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Protein

Electron transfer flavoprotein subunit beta

Gene

Etfb

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 similarity1 Publication

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarityNote: Binds 1 FAD per dimer.By similarity
  • AMPBy similarityNote: Binds 1 AMP per subunit.By similarity

GO - Molecular functioni

GO - Biological processi

  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: UniProtKB
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 betaCurated
Short name:
Beta-ETFBy similarity
Gene namesi
Name:EtfbImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:106098. Etfb.

Subcellular locationi

  • Mitochondrion matrix By similarity

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • mitochondrial electron transfer flavoprotein complex Source: MGI
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 255254Electron transfer flavoprotein subunit betaPRO_0000167871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei200 – 2001N6,N6,N6-trimethyllysine; by ETFBKMT; alternate1 Publication
Modified residuei200 – 2001N6-acetyllysine; alternateCombined sources
Modified residuei203 – 2031N6,N6,N6-trimethyllysine; by ETFBKMT1 Publication
Modified residuei210 – 2101N6-acetyllysine; alternateCombined sources
Modified residuei210 – 2101N6-succinyllysine; alternateCombined sources
Modified residuei223 – 2231PhosphoserineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei238 – 2381N6-acetyllysineCombined sources
Modified residuei248 – 2481N6-acetyllysine; alternateCombined sources
Modified residuei248 – 2481N6-succinyllysine; alternateCombined sources

Post-translational modificationi

Methylated. Trimethylation at Lys-200 and Lys-203 may negatively regulate the activity in electron transfer from Acyl-CoA dehydrogenases.By similarity1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ9DCW4.
MaxQBiQ9DCW4.
PaxDbiQ9DCW4.
PRIDEiQ9DCW4.
TopDownProteomicsiQ9DCW4.

2D gel databases

REPRODUCTION-2DPAGEQ9DCW4.

PTM databases

iPTMnetiQ9DCW4.
PhosphoSiteiQ9DCW4.
SwissPalmiQ9DCW4.

Expressioni

Gene expression databases

BgeeiQ9DCW4.
GenevisibleiQ9DCW4. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi225938. 2 interactions.
IntActiQ9DCW4. 6 interactions.
MINTiMINT-1859959.
STRINGi10090.ENSMUSP00000004729.

Structurei

3D structure databases

ProteinModelPortaliQ9DCW4.
SMRiQ9DCW4. Positions 4-231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 20523Recognition loopBy similarityAdd
BLAST

Domaini

The recognition loop recognizes a hydrophobic patch at the surface of interacting dehydrogenases and acts as a static anchor at the interface.By similarity

Sequence similaritiesi

Belongs to the ETF beta-subunit/FixA family.Curated

Phylogenomic databases

eggNOGiKOG3180. Eukaryota.
COG2086. LUCA.
GeneTreeiENSGT00390000009936.
HOGENOMiHOG000247877.
HOVERGENiHBG005614.
InParanoidiQ9DCW4.
KOiK03521.
OMAiNPFCDIA.
OrthoDBiEOG7X3QS5.
PhylomeDBiQ9DCW4.
TreeFamiTF314039.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR000049. ET-Flavoprotein_bsu_CS.
IPR014730. ETF_a/b_N.
IPR012255. ETF_b.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21294. PTHR21294. 1 hit.
PfamiPF01012. ETF. 1 hit.
[Graphical view]
PIRSFiPIRSF000090. Beta-ETF. 1 hit.
SMARTiSM00893. ETF. 1 hit.
[Graphical view]
PROSITEiPS01065. ETF_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DCW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELRALVAV KRVIDFAVKI RVKPDKSGVV TDGVKHSMNP FCEIAVEEAV
60 70 80 90 100
RLKEKKLVKE IIAVSCGPSQ CQETIRTALA MGADRGIHVE IPGAQAESLG
110 120 130 140 150
PLQVARVLAK LAEKEKVDLL FLGKQAIDDD CNQTGQMTAG LLDWPQGTFA
160 170 180 190 200
SQVTLEGDKV KVEREIDGGL ETLRLKLPAV VTADLRLNEP RYATLPNIMK
210 220 230 240 250
AKKKKIEVVK AGDLGVDLTS KVSVISVEEP PQRSAGVKVE TTEDLVAKLK

