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UniProtKB/Swiss-Prot entry Q9D2G2


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

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Entry information
Entry name ODO2_MOUSE
Primary accession number Q9D2G2
Secondary accession numbers Q3UEA0 Q4FK55 Q8CIE8
Integrated into Swiss-Prot on April 12, 2005
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 58)
Name and origin of the protein
Protein name Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial [Precursor]
Synonyms EC 2.3.1.61
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
E2
E2K
Gene name
Name: Dlst
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone marrow, Heart, Oviduct, Testis, and Visual cortex;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=Czech II, and FVB/N;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 314-326, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
Comments
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
AK019713; BAB31840.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK054053; BAC35637.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK149664; BAE29011.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK158877; BAE34709.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK168570; BAE40440.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169943; BAE41472.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CT010197; CAJ18405.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006702; AAH06702.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024066; AAH24066.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_084501.1; -.
UniGene Mm.296221
3D structure databases
HSSP P07016; 1C4T. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q9D2G2.
2D gel databases
REPRODUCTION-2DPAGE Q9D2G2; -.
Organism-specific databases
MGI MGI:1926170; Dlst.
Gene expression databases
ArrayExpress Q9D2G2; -.
GermOnline ENSMUSG00000004789; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0031405; Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR000089; Biotin_lipoyl.
IPR006255; SucB.
Graphical view of domain structure.
Pfam PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 1.
Pfam graphical view of domain structure.
ProDom PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01347; sucB; 1.
PROSITE PS50968; BIOTINYL_LIPOYL; 1.
PS00189; LIPOYL; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9D2G2.
ProtoNet Q9D2G2.
Genome annotation databases
Ensembl ENSMUSG00000004789; Mus musculus. [Contig view]
GeneID 78920; -.
KEGG mmu:78920; -.
Phylogenomic databases
HOGENOM Q9D2G2; -.
HOVERGEN Q9D2G2; -.
Other
NextBio 349758; -.
SOURCE Dlst; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Alternative splicing; Direct protein sequencing; Lipoyl; Mitochondrion; Transferase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    68  68     Mitochondrion (By similarity). 
CHAIN   69   454  386     Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial. PRO_0000020473
DOMAIN   72   144  73     Lipoyl-binding. 
ACT_SITE   425   425        Potential. 
ACT_SITE   429   429        Potential. 
BINDING   111   111        Lipoyl (covalent) (Potential). 
VAR_SEQ   1   253        Missing (in isoform 2). VSP_025015
VAR_SEQ   254   257        EVDM -> MTSL (in isoform 2). VSP_025016
CONFLICT   276   276        N -> S (in Ref. 1; BAE29011). 
Sequence information
Length: 454 AA [This is the length of the unprocessed precursor] Molecular weight: 48995 Da [This is the MW of the unprocessed precursor] CRC64: 9CB31698D185442A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCRGP GYPDNRKMVI NSGSVFRVRF 

        70         80         90        100        110        120 
FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE DEVVCEIETD KTSVQVPSPA 

       130        140        150        160        170        180 
NGIIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAETP APAHKAEPAA PAAPPPPAAP 

       190        200        210        220        230        240 
VLTQMPPVPS PSQPPSSKPV SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK 

       250        260        270        280        290        300 
EAQNTCAMLT TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN 

       310        320        330        340        350        360 
AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE LGEKARKNEL 

       370        380        390        400        410        420 
AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHAI FDRPVAVGGK VEVRPMMYVA 

       430        440        450 
LTYDHRLIDG REAVTFLRKI KAAVEDPRVL LLDL 

Q9D2G2 in FASTA format

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