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Q8BMF4 (ODP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name=PDC-E2
Short name=PDCE2
Gene names
Name:Dlat
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Subunit structure

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. Interacts with PDK2 and PDK3 By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 2 lipoyl-binding domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8585Mitochondrion By similarity
Chain86 – 642557Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
PRO_0000285717

Regions

Domain91 – 16575Lipoyl-binding 1
Domain218 – 29275Lipoyl-binding 2
Region353 – 38432E3- and/or E1-component binding domain Potential
Region466 – 642177Catalytic By similarity
Region610 – 62112CoA-binding By similarity

Sites

Active site6151 Potential
Active site6191 Potential

Amino acid modifications

Modified residue2581N6-lipoyllysine By similarity
Modified residue4611N6-acetyllysine By similarity
Modified residue4681N6-succinyllysine Ref.6
Modified residue5421N6-succinyllysine Ref.6

Experimental info

Sequence conflict841S → Y in AAL02400. Ref.3
Sequence conflict1981P → T in BAC27715. Ref.1
Sequence conflict2251L → P in AAL02400. Ref.3
Sequence conflict3931A → V in AAH31495. Ref.2
Sequence conflict6041A → V in AAH31495. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BMF4 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 1294FAC4857FC29C

FASTA64267,942
        10         20         30         40         50         60 
MWRVCARRAR SAVPRDGFRA RWAALKEGPG APCGSPRIGP AAVRCGSGIP RYGVRSLCGW 

        70         80         90        100        110        120 
SSGSGTVPRN RLLRQLLGSP SRRSYSLPPH QKVPLPSLSP TMQAGTIARW EKKEGEKISE 

       130        140        150        160        170        180 
GDLIAEVETD KATVGFESLE ECYMAKILVP EGTRDVPVGS IICITVEKPQ DIEAFKNYTL 

       190        200        210        220        230        240 
DLAAAAAPQA APAAAPAPAA APAAPSASAP GSSYPTHMQI VLPALSPTMT MGTVQRWEKK 

       250        260        270        280        290        300 
VGEKLSEGDL LAEIETDKAT IGFEVQEEGY LAKILVPEGT RDVPLGAPLC IIVEKQEDIA 

       310        320        330        340        350        360 
AFADYRPTEV TSLKPQAAPP APPPVAAVPP TPQPVAPTPS AAPAGPKGRV FVSPLAKKLA 

       370        380        390        400        410        420 
AEKGIDLTQV KGTGPEGRII KKDIDSFVPS KAAPAAAAAM APPGPRVAPA PAGVFTDIPI 

       430        440        450        460        470        480 
SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG EVLLVRKELN KMLEGKGKIS VNDFIIKASA 

       490        500        510        520        530        540 
LACLKVPEAN SSWMDTVIRQ NHVVDVSVAV STPAGLITPI VFNAHIKGLE TIASDVVSLA 

       550        560        570        580        590        600 
SKAREGKLQP HEFQGGTFTI SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG 

       610        620        630        640 
FDVASVMSVT LSCDHRVVDG AVGAQWLAEF KKYLEKPITM LL 

« Hide

References

« Hide 'large scale' references
[1]"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: Medulla oblongata.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II, FVB/N-3 and NMRI.
Tissue: Mammary tumor.
[3]"Molecular cloning, and characterization and expression of dihydrolipoamide acetyltransferase component of murine pyruvate dehydrogenase complex in bile duct cancer cells."
Wang L., Kaneko S., Kagaya M., Ohno H., Honda M., Kobayashi K.
J. Gastroenterol. 37:449-454(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 84-642.
Tissue: Hepatoma.
[4]Lubec G., Klug S., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 93-109; 147-176; 282-295; 383-424; 469-477; 486-499; 528-542; 548-569; 600-631 AND 633-642, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-468 AND LYS-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK032124 mRNA. Translation: BAC27715.1.
BC026680 mRNA. Translation: AAH26680.1.
BC031495 mRNA. Translation: AAH31495.1.
BC069862 mRNA. Translation: AAH69862.1.
AY044265 mRNA. Translation: AAL02400.1.
RefSeqNP_663589.3. NM_145614.4.
UniGeneMm.285076.
Mm.471144.

3D structure databases

ProteinModelPortalQ8BMF4.
SMRQ8BMF4. Positions 91-181, 217-294, 349-388, 404-642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231646. 2 interactions.
IntActQ8BMF4. 7 interactions.
MINTMINT-135876.

PTM databases

PhosphoSiteQ8BMF4.

2D gel databases

REPRODUCTION-2DPAGEIPI00153660.
UCD-2DPAGEQ8BMF4.

Proteomic databases

PaxDbQ8BMF4.
PRIDEQ8BMF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034567; ENSMUSP00000034567; ENSMUSG00000000168.
GeneID235339.
KEGGmmu:235339.
UCSCuc009pka.2. mouse.

Organism-specific databases

CTD1737.
MGIMGI:2385311. Dlat.

Phylogenomic databases

eggNOGCOG0508.
GeneTreeENSGT00740000115255.
HOGENOMHOG000281566.
HOVERGENHBG005063.
InParanoidQ8BMF4.
KOK00627.
OMAATMEFES.
OrthoDBEOG7K3TKW.
PhylomeDBQ8BMF4.
TreeFamTF106145.

Gene expression databases

BgeeQ8BMF4.
GenevestigatorQ8BMF4.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDLAT. mouse.
NextBio382617.
PROQ8BMF4.
SOURCESearch...

Entry information

Entry nameODP2_MOUSE
AccessionPrimary (citable) accession number: Q8BMF4
Secondary accession number(s): Q8K2G8, Q8R339, Q91ZB1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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