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Protein

Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Gene

Etfdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Accepts electrons from ETF and reduces ubiquinone.By similarity

Catalytic activityi

Reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei304 – 3041Ubiquinone; via carbonyl oxygenBy similarity
Binding sitei305 – 3051Ubiquinone; via amide nitrogenBy similarity
Metal bindingi560 – 5601Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi585 – 5851Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi588 – 5881Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi591 – 5911Iron-sulfur (4Fe-4S)Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi70 – 8415FADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Ubiquinone

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (EC:1.5.5.1)
Short name:
ETF-QO
Short name:
ETF-ubiquinone oxidoreductase
Alternative name(s):
Electron-transferring-flavoprotein dehydrogenase
Short name:
ETF dehydrogenase
Gene namesi
Name:Etfdh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:106100. Etfdh.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei108 – 12922By similarityAdd
BLAST
Intramembranei427 – 44620By similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionSequence analysisAdd
BLAST
Chaini33 – 616584Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrialPRO_0000008662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 951N6-acetyllysineCombined sources
Modified residuei131 – 1311N6-acetyllysineCombined sources
Modified residuei222 – 2221N6-acetyllysineCombined sources
Modified residuei356 – 3561N6-acetyllysineCombined sources
Modified residuei415 – 4151N6-acetyllysineCombined sources
Modified residuei550 – 5501PhosphoserineCombined sources

Post-translational modificationi

Acetylation of Lys-95 and Lys-222 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ921G7.
MaxQBiQ921G7.
PaxDbiQ921G7.
PeptideAtlasiQ921G7.
PRIDEiQ921G7.

PTM databases

iPTMnetiQ921G7.
PhosphoSiteiQ921G7.
SwissPalmiQ921G7.

Expressioni

Gene expression databases

BgeeiQ921G7.
CleanExiMM_ETFDH.
ExpressionAtlasiQ921G7. baseline and differential.
GenevisibleiQ921G7. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ921G7. 3 interactions.
MINTiMINT-1844957.
STRINGi10090.ENSMUSP00000029386.

Structurei

3D structure databases

ProteinModelPortaliQ921G7.
SMRiQ921G7. Positions 38-616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini576 – 605304Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ETF-QO/FixC family.Curated
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2415. Eukaryota.
COG0644. LUCA.
GeneTreeiENSGT00390000010773.
HOGENOMiHOG000259450.
HOVERGENiHBG005615.
InParanoidiQ921G7.
KOiK00311.
OMAiLRGMEPW.
OrthoDBiEOG7WX07W.
PhylomeDBiQ921G7.
TreeFamiTF105687.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR007859. ETFD_OxRdtase/FixX.
IPR023753. FAD/NAD-binding_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
PANTHERiPTHR10617:SF107. PTHR10617:SF107. 1 hit.
PfamiPF05187. ETF_QO. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q921G7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVRLTKLSC PAYHWFHALK IKKCLPLCAP RCSSTSAVPQ ITTHYTVHPR
60 70 80 90 100
EKDKRWEGVN MERFAEEADV VIVGAGPAGL SAAIRLKQLA AEQGKDIRVC
110 120 130 140 150
LVEKAAQIGA HTLSGACLDP AAFKELFPDW KEKGAPLNTP VTEDRFAILT
160 170 180 190 200
EKHRIPVPIL PGLPMNNHGN YIVRLGHLVS WMGEQAEALG VEVYPGYAAA
210 220 230 240 250
EVLYHEDGSV KGIATNDVGI QKDGAPKTTF ERGLELHAKV TVFAEGCHGH
260 270 280 290 300
LAKQLYKKFD LRASCDAQTY GIGLKELWII DEKKWKPGRV DHTVGWPLDR
310 320 330 340 350
HTYGGSFLYH LNEGEPLVAV GFVVGLDYQN PYLSPFREFQ RWKHHPSIQP
360 370 380 390 400
TLEGGKRIAY GARALNEGGL QSIPKLTFPG GLLIGCSPGF MNVPKIKGTH
410 420 430 440 450
TAMKSGSLAA ESIFKQLTSE NLQSKTTGLH VTEYEDNLKQ SWVWKELHAV
460 470 480 490 500
RNIRPSCHGI LGVYGGMIYT GIFYWILRGM EPWTLKHKGS DSDQLKPAKD
510 520 530 540 550
CTPIEYPKPD GQISFDLLSS VALSGTNHEH DQPAHLTLKD DSIPVNRNLS
560 570 580 590 600
IYDGPEQRFC PAGVYEFVPL EQGDGFRLQI NAQNCVHCKT CDIKDPSQNI
610
NWVVPEGGGG PAYNGM
Length:616
Mass (Da):68,091
Last modified:December 1, 2001 - v1
Checksum:i1E5C6F85725E3CEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti342 – 3421W → C in BAB22135 (PubMed:16141072).Curated
Sequence conflicti355 – 3551G → W in BAC35888 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17418.1.
RefSeqiNP_080070.2. NM_025794.2.
UniGeneiMm.28336.

Genome annotation databases

EnsembliENSMUST00000029386; ENSMUSP00000029386; ENSMUSG00000027809.
GeneIDi66841.
KEGGimmu:66841.
UCSCiuc008pnq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17418.1.
RefSeqiNP_080070.2. NM_025794.2.
UniGeneiMm.28336.

3D structure databases

ProteinModelPortaliQ921G7.
SMRiQ921G7. Positions 38-616.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ921G7. 3 interactions.
MINTiMINT-1844957.
STRINGi10090.ENSMUSP00000029386.

PTM databases

iPTMnetiQ921G7.
PhosphoSiteiQ921G7.
SwissPalmiQ921G7.

Proteomic databases

EPDiQ921G7.
MaxQBiQ921G7.
PaxDbiQ921G7.
PeptideAtlasiQ921G7.
PRIDEiQ921G7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029386; ENSMUSP00000029386; ENSMUSG00000027809.
GeneIDi66841.
KEGGimmu:66841.
UCSCiuc008pnq.2. mouse.

Organism-specific databases

CTDi2110.
MGIiMGI:106100. Etfdh.

Phylogenomic databases

eggNOGiKOG2415. Eukaryota.
COG0644. LUCA.
GeneTreeiENSGT00390000010773.
HOGENOMiHOG000259450.
HOVERGENiHBG005615.
InParanoidiQ921G7.
KOiK00311.
OMAiLRGMEPW.
OrthoDBiEOG7WX07W.
PhylomeDBiQ921G7.
TreeFamiTF105687.

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Miscellaneous databases

PROiQ921G7.
SOURCEiSearch...

Gene expression databases

BgeeiQ921G7.
CleanExiMM_ETFDH.
ExpressionAtlasiQ921G7. baseline and differential.
GenevisibleiQ921G7. MM.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR007859. ETFD_OxRdtase/FixX.
IPR023753. FAD/NAD-binding_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
PANTHERiPTHR10617:SF107. PTHR10617:SF107. 1 hit.
PfamiPF05187. ETF_QO. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131; LYS-222; LYS-356 AND LYS-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiETFD_MOUSE
AccessioniPrimary (citable) accession number: Q921G7
Secondary accession number(s): Q3U7K2, Q8BK82, Q9DCT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.