Reviewed, UniProtKB/Swiss-Prot Q06437 (ODPAT_RAT)

Names and origin

Protein names

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

Gene names

Name:

Pdha2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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 + CO(2).
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	MitochondrionProbable.
Tissue specificity	Testis.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
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 – 30	30	Mitochondrion By similarity
	Chain	31 – 391	361	Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial		PRO_0000020449
Amino acid modifications
	Modified residue	290	1	Phosphotyrosine By similarity
	Modified residue	294	1	Phosphoserine By similarity
	Modified residue	301	1	Phosphoserine By similarity
	Modified residue	302	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q06437-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 5BF049BEE483EF5D	FASTA	391	43,393
	10 20 30 40 50 60 MRKMLATVLS QVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYLLEQG PPTSTVLTRE 70 80 90 100 110 120 EALKYYRNMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA CNVGLEAGIN PTDHIITSYR 130 140 150 160 170 180 AHGLCYTRGL SVKSILAELT GRKGGCAKGK GGSMHMYAKN FYGGNGIVGA QVPLGAGVAL 190 200 210 220 230 240 ACKYLKNGQI CLALYGDGAA NQGQVFEAYN MSALWKLPCV FICENNRYGM GTAIERSAAS 250 260 270 280 290 300 TDYHKKGFVI PGLRVNGMDI LSVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI 310 320 330 340 350 360 SYRTREEVQN VRSKSDPIML LRERMISNNL SSVEELKEID ADVKKEVEEA AQFATTDPEP 370 380 390 PLEDLANYLY HQNPPFEVRG AHKWLKFKSV S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of cDNAs encoding the rat testis-specific E1 alpha subunit of the pyruvate dehydrogenase complex: comparison of expression of the corresponding mRNA with that of the somatic E1 alpha subunit." Cullingford T.E., Clark J.B., Phillips I.R. Biochim. Biophys. Acta 1216:149-153(1993) [PubMed: 7916643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"Pyruvate dehydrogenase E1 alpha isoform in rat testis: cDNA cloning, characterization, and biochemical comparison of the recombinant testis and liver enzymes." Jeng J., Kallarakal A.T., Kim S.F., Popov K.M., Song B.J. Comp. Biochem. Physiol. 120B:205-216(1998) [PubMed: 9787790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Testis.
[3]	"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]. Tissue: Testis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z18878 mRNA. Translation: CAA79318.1. U44125 mRNA. Translation: AAB68458.1. BC078757 mRNA. Translation: AAH78757.1.
PIR	S31416.
RefSeq	NP_446446.1.
UniGene	Rn.11126
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
SMR	Q06437. Positions 31-391.
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000016223. Rattus norvegicus. [Contig view]
GeneID	117098.
KEGG	rno:117098.
NMPDR	fig|10116.3.peg.17098.
Organism-specific databases
RGD	620095. Pdha2.
Phylogenomic databases
HOVERGEN	Q06437.
Gene expression databases
ArrayExpress	Q06437.
GermOnline	ENSRNOG00000016223. Rattus norvegicus.
Family and domain databases
InterPro	IPR001017. DHase_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	619976.

Entry information

Entry name

ODPAT_RAT

Accession

Primary (citable) accession number: Q06437

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 25, 2008
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)