Reviewed, UniProtKB/Swiss-Prot P35487 (ODPAT_MOUSE)

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
Synonyms:	Pdha-2, Pdhal

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	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 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 Probable.
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-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 – 30	30	Mitochondrion By similarity
	Chain	31 – 391	361	Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial		PRO_0000020448
Amino acid modifications
	Modified residue	233	1	Phosphoserine By similarity
	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)
	P35487-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: A2DE823362485977	FASTA	391	43,413
	10 20 30 40 50 60 MRKMLTAVLS HVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYRLEEG PPTSTVLTRA 70 80 90 100 110 120 EALKYYRTMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA CCVGLEAGIN PTDHVITSYR 130 140 150 160 170 180 AHGFCYTRGL SVKSILAELT GRKGGCAKGK GGSMHMYGKN FYGGNGIVGA QVPLGAGVAF 190 200 210 220 230 240 ACKYLKNGQV CLALYGDGAA NQGQVFEAYN MSALWKLPCV FICENNLYGM GTSNERSAAS 250 260 270 280 290 300 TDYHKKGFII PGLRVNGMDI LCVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI 310 320 330 340 350 360 SYRSREEVHN VRSKSDPIML LRERIISNNL SNIEELKEID ADVKKEVEDA AQFATTDPEP 370 380 390 AVEDIANYLY HQDPPFEVRG AHKWLKYKSH S

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 transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M76728 mRNA. Translation: AAA53047.1. AK076791 mRNA. Translation: BAC36482.1.
IPI	IPI00118594.
PIR	S23507.
RefSeq	NP_032837.1.
UniGene	Mm.4223
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
SMR	P35487. Positions 31-391.
ModBase	Search...
PTM databases
PhosphoSite	P35487.
2-D gel databases
REPRODUCTION-2DPAGE	P35487.
Proteomic databases
PRIDE	P35487.
Genome annotation databases
Ensembl	ENSMUSG00000047674. Mus musculus. [Contig view]
GeneID	18598.
KEGG	mmu:18598.
Organism-specific databases
MGI	MGI:97533. Pdha2.
Phylogenomic databases
HOGENOM	P35487.
HOVERGEN	P35487.
OMA	P35487. NDATCDI.
Enzyme and pathway databases
BRENDA	1.2.4.1. 244.
Gene expression databases
ArrayExpress	P35487.
Bgee	P35487.
CleanEx	MM_PDHA2.
GermOnline	ENSMUSG00000047674. 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	294494.
SOURCE	Search...

Entry information

Entry name

ODPAT_MOUSE

Accession

Primary (citable) accession number: P35487

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)