Reviewed, UniProtKB/Swiss-Prot Q921G7 (ETFD_MOUSE)

Names and origin

Protein names

Recommended name:
    Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
      Short name=ETF-ubiquinone oxidoreductase
      Short name=ETF-QO
    EC=1.5.5.1
Alternative name(s):
    Electron-transferring-flavoprotein dehydrogenase
      Short name=ETF dehydrogenase

Gene names

Name:

Etfdh

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	616 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	Accepts electrons from ETF and reduces ubiquinone By similarity.
Catalytic activity	Reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol.
Cofactor	Binds 1 4Fe-4S cluster By similarity. FAD By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion inner membrane By similarity.
Post-translational modification	Acetylation of Lys-95 and Lys-222 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the ETF-QO/fixC family. Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane
Ligand	4Fe-4S FAD Flavoprotein Iron Iron-sulfur Metal-binding Ubiquinone
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial electron transfer flavoprotein complex Traceable author statement. Source: MGI mitochondrial inner membrane Inferred from direct assay. Source: MGI
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron-transferring-flavoprotein dehydrogenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 32	32	Mitochondrion Potential
	Chain	33 – 616	584	Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial		PRO_0000008662
Regions
	Transmembrane	457 – 477	21	Potential
	Domain	576 – 605	30	4Fe-4S ferredoxin-type
	Nucleotide binding	70 – 84	15	FAD Potential
Sites
	Metal binding	560	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	585	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	588	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	591	1	Iron-sulfur (4Fe-4S) Potential
Amino acid modifications
	Modified residue	95	1	N6-acetyllysine Ref.4
	Modified residue	152	1	N6-acetyllysine Ref.4
	Modified residue	222	1	N6-acetyllysine Ref.4
	Modified residue	343	1	N6-acetyllysine Ref.4
Experimental info
	Sequence conflict	342	1	W → C in BAB22135. Ref.1
	Sequence conflict	355	1	G → W in BAC35888. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q921G7-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 1E5C6F85725E3CEE	FASTA	616	68,091
	10 20 30 40 50 60 MLVRLTKLSC PAYHWFHALK IKKCLPLCAP RCSSTSAVPQ ITTHYTVHPR EKDKRWEGVN 70 80 90 100 110 120 MERFAEEADV VIVGAGPAGL SAAIRLKQLA AEQGKDIRVC LVEKAAQIGA HTLSGACLDP 130 140 150 160 170 180 AAFKELFPDW KEKGAPLNTP VTEDRFAILT EKHRIPVPIL PGLPMNNHGN YIVRLGHLVS 190 200 210 220 230 240 WMGEQAEALG VEVYPGYAAA EVLYHEDGSV KGIATNDVGI QKDGAPKTTF ERGLELHAKV 250 260 270 280 290 300 TVFAEGCHGH LAKQLYKKFD LRASCDAQTY GIGLKELWII DEKKWKPGRV DHTVGWPLDR 310 320 330 340 350 360 HTYGGSFLYH LNEGEPLVAV GFVVGLDYQN PYLSPFREFQ RWKHHPSIQP TLEGGKRIAY 370 380 390 400 410 420 GARALNEGGL QSIPKLTFPG GLLIGCSPGF MNVPKIKGTH TAMKSGSLAA ESIFKQLTSE 430 440 450 460 470 480 NLQSKTTGLH VTEYEDNLKQ SWVWKELHAV RNIRPSCHGI LGVYGGMIYT GIFYWILRGM 490 500 510 520 530 540 EPWTLKHKGS DSDQLKPAKD CTPIEYPKPD GQISFDLLSS VALSGTNHEH DQPAHLTLKD 550 560 570 580 590 600 DSIPVNRNLS IYDGPEQRFC PAGVYEFVPL EQGDGFRLQI NAQNCVHCKT CDIKDPSQNI 610 NWVVPEGGGG PAYNGM

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]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Kidney and Thymus.
[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: FVB/N. Tissue: Mammary tumor.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 212-222, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-152; LYS-222 AND LYS-343, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK002483 mRNA. Translation: BAB22135.1. AK075673 mRNA. Translation: BAC35888.1. AK141684 mRNA. Translation: BAE24798.1. AK152624 mRNA. Translation: BAE31367.1. AK169686 mRNA. Translation: BAE41304.1. BC012522 mRNA. Translation: AAH12522.1.
IPI	IPI00121322.
RefSeq	NP_080070.1.
UniGene	Mm.28336
3D structure databases
SMR	Q921G7. Positions 38-616.
ModBase	Search...
PTM databases
PhosphoSite	Q921G7.
Genome annotation databases
Ensembl	ENSMUSG00000027809. Mus musculus. [Contig view]
GeneID	66841.
KEGG	mmu:66841.
Organism-specific databases
MGI	MGI:106100. Etfdh.
Phylogenomic databases
HOGENOM	Q921G7.
HOVERGEN	Q921G7.
OMA	Q921G7. YTPGMEL.
Enzyme and pathway databases
BRENDA	1.5.5.1. 244.
Gene expression databases
Bgee	Q921G7.
CleanEx	MM_ETFDH.
GermOnline	ENSMUSG00000027809. Mus musculus.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR007859. ETFD_OxRdtase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000103. Pyridine_nuc-diS_OxRdtase_2. [Graphical view]
Pfam	PF05187. ETF_QO. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00469. PNDRDTASEII.
PROSITE	PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	322795.
SOURCE	Search...

Entry information

Entry name

ETFD_MOUSE

Accession

Primary (citable) accession number: Q921G7
Secondary accession number(s): Q3U7K2, Q8BK82, Q9DCT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)