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P35487 (ODPAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle By similarity.

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate By similarity.

Enzyme regulation

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA2; it is reactivated by dephosphorylation By similarity.

Subunit structure

Heterotetramer of two PDHA2 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Tissue specificity

Testis.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion By similarity
Chain31 – 391361Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
PRO_0000020448

Amino acid modifications

Modified residue2941Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residue3011Phosphoserine; by PDK3 By similarity

Sequences

Sequence LengthMass (Da)Tools
P35487 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: A2DE823362485977

FASTA39143,413
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76728 mRNA. Translation: AAA53047.1.
AK076791 mRNA. Translation: BAC36482.1.
BC100460 mRNA. Translation: AAI00461.1.
PIRS23507.
RefSeqNP_032837.1. NM_008811.2.
UniGeneMm.4223.

3D structure databases

ProteinModelPortalP35487.
SMRP35487. Positions 31-391.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP35487.

2D gel databases

REPRODUCTION-2DPAGEP35487.

Proteomic databases

PaxDbP35487.
PRIDEP35487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057860; ENSMUSP00000060774; ENSMUSG00000047674.
GeneID18598.
KEGGmmu:18598.
UCSCuc008rob.1. mouse.

Organism-specific databases

CTD5161.
MGIMGI:97533. Pdha2.

Phylogenomic databases

eggNOGCOG1071.
GeneTreeENSGT00530000063174.
HOGENOMHOG000281336.
HOVERGENHBG001863.
InParanoidQ497M8.
KOK00161.
OMAELTINIY.
OrthoDBEOG73JKVQ.
PhylomeDBP35487.
TreeFamTF300742.

Gene expression databases

BgeeP35487.
CleanExMM_PDHA2.
GenevestigatorP35487.

Family and domain databases

InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Other

NextBio294494.
PROP35487.
SOURCESearch...

Entry information

Entry nameODPAT_MOUSE
AccessionPrimary (citable) accession number: P35487
Secondary accession number(s): Q497M8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot