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UniProtKB/Swiss-Prot entry P35487


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPAT_MOUSE
Primary accession number P35487
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on June 1, 1994 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 66)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial [Precursor]
Synonyms EC 1.2.4.1
PDHE1-A type II
Gene name
Name: Pdha2
Synonyms: Pdha-2, Pdhal
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0167-4781(92)90102-6; PubMed=1581363 [NCBI, ExPASy, EBI, Israel, Japan]
Fitzgerald G.F., Hutchison W.M., Dahl H.H.M.;
"Isolation and characterisation of the mouse pyruvate dehydrogenase E1 alpha genes.";
Biochim. Biophys. Acta 1131:83-90(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Testis;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
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 + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • ENZYME REGULATION: E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
  • SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
  • SUBCELLULAR LOCATION: Mitochondrion (Probable).
  • TISSUE SPECIFICITY: Testis.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M76728; AAA53047.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK076791; BAC36482.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S23507; S23507.
RefSeq NP_032837.1; -.
UniGene Mm.4223
3D structure databases
HSSP P08559; 1NI4. [HSSP ENTRY / PDB]
SMR P35487; 31-391.
ModBase P35487.
PTM databases
PhosphoSite P35487; -.
2D gel databases
REPRODUCTION-2DPAGE P35487; -.
Organism-specific databases
MGI MGI:97533; Pdha2.
Gene expression databases
ArrayExpress P35487; -.
CleanEx MM_PDHA2; -.
GermOnline ENSMUSG00000047674; Mus musculus.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS P35487.
Genome annotation databases
Ensembl ENSMUSG00000047674; Mus musculus. [Contig view]
GeneID 18598; -.
KEGG mmu:18598; -.
Phylogenomic databases
HOGENOM P35487; -.
HOVERGEN P35487; -.
Other
SOURCE Pdha2; Mus musculus.
ProtoNet P35487.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    30  30     Mitochondrion (By similarity). 
CHAIN   31   391  361     Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial. PRO_0000020448
MOD_RES   233   233        Phosphoserine (By similarity). 
MOD_RES   294   294        Phosphoserine (By similarity). 
MOD_RES   301   301        Phosphoserine (By similarity). 
Sequence information
Length: 391 AA [This is the length of the unprocessed precursor] Molecular weight: 43413 Da [This is the MW of the unprocessed precursor] CRC64: A2DE823362485977 [This is a checksum on the sequence]
        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 

P35487 in FASTA format

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