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Reviewed, UniProtKB/Swiss-Prot Q8BMF4 (ODP2_MOUSE)

Last modified February 9, 2010. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) 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

20 to 30 alpha(2)-beta2 tetramers of E1 + 6 homodimers of E3 + 60 copies of E2 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

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
Q8BMF4-1 [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: 16141072] [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: 15489334] [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: 12108679] [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, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+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.
IPIIPI00153660.
RefSeqNP_663589.3.
UniGeneMm.285076
Mm.471144

3D structure databases

HSSPHSSP built from PDB template 1FYC based on UniProtKB P10515.
SMRQ8BMF4. Positions 91-181, 213-314, 347-395, 404-642.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BMF4.

Proteomic databases

PRIDEQ8BMF4.

Genome annotation databases

EnsemblENSMUST00000034567; ENSMUSP00000034567; ENSMUSG00000000168; Mus musculus. [Genome view]
GeneID235339.
KEGGmmu:235339.

Organism-specific databases

CTD235339.
MGIMGI:2385311. Dlat.

Phylogenomic databases

eggNOGroNOG14419.
HOGENOMHBG630916.
HOVERGENQ8BMF4.
InParanoidQ8BMF4.
OMAGKLLCII.
OrthoDBEOG9NCPZ1.
PhylomeDBQ8BMF4.

Enzyme and pathway databases

BRENDA2.3.1.12. 244.

Gene expression databases

ArrayExpressQ8BMF4.
BgeeQ8BMF4.
GenevestigatorQ8BMF4.

Family and domain databases

InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006257. AcTrfase_Pyrv_DH_cplx_L.
IPR000089. Biotin_lipoyl.
IPR004167. E3_bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
Gene3DG3DSA:4.10.320.10. E3_bd. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio382617.
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: February 9, 2010
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents