08559; 1NI4. DR SMR; Q06437; 31-391. DR Ensembl; ENSRNOG00000016223; Rattus norvegicus. DR GeneID; 117098; -. DR KEGG; rno:117098; -. DR NMPDR; fig|10116.3.peg.17098; -. DR RGD; 620095; Pdha2. DR HOVERGEN; Q06437; -. DR OMA; Q06437; NDATCDI. DR BRENDA; 1.2.4.1; 248. DR NextBio; 619976; -. DR ArrayExpress; Q06437; -. DR GermOnline; ENSRNOG00000016223; Rattus norvegicus. 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...; IDA:RGD. DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:RGD. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y. DR Pfam; PF00676; E1_dh; 1. DR TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1. PE 2: Evidence at transcript level; KW Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; KW Thiamine pyrophosphate; Transit peptide. FT TRANSIT 1 30 Mitochondrion (By similarity). FT CHAIN 31 391 Pyruvate dehydrogenase E1 component FT subunit alpha, testis-specific form, FT mitochondrial. FT /FTId=PRO_0000020449. FT MOD_RES 290 290 Phosphotyrosine (By similarity). FT MOD_RES 294 294 Phosphoserine (By similarity). FT MOD_RES 301 301 Phosphoserine (By similarity). FT MOD_RES 302 302 Phosphotyrosine (By similarity). 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 //