ID   ODPAT_MOUSE             Reviewed;         391 AA.
AC   P35487;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-NOV-2008, entry version 68.
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; Synonyms=Pdha-2, Pdhal;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92256495; PubMed=1581363; DOI=10.1016/0167-4781(92)90102-6;
RA   Fitzgerald G.F., Hutchison W.M., Dahl H.H.M.;
RT   "Isolation and characterisation of the mouse pyruvate dehydrogenase E1
RT   alpha genes.";
RL   Biochim. Biophys. Acta 1131:83-90(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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.
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DR   EMBL; M76728; AAA53047.1; -; mRNA.
DR   EMBL; AK076791; BAC36482.1; -; mRNA.
DR   PIR; S23507; S23507.
DR   RefSeq; NP_032837.1; -.
DR   UniGene; Mm.4223; -.
DR   HSSP; P08559; 1NI4.
DR   SMR; P35487; 31-391.
DR   PhosphoSite; P35487; -.
DR   REPRODUCTION-2DPAGE; P35487; -.
DR   Ensembl; ENSMUSG00000047674; Mus musculus.
DR   GeneID; 18598; -.
DR   KEGG; mmu:18598; -.
DR   MGI; MGI:97533; Pdha2.
DR   HOGENOM; P35487; -.
DR   HOVERGEN; P35487; -.
DR   NextBio; 294494; -.
DR   ArrayExpress; P35487; -.
DR   CleanEx; MM_PDHA2; -.
DR   GermOnline; ENSMUSG00000047674; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DHase_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 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_0000020448.
FT   MOD_RES     233    233       Phosphoserine (By similarity).
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;  43413 MW;  A2DE823362485977 CRC64;
     MRKMLTAVLS HVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYRLEEG PPTSTVLTRA
     EALKYYRTMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA CCVGLEAGIN PTDHVITSYR
     AHGFCYTRGL SVKSILAELT GRKGGCAKGK GGSMHMYGKN FYGGNGIVGA QVPLGAGVAF
     ACKYLKNGQV CLALYGDGAA NQGQVFEAYN MSALWKLPCV FICENNLYGM GTSNERSAAS
     TDYHKKGFII PGLRVNGMDI LCVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI
     SYRSREEVHN VRSKSDPIML LRERIISNNL SNIEELKEID ADVKKEVEDA AQFATTDPEP
     AVEDIANYLY HQDPPFEVRG AHKWLKYKSH S
//