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Protein

Electron transfer flavoprotein subunit alpha, mitochondrial

Gene

Etfa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).By similarity

Cofactori

FADBy similarityNote: Binds 1 FAD per dimer.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi274 – 30229FADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Electron transfer flavoprotein subunit alpha, mitochondrial
Short name:
Alpha-ETF
Gene namesi
Name:Etfa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:106092. Etfa.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial electron transfer flavoprotein complex Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionSequence analysisAdd
BLAST
Chaini20 – 333314Electron transfer flavoprotein subunit alpha, mitochondrialPRO_0000008652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-acetyllysine; alternateCombined sources
Modified residuei59 – 591N6-succinyllysine; alternateCombined sources
Modified residuei62 – 621N6-acetyllysineCombined sources
Modified residuei69 – 691N6-acetyllysine; alternateCombined sources
Modified residuei69 – 691N6-succinyllysine; alternateCombined sources
Modified residuei75 – 751N6-acetyllysineCombined sources
Modified residuei85 – 851N6-acetyllysine; alternateCombined sources
Modified residuei85 – 851N6-succinyllysine; alternateCombined sources
Modified residuei93 – 931PhosphothreonineCombined sources
Modified residuei101 – 1011N6-acetyllysineCombined sources
Modified residuei139 – 1391N6-acetyllysineCombined sources
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei158 – 1581N6-acetyllysine; alternateCombined sources
Modified residuei158 – 1581N6-succinyllysine; alternateCombined sources
Modified residuei164 – 1641N6-acetyllysineCombined sources
Modified residuei187 – 1871N6-succinyllysineCombined sources
Modified residuei203 – 2031N6-acetyllysine; alternateCombined sources
Modified residuei203 – 2031N6-succinyllysine; alternateCombined sources
Modified residuei216 – 2161N6-succinyllysineCombined sources
Modified residuei226 – 2261N6-acetyllysine; alternateCombined sources
Modified residuei226 – 2261N6-succinyllysine; alternateCombined sources
Modified residuei232 – 2321N6-acetyllysine; alternateCombined sources
Modified residuei232 – 2321N6-succinyllysine; alternateCombined sources
Modified residuei301 – 3011N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99LC5.
MaxQBiQ99LC5.
PaxDbiQ99LC5.
PeptideAtlasiQ99LC5.
PRIDEiQ99LC5.

2D gel databases

REPRODUCTION-2DPAGEQ99LC5.
UCD-2DPAGEQ99LC5.

PTM databases

iPTMnetiQ99LC5.
PhosphoSiteiQ99LC5.
SwissPalmiQ99LC5.

Expressioni

Gene expression databases

BgeeiQ99LC5.
GenevisibleiQ99LC5. MM.

Interactioni

Subunit structurei

Electron transfer flavoprotein is a heterodimer composed of ETFA and ETFB.By similarity

Protein-protein interaction databases

IntActiQ99LC5. 3 interactions.
MINTiMINT-1859759.
STRINGi10090.ENSMUSP00000034866.

Structurei

3D structure databases

ProteinModelPortaliQ99LC5.
SMRiQ99LC5. Positions 20-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 204185Domain IBy similarityAdd
BLAST
Regioni205 – 333129Domain IIBy similarityAdd
BLAST

Domaini

Domain I shares an identical polypeptide fold with the beta subunit ETFB though there is no sequence similarity.By similarity

Sequence similaritiesi

Belongs to the ETF alpha-subunit/FixB family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3954. Eukaryota.
COG2025. LUCA.
GeneTreeiENSGT00390000013422.
HOGENOMiHOG000247865.
HOVERGENiHBG002317.
InParanoidiQ99LC5.
KOiK03522.
OMAiCCIESID.
OrthoDBiEOG76MK8R.
PhylomeDBiQ99LC5.
TreeFamiTF105763.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR014730. ETF_a/b_N.
IPR001308. ETF_a/FixB.
IPR014731. ETF_asu_C.
IPR018206. ETF_asu_C_CS.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01012. ETF. 1 hit.
PF00766. ETF_alpha. 1 hit.
[Graphical view]
PIRSFiPIRSF000089. Electra_flavoP_a. 1 hit.
SMARTiSM00893. ETF. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS00696. ETF_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99LC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRAAAPGQL RRAASLLRFQ STLVIAEHAN DSLAPITLNT ITAAGRLGGE
60 70 80 90 100
VSCLVAGTKC DKVVQDLCKV AGVAKVLVAQ HDAYKGLLPE ELTPLILETQ
110 120 130 140 150
KQFSYTHICA GASAFGKNLL PRVAAKLNVA PVSDIIEIKS PDTFVRTIYA
160 170 180 190 200
GNALCTVKCD EKVKVFSVRG TSFEAAATSG GSASSEKAPS SSSVGISEWL
210 220 230 240 250
DQKLTKSDRP ELTGAKVVVS GGRGLKSGEN FKLLYDLADQ LHAAVGASRA
260 270 280 290 300
AVDAGFVPND MQVGQTGKIV APELYIAVGI SGAIQHLAGM KDSKTIVAIN
310 320 330
KDPEAPIFQV ADYGIVADLF KVVPEMTEIL KKK
Length:333
Mass (Da):35,009
Last modified:May 1, 2007 - v2
Checksum:i635F34ADCDA254C0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201Q → R in BAE40260 (PubMed:16141072).Curated
Sequence conflicti85 – 851K → E in BAE21705 (PubMed:16141072).Curated
Sequence conflicti209 – 2091R → P in BAC25758 (PubMed:16141072).Curated
Sequence conflicti288 – 2881A → T in AAH03432 (PubMed:15489334).Curated
Sequence conflicti299 – 2991I → V in BAC28046 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028118 mRNA. Translation: BAC25758.1.
AK032830 mRNA. Translation: BAC28046.1.
AK133525 mRNA. Translation: BAE21705.1.
AK167572 mRNA. Translation: BAE39635.1.
AK168321 mRNA. Translation: BAE40260.1.
BC003432 mRNA. Translation: AAH03432.1.
BC096645 mRNA. Translation: AAH96645.1.
CCDSiCCDS23204.1.
RefSeqiNP_663590.3. NM_145615.4.
UniGeneiMm.290853.

