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Protein

Electron transfer flavoprotein subunit beta

Gene

ETFB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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

Cofactori

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-BTA-611105. Respiratory electron transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Electron transfer flavoprotein subunit betaCurated
Short name:
Beta-ETFBy similarity
Gene namesi
Name:ETFBBy similarity
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 18

Subcellular locationi

  • Mitochondrion matrix By similarity

GO - Cellular componenti

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_0000231524Add
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; alternateBy similarity
Modified residuei203 – 2031N6,N6,N6-trimethyllysine; by ETFBKMT1 Publication
Modified residuei210 – 2101N6-acetyllysine; alternateBy similarity
Modified residuei210 – 2101N6-succinyllysine; alternateBy similarity
Modified residuei223 – 2231PhosphoserineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei238 – 2381N6-acetyllysineBy similarity
Modified residuei248 – 2481N6-acetyllysine; alternateBy similarity
Modified residuei248 – 2481N6-succinyllysine; alternateBy similarity

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

PaxDbiQ2TBV3.
PRIDEiQ2TBV3.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027250.

Structurei

3D structure databases

ProteinModelPortaliQ2TBV3.
SMRiQ2TBV3. Positions 4-255.
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.
InParanoidiQ2TBV3.
KOiK03521.
OMAiNPFCDIA.
OrthoDBiEOG7X3QS5.
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.

Q2TBV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELRALVAV KRVIDFAVKI RVKPDKTGVV TDGVKHSMNP FCEIAVEEAV
60 70 80 90 100
RLKEKKLVKE IIAVSCGPAQ CQETIRTALA MGADRGIHVE VPAAEANHLG
110 120 130 140 150
PLQVARVLAK LAEKEKVDLV LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA
160 170 180 190 200
SQVTLEGDKI KVEREIDGGL ETLRLKLPAV VTADLRLNEP RYATLPNIMK
210 220 230 240 250
AKKKKIEVIK AGDLGVDLTS KLSVISVEDP PQRTAGVKVE TTEDLVAKLK

EIGRI
Length:255
Mass (Da):27,699
Last modified:January 23, 2007 - v3
Checksum:i0B96D6893DEF3C6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109603 mRNA. Translation: AAI09604.1.
RefSeqiNP_001033671.1. NM_001038582.1.
UniGeneiBt.38985.

Genome annotation databases

EnsembliENSBTAT00000027250; ENSBTAP00000027250; ENSBTAG00000020449.
GeneIDi617210.
KEGGibta:617210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109603 mRNA. Translation: AAI09604.1.
RefSeqiNP_001033671.1. NM_001038582.1.
UniGeneiBt.38985.

3D structure databases

ProteinModelPortaliQ2TBV3.
SMRiQ2TBV3. Positions 4-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027250.

Proteomic databases

PaxDbiQ2TBV3.
PRIDEiQ2TBV3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000027250; ENSBTAP00000027250; ENSBTAG00000020449.
GeneIDi617210.
KEGGibta:617210.

Organism-specific databases

CTDi2109.

Phylogenomic databases

eggNOGiKOG3180. Eukaryota.
COG2086. LUCA.
GeneTreeiENSGT00390000009936.
HOGENOMiHOG000247877.
HOVERGENiHBG005614.
InParanoidiQ2TBV3.
KOiK03521.
OMAiNPFCDIA.
OrthoDBiEOG7X3QS5.
TreeFamiTF314039.

Enzyme and pathway databases

ReactomeiR-BTA-611105. Respiratory electron transport.

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  2. "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: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, METHYLATION AT LYS-200 AND LYS-203.

Entry informationi

Entry nameiETFB_BOVIN
AccessioniPrimary (citable) accession number: Q2TBV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 77 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. 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.