Reviewed, UniProtKB/Swiss-Prot Q9D2G2 (ODO2_MOUSE)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
    EC=2.3.1.61
Alternative name(s):
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
      Short name=E2
    E2K

Gene names

Name:

Dlst

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Lipoyl Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9D2G2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9D2G2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-253: Missing.
     254-257: EVDM → MTSL

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 68	68	Mitochondrion By similarity
	Chain	69 – 454	386	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		PRO_0000020473
Regions
	Domain	72 – 144	73	Lipoyl-binding
Sites
	Active site	425	1	Potential
	Active site	429	1	Potential
Amino acid modifications
	Modified residue	111	1	N6-lipoyllysine Potential
Natural variations
	Alternative sequence	1 – 253	253	Missing in isoform 2.		VSP_025015
	Alternative sequence	254 – 257	4	EVDM → MTSL in isoform 2.		VSP_025016
Experimental info
	Sequence conflict	276	1	N → S in BAE29011. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9CB31698D185442A	FASTA	454	48,995
	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
	Isoform 2. Checksum: D999AAE99C49D3D8	FASTA	201	22,230
	10 20 30 40 50 60 MTSLSNIQEM RARHKDAFLK KHNLKLGFMS AFVKASAFAL QEQPVVNAVI DDATKEVVYR 70 80 90 100 110 120 DYIDISVAVA TPRGLVVPVI RNVETMNYAD IERTINELGE KARKNELAIE DMDGGTFTIS 130 140 150 160 170 180 NGGVFGSLFG TPIINPPQSA ILGMHAIFDR PVAVGGKVEV RPMMYVALTY DHRLIDGREA 190 200 VTFLRKIKAA VEDPRVLLLD L

References

	« Hide 'large scale' referencesShow '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. , 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] (ISOFORM 1). Strain: C57BL/6J and NOD. Tissue: Bone marrow, Heart, Oviduct, Testis and Visual cortex.
[2]	"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)." Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: Czech II and FVB/N. Tissue: Mammary tumor.
[4]	Lubec G., Klug S., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 69-89; 288-308; 314-334 AND 355-346, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK019713 mRNA. Translation: BAB31840.1. AK054053 mRNA. Translation: BAC35637.1. AK149664 mRNA. Translation: BAE29011.1. AK158877 mRNA. Translation: BAE34709.1. AK168570 mRNA. Translation: BAE40440.1. AK169943 mRNA. Translation: BAE41472.1. CT010197 mRNA. Translation: CAJ18405.1. BC006702 mRNA. Translation: AAH06702.1. BC024066 mRNA. Translation: AAH24066.1.
IPI	IPI00134809. IPI00845858.
RefSeq	NP_084501.1.
UniGene	Mm.296221
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ModBase	Search...
2-D gel databases
REPRODUCTION-2DPAGE	Q9D2G2.
Proteomic databases
PRIDE	Q9D2G2.
Genome annotation databases
Ensembl	ENSMUSG00000004789. Mus musculus. [Contig view]
GeneID	78920.
KEGG	mmu:78920.
Organism-specific databases
MGI	MGI:1926170. Dlst.
Phylogenomic databases
HOGENOM	Q9D2G2.
HOVERGEN	Q9D2G2.
OMA	Q9D2G2. SMNYADI.
Enzyme and pathway databases
BRENDA	2.3.1.61. 244.
Gene expression databases
ArrayExpress	Q9D2G2.
Bgee	Q9D2G2.
GermOnline	ENSMUSG00000004789. Mus musculus.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR006255. SucB. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	349758.
SOURCE	Search...

Entry information

Entry name

ODO2_MOUSE

Accession

Primary (citable) accession number: Q9D2G2
Secondary accession number(s): Q3UEA0, Q4FK55, Q8CIE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)