Genome annotation databases

EnsembliENSMUST00000034866; ENSMUSP00000034866; ENSMUSG00000032314.
GeneIDi110842.
KEGGimmu:110842.
UCSCiuc009psl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028118 mRNA. Translation: BAC25758.1.
AK032830 mRNA. Translation: BAC28046.1.
AK133525 mRNA. Translation: BAE21705.1.
AK167572 mRNA. Translation: BAE39635.1.
AK168321 mRNA. Translation: BAE40260.1.
BC003432 mRNA. Translation: AAH03432.1.
BC096645 mRNA. Translation: AAH96645.1.
CCDSiCCDS23204.1.
RefSeqiNP_663590.3. NM_145615.4.
UniGeneiMm.290853.

3D structure databases

ProteinModelPortaliQ99LC5.
SMRiQ99LC5. Positions 20-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99LC5. 3 interactions.
MINTiMINT-1859759.
STRINGi10090.ENSMUSP00000034866.

PTM databases

iPTMnetiQ99LC5.
PhosphoSiteiQ99LC5.
SwissPalmiQ99LC5.

2D gel databases

REPRODUCTION-2DPAGEQ99LC5.
UCD-2DPAGEQ99LC5.

Proteomic databases

EPDiQ99LC5.
MaxQBiQ99LC5.
PaxDbiQ99LC5.
PeptideAtlasiQ99LC5.
PRIDEiQ99LC5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034866; ENSMUSP00000034866; ENSMUSG00000032314.
GeneIDi110842.
KEGGimmu:110842.
UCSCiuc009psl.2. mouse.

Organism-specific databases

CTDi2108.
MGIiMGI:106092. Etfa.

Phylogenomic databases

eggNOGiKOG3954. Eukaryota.
COG2025. LUCA.
GeneTreeiENSGT00390000013422.
HOGENOMiHOG000247865.
HOVERGENiHBG002317.
InParanoidiQ99LC5.
KOiK03522.
OMAiCCIESID.
OrthoDBiEOG76MK8R.
PhylomeDBiQ99LC5.
TreeFamiTF105763.

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Miscellaneous databases

PROiQ99LC5.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LC5.
GenevisibleiQ99LC5. MM.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR014730. ETF_a/b_N.
IPR001308. ETF_a/FixB.
IPR014731. ETF_asu_C.
IPR018206. ETF_asu_C_CS.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01012. ETF. 1 hit.
PF00766. ETF_alpha. 1 hit.
[Graphical view]
PIRSFiPIRSF000089. Electra_flavoP_a. 1 hit.
SMARTiSM00893. ETF. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS00696. ETF_ALPHA. 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 DBA/2.
    Tissue: Ovary, Placenta, Small intestine and Uterus.
  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: C57BL/6J.
    Tissue: Mammary gland.
  3. Lubec G., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 86-117 AND 233-249, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-69; LYS-85; LYS-158; LYS-187; LYS-203; LYS-216; LYS-226; LYS-232 AND LYS-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  6. "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-59; LYS-62; LYS-69; LYS-75; LYS-85; LYS-101; LYS-139; LYS-158; LYS-164; LYS-203; LYS-226 AND LYS-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiETFA_MOUSE
AccessioniPrimary (citable) accession number: Q99LC5
Secondary accession number(s): Q3THD7
, Q3V000, Q4V9X5, Q8BMD3, Q8BMU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: May 1, 2007
Last modified: July 6, 2016
This is version 128 of the entry and version 2 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.