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Protein

Electron transfer flavoprotein subunit beta

Gene

ETFB

Organism
Sus scrofa (Pig)
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

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

ReactomeiR-SSC-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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 6

Subcellular locationi

  • Mitochondrion matrix By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002315252 – 255Electron transfer flavoprotein subunit betaAdd BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei200N6,N6,N6-trimethyllysine; by ETFBKMT; alternateBy similarity1
Modified residuei200N6-acetyllysine; alternateBy similarity1
Modified residuei200N6-methyllysine; alternateBy similarity1
Modified residuei203N6,N6,N6-trimethyllysine; by ETFBKMTBy similarity1
Modified residuei210N6-acetyllysine; alternateBy similarity1
Modified residuei210N6-succinyllysine; alternateBy similarity1
Modified residuei223PhosphoserineBy similarity1
Modified residuei226PhosphoserineBy similarity1
Modified residuei238N6-acetyllysineBy similarity1
Modified residuei248N6-acetyllysine; alternateBy similarity1
Modified residuei248N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PeptideAtlasiQ6UAQ8.
PRIDEiQ6UAQ8.

Expressioni

Gene expression databases

BgeeiENSSSCG00000003229.
GenevisibleiQ6UAQ8. SS.

Interactioni

Subunit structurei

Electron transfer flavoprotein is a heterodimer composed of ETFA and ETFB. Interacts with ETFRF1.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6UAQ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni183 – 205Recognition loopBy similarityAdd BLAST23

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

GeneTreeiENSGT00390000009936.
HOVERGENiHBG005614.
InParanoidiQ6UAQ8.
KOiK03521.
OMAiCVISAGP.
OrthoDBiEOG091G0KHH.
TreeFamiTF314039.

Family and domain databases

CDDicd01714. ETF_beta. 1 hit.
Gene3Di3.40.50.620. 1 hit.
InterProiIPR000049. ET-Flavoprotein_bsu_CS.
IPR014730. ETF_a/b_N.
IPR012255. ETF_b.
IPR033948. ETF_beta_N.
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.

Q6UAQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELRALVAV KRVIDFAVKI RVKPDRTGVV MDGVKHSMNP FCEIAVEEAV
60 70 80 90 100
RLKEKKLVKE VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPAAEAHHLG
110 120 130 140 150
PLQVARVLAK LAQKEKVDLV LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA
160 170 180 190 200
SQVTLEGDKV KVEREIDGGL ETLRLKLPAV VTADLRLNEP RYATLPNIMK
210 220 230 240 250
AKKKKIEVIK AGDLGVDLTS KLSVVSVEDP PQRVAGVKVE TTEDLVAKLR

EIGRI
Length:255
Mass (Da):27,764
Last modified:January 23, 2007 - v3
Checksum:i30C3786463FB5AB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY374470 mRNA. Translation: AAQ84565.1.
RefSeqiNP_001192208.1. NM_001205279.1.
UniGeneiSsc.1459.

Genome annotation databases

EnsembliENSSSCT00000003588; ENSSSCP00000003505; ENSSSCG00000003229.
GeneIDi396614.
KEGGissc:396614.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY374470 mRNA. Translation: AAQ84565.1.
RefSeqiNP_001192208.1. NM_001205279.1.
UniGeneiSsc.1459.

3D structure databases

ProteinModelPortaliQ6UAQ8.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiQ6UAQ8.
PRIDEiQ6UAQ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000003588; ENSSSCP00000003505; ENSSSCG00000003229.
GeneIDi396614.
KEGGissc:396614.

Organism-specific databases

CTDi2109.

Phylogenomic databases

GeneTreeiENSGT00390000009936.
HOVERGENiHBG005614.
InParanoidiQ6UAQ8.
KOiK03521.
OMAiCVISAGP.
OrthoDBiEOG091G0KHH.
TreeFamiTF314039.

Enzyme and pathway databases

ReactomeiR-SSC-611105. Respiratory electron transport.

Gene expression databases

BgeeiENSSSCG00000003229.
GenevisibleiQ6UAQ8. SS.

Family and domain databases

CDDicd01714. ETF_beta. 1 hit.
Gene3Di3.40.50.620. 1 hit.
InterProiIPR000049. ET-Flavoprotein_bsu_CS.
IPR014730. ETF_a/b_N.
IPR012255. ETF_b.
IPR033948. ETF_beta_N.
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...

Entry informationi

Entry nameiETFB_PIG
AccessioniPrimary (citable) accession number: Q6UAQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 74 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

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.