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Protein

Electron transfer flavoprotein subunit beta

Gene

Etfb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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

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

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_347303. Respiratory electron transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Electron transfer flavoprotein subunit beta
Short name:
Beta-ETF
Gene namesi
Name:Etfb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1303312. Etfb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 255254Electron transfer flavoprotein subunit betaPRO_0000231526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei19 – 191N6-acetyllysine; alternateBy similarity
Modified residuei19 – 191N6-succinyllysine; alternateBy similarity
Modified residuei35 – 351N6-acetyllysine; alternateBy similarity
Modified residuei35 – 351N6-succinyllysine; alternateBy similarity
Modified residuei56 – 561N6-acetyllysineBy similarity
Modified residuei59 – 591N6-acetyllysine; alternateBy similarity
Modified residuei59 – 591N6-succinyllysine; alternateBy similarity
Modified residuei110 – 1101N6-acetyllysine; alternateBy similarity
Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
Modified residuei114 – 1141N6-acetyllysineBy similarity
Modified residuei116 – 1161N6-acetyllysine; alternateBy similarity
Modified residuei116 – 1161N6-succinyllysine; alternateBy similarity
Modified residuei200 – 2001N6,N6,N6-trimethyllysine; by METTL20; alternateBy similarity
Modified residuei200 – 2001N6-acetyllysine; alternateBy similarity
Modified residuei203 – 2031N6,N6,N6-trimethyllysine; by METTL20By similarity
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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ68FU3.
PRIDEiQ68FU3.

PTM databases

PhosphoSiteiQ68FU3.

Expressioni

Gene expression databases

GenevisibleiQ68FU3. RN.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024083.

Structurei

3D structure databases

ProteinModelPortaliQ68FU3.
SMRiQ68FU3. 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

eggNOGiCOG2086.
GeneTreeiENSGT00390000009936.
HOGENOMiHOG000247877.
HOVERGENiHBG005614.
InParanoidiQ68FU3.
KOiK03521.
OMAiANQTAQM.
OrthoDBiEOG7X3QS5.
PhylomeDBiQ68FU3.
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.

Q68FU3-1 [UniParc]FASTAAdd to basket

« Hide

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

EVGRI
Length:255
Mass (Da):27,687
Last modified:January 23, 2007 - v3
Checksum:i3D916689B2CB6FAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079351 mRNA. Translation: AAH79351.1.
RefSeqiNP_001004220.1. NM_001004220.1.
UniGeneiRn.60152.

Genome annotation databases

EnsembliENSRNOT00000024083; ENSRNOP00000024083; ENSRNOG00000017851.
GeneIDi292845.
KEGGirno:292845.
UCSCiRGD:1303312. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079351 mRNA. Translation: AAH79351.1.
RefSeqiNP_001004220.1. NM_001004220.1.
UniGeneiRn.60152.

3D structure databases

ProteinModelPortaliQ68FU3.
SMRiQ68FU3. Positions 4-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024083.

PTM databases

PhosphoSiteiQ68FU3.

Proteomic databases

PaxDbiQ68FU3.
PRIDEiQ68FU3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024083; ENSRNOP00000024083; ENSRNOG00000017851.
GeneIDi292845.
KEGGirno:292845.
UCSCiRGD:1303312. rat.

Organism-specific databases

CTDi2109.
RGDi1303312. Etfb.

Phylogenomic databases

eggNOGiCOG2086.
GeneTreeiENSGT00390000009936.
HOGENOMiHOG000247877.
HOVERGENiHBG005614.
InParanoidiQ68FU3.
KOiK03521.
OMAiANQTAQM.
OrthoDBiEOG7X3QS5.
PhylomeDBiQ68FU3.
TreeFamiTF314039.

Enzyme and pathway databases

ReactomeiREACT_347303. Respiratory electron transport.

Miscellaneous databases

NextBioi634891.
PROiQ68FU3.

Gene expression databases

GenevisibleiQ68FU3. RN.

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

  1. "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].
    Tissue: Kidney.

Entry informationi

Entry nameiETFB_RAT
AccessioniPrimary (citable) accession number: Q68FU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 78 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.