EVGRI
Length:255
Mass (Da):27,623
Last modified:January 23, 2007 - v3
Checksum:i89E7100B327822FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 43Missing in BAB22076 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002407 mRNA. Translation: BAB22076.1.
AK150293 mRNA. Translation: BAE29447.1.
BC069877 mRNA. Translation: AAH69877.1.
BC049237 mRNA. Translation: AAH49237.1.
CCDSiCCDS21171.1.
RefSeqiNP_080971.2. NM_026695.3.
UniGeneiMm.30200.

Genome annotation databases

EnsembliENSMUST00000004729; ENSMUSP00000004729; ENSMUSG00000004610.
GeneIDi110826.
KEGGimmu:110826.
UCSCiuc009gmt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002407 mRNA. Translation: BAB22076.1.
AK150293 mRNA. Translation: BAE29447.1.
BC069877 mRNA. Translation: AAH69877.1.
BC049237 mRNA. Translation: AAH49237.1.
CCDSiCCDS21171.1.
RefSeqiNP_080971.2. NM_026695.3.
UniGeneiMm.30200.

3D structure databases

ProteinModelPortaliQ9DCW4.
SMRiQ9DCW4. Positions 4-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi225938. 2 interactions.
IntActiQ9DCW4. 6 interactions.
MINTiMINT-1859959.
STRINGi10090.ENSMUSP00000004729.

PTM databases

iPTMnetiQ9DCW4.
PhosphoSiteiQ9DCW4.
SwissPalmiQ9DCW4.

2D gel databases

REPRODUCTION-2DPAGEQ9DCW4.

Proteomic databases

EPDiQ9DCW4.
MaxQBiQ9DCW4.
PaxDbiQ9DCW4.
PRIDEiQ9DCW4.
TopDownProteomicsiQ9DCW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004729; ENSMUSP00000004729; ENSMUSG00000004610.
GeneIDi110826.
KEGGimmu:110826.
UCSCiuc009gmt.2. mouse.

Organism-specific databases

CTDi2109.
MGIiMGI:106098. Etfb.

Phylogenomic databases

eggNOGiKOG3180. Eukaryota.
COG2086. LUCA.
GeneTreeiENSGT00390000009936.
HOGENOMiHOG000247877.
HOVERGENiHBG005614.
InParanoidiQ9DCW4.
KOiK03521.
OMAiNPFCDIA.
OrthoDBiEOG7X3QS5.
PhylomeDBiQ9DCW4.
TreeFamiTF314039.

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Miscellaneous databases

ChiTaRSiEtfb. mouse.
NextBioi364735.
PROiQ9DCW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCW4.
GenevisibleiQ9DCW4. MM.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR000049. ET-Flavoprotein_bsu_CS.
IPR014730. ETF_a/b_N.
IPR012255. ETF_b.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21294. PTHR21294. 1 hit.
PfamiPF01012. ETF. 1 hit.
[Graphical view]
PIRSFiPIRSF000090. Beta-ETF. 1 hit.
SMARTiSM00893. ETF. 1 hit.
[Graphical view]
PROSITEiPS01065. ETF_BETA. 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.
    Tissue: Kidney and Macrophage.
  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 and FVB/N-3.
    Tissue: Kidney and Mammary tumor.
  3. Kanor S., Quadroni M., Bienvenut W.V.
    Submitted (MAR-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10 AND 210-220, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Skeletal muscle.
  4. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 77-106 AND 239-248, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-210 AND LYS-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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-200; LYS-210; LYS-238 AND LYS-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Human METTL20 methylates lysine residues adjacent to the recognition loop of the electron transfer flavoprotein in mitochondria."
    Rhein V.F., Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.
    J. Biol. Chem. 289:24640-24651(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, METHYLATION AT LYS-200 AND LYS-203.

Entry informationi

Entry nameiETFB_MOUSE
AccessioniPrimary (citable) accession number: Q9DCW4
Secondary accession number(s): Q810V3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 125 of the entry and version 3 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.