Reviewed, UniProtKB/Swiss-Prot P35486 (ODPA_MOUSE)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
    EC=1.2.4.1
Alternative name(s):
    PDHE1-A type I

Gene names

Name:	Pdha1
Synonyms:	Pdha-1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate.
Enzyme regulation	E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
Subunit structure	Tetramer of 2 alpha and 2 beta subunits.
Subcellular location	Mitochondrion matrix.
Tissue specificity	In all tissues, but in very low amount in testis.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 29	29	Mitochondrion By similarity
	Chain	30 – 390	361	Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial		PRO_0000020442
Amino acid modifications
	Modified residue	77	1	N6-acetyllysine By similarity
	Modified residue	83	1	N6-acetyllysine By similarity
	Modified residue	231	1	Phosphothreonine By similarity
	Modified residue	232	1	Phosphoserine Ref.6 Ref.7
	Modified residue	289	1	Phosphotyrosine Ref.7
	Modified residue	293	1	Phosphoserine Ref.6 Ref.7 Ref.4 Ref.8
	Modified residue	295	1	Phosphoserine By similarity
	Modified residue	300	1	Phosphoserine Ref.6 Ref.7 Ref.8
	Modified residue	301	1	Phosphotyrosine Ref.5
	Modified residue	321	1	N6-acetyllysine By similarity
	Modified residue	336	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35486-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 40898944CE8E0A03	FASTA	390	43,232
	10 20 30 40 50 60 MRKMLAAVSR VLAGSAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 70 80 90 100 110 120 GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 130 140 150 160 170 180 HGFTFTRGLP VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 190 200 210 220 230 240 CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 250 260 270 280 290 300 DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 310 320 330 340 350 360 YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 370 380 390 LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterisation of the mouse pyruvate dehydrogenase E1 alpha genes." Fitzgerald G.F., Hutchison W.M., Dahl H.-H.M. Biochim. Biophys. Acta 1131:83-90(1992) [PubMed: 1581363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[3]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-58; 120-127; 133-141; 159-182; 216-244; 246-263; 268-274; 278-321; 324-343 AND 379-385, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[4]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-293 AND SER-300, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; TYR-289; SER-293 AND SER-300, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-300, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M76727 mRNA. Translation: AAA53046.1. BC007142 mRNA. Translation: AAH07142.1.
IPI	IPI00337893.
PIR	S23506.
RefSeq	NP_032836.1.
UniGene	Mm.34775
3D structure databases
SMR	P35486. Positions 29-390.
ModBase	Search...
Protein-protein interaction databases
STRING	P35486.
PTM databases
PhosphoSite	P35486.
2-D gel databases
REPRODUCTION-2DPAGE	P35486.
Proteomic databases
PRIDE	P35486.
Genome annotation databases
Ensembl	ENSMUST00000033662; ENSMUSP00000033662; ENSMUSG00000031299; Mus musculus. [Genome view]
GeneID	18597.
KEGG	mmu:18597.
UCSC	uc009utc.1. mouse.
Organism-specific databases
CTD	18597.
MGI	MGI:97532. Pdha1.
Phylogenomic databases
eggNOG	roNOG13286.
HOGENOM	HBG753263.
HOVERGEN	P35486.
InParanoid	P35486.
OMA	IVENNRY.
OrthoDB	EOG91VNNQ.
PhylomeDB	P35486.
Enzyme and pathway databases
BRENDA	1.2.4.1. 244.
Gene expression databases
ArrayExpress	P35486.
Bgee	P35486.
CleanEx	MM_PDHA1.
Genevestigator	P35486.
GermOnline	ENSMUSG00000031299. Mus musculus.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	294490.
SOURCE	Search...

Entry information

Entry name

ODPA_MOUSE

Accession

Primary (citable) accession number: P35486

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	February 9, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)