ID   ODPA_RAT                Reviewed;         390 AA.
AC   P26284;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   04-NOV-2008, entry version 70.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial;
DE            EC=1.2.4.1;
DE   AltName: Full=PDHE1-A type I;
DE   Flags: Precursor;
GN   Name=Pdha1;
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].
RX   MEDLINE=91223087; PubMed=2025639; DOI=10.1016/0167-4781(91)90076-X;
RA   Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T.;
RT   "The alpha-ketoacid dehydrogenase complexes. Sequence similarity of
RT   rat pyruvate dehydrogenase with Escherichia coli and Azotobacter
RT   vinelandii alpha-ketoglutarate dehydrogenase.";
RL   Biochim. Biophys. Acta 1089:1-7(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   MEDLINE=94209873; PubMed=8158120;
RA   Cullingford T.E., Clark J.B., Phillips I.R.;
RT   "The pyruvate dehydrogenase complex: cloning of the rat somatic E1
RT   alpha subunit and its coordinate expression with the mRNAs for the E1
RT   beta, E2, and E3 catalytic subunits in developing rat brain.";
RL   J. Neurochem. 62:1682-1690(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 133-141; 216-226; 245-253; 289-302 AND 324-343,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Diao W., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-295; SER-300
RP   AND TYR-301, AND MASS SPECTROMETRY.
RC   TISSUE=Kidney;
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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 matrix.
CC   -!- TISSUE SPECIFICITY: In all tissues, but in very low amount in
CC       testis.
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DR   EMBL; Z12158; CAA78146.1; -; mRNA.
DR   PIR; S15891; DERTPA.
DR   PIR; S21553; DERTP1.
DR   UniGene; Rn.3655; -.
DR   HSSP; P08559; 1NI4.
DR   SMR; P26284; 29-390.
DR   PhosphoSite; P26284; -.
DR   Ensembl; ENSRNOG00000025383; Rattus norvegicus.
DR   RGD; 3286; Pdha1.
DR   HOVERGEN; P26284; -.
DR   ArrayExpress; P26284; -.
DR   GermOnline; ENSRNOG00000025383; Rattus norvegicus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     29       Mitochondrion (By similarity).
FT   CHAIN        30    390       Pyruvate dehydrogenase E1 component
FT                                subunit alpha, somatic form,
FT                                mitochondrial.
FT                                /FTId=PRO_0000020445.
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     289    289       Phosphotyrosine (By similarity).
FT   MOD_RES     293    293       Phosphoserine.
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     300    300       Phosphoserine.
FT   MOD_RES     301    301       Phosphotyrosine.
FT   CONFLICT     10     10       R -> H (in Ref. 2; CAA78146).
FT   CONFLICT    126    126       N -> T (in Ref. 2; CAA78146).
FT   CONFLICT    129    130       HA -> LP (in Ref. 2; CAA78146).
FT   CONFLICT    134    134       I -> V (in Ref. 1).
SQ   SEQUENCE   390 AA;  43227 MW;  254B5A801E750DC0 CRC64;
     MRKMLAAVSR VLAGAAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED
     GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA
     HGFTFNRGHA VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA
     CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST
     DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS
     YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP
     LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
//