[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Fetal liver; PubMed=8306995 [NCBI, ExPASy, EBI, Israel, Japan] Goodman S.I., Axtell K.M., Bindoff L.A., Beard S.E., Gill R.E., Frerman F.E.; "Molecular cloning and expression of a cDNA encoding human electron transfer flavoprotein-ubiquinone oxidoreductase."; Eur. J. Biochem. 219:277-286(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Small intestine; The German cDNA consortium; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	VARIANT [LARGE SCALE ANALYSIS] LEU-565. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).

Comments

FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CATALYTIC ACTIVITY: Reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol.
COFACTOR: Binds 1 4Fe-4S cluster.
COFACTOR: FAD.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Mitochondrion inner membrane.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q16134-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q16134-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_011553, VSP_011554.

DISEASE: Defects in ETFDH are the cause of glutaric aciduria type IIc (GAIIC) [MIM:231680]; also known as glutaricaciduria IIC. GAIIC results in the excretion not only of glutaric acid but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids.
SIMILARITY: Belongs to the ETF-QO/fixC family.
SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ETFDH";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S69232; AAC60628.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX538129; CAD98030.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011890; AAH11890.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S41115; S41115.

NP_004444.2; -.

3D structure databases

Q16134; 39-617.

PTM databases

Q16134; -.

Enzyme and pathway databases

Reactome

REACT_6305; Electron Transport Chain.

Organism-specific databases

GC04P159812; -.

HIX0004598; -.

HGNC:3483; ETFDH.

231675; gene. [NCBI / EBI]
231680; phenotype. [NCBI / EBI]

Orphanet

25; Glutaryl-CoA dehydrogenase deficiency.
26791; Multiple FAD dehydrogenase deficiency.

PharmGKB

PA27899; -.

GeneCards

Q16134.

Gene expression databases

ArrayExpress

Q16134; -.

CleanEx

HS_ETFDH; -.

GermOnline

ENSG00000171503; Homo sapiens.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005743;	Cellular component: mitochondrial inner membrane (non-traceable author statement from ProtInc).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0004174;	Molecular function: electron-transferring-flavoprotein dehydrogenase activity (traceable author statement from ProtInc).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007859; ETFD_OxRdtase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
Graphical view of domain structure.

Pfam

PF05187; ETF_QO; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00469; PNDRDTASEII.

PROSITE

PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

Q16134; -.

Genome annotation databases

Ensembl

ENSG00000171503; Homo sapiens. [Contig view]

GeneID

2110; -.

KEGG

hsa:2110; -.

Phylogenomic databases

HOGENOM

Q16134; -.

HOVERGEN

Q16134; -.

Other

8533; -.

ETFDH; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Acetylation; Alternative splicing; Electron transport; FAD; Flavoprotein; Glutaricaciduria; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Polymorphism; Transit peptide; Transmembrane; Transport; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 33`	`33`	`Mitochondrion (Potential).`
`CHAIN`	`34 617`	`584`	`Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial.`	`PRO_0000008661`
`TRANSMEM`	`458 478`	`21`	`Potential.`
`DOMAIN`	`577 606`	`30`	`4Fe-4S ferredoxin-type.`
`NP_BIND`	`71 85`	`15`	`FAD (Potential).`
`METAL`	`561 561`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`586 586`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`589 589`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`592 592`		`Iron-sulfur (4Fe-4S) (Potential).`
`MOD_RES`	`96 96`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`153 153`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`223 223`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`344 344`		`N6-acetyllysine (By similarity).`
`VAR_SEQ`	`88 103`		`Missing (in isoform 2).`	`VSP_011553`
`VAR_SEQ`	`163 179`		`Missing (in isoform 2).`	`VSP_011554`
`VARIANT`	`565 565`	`1`	`V -> L (in a colorectal cancer sample; somatic mutation).`	`VAR_036134 [3D]`
`CONFLICT`	`109 109`		`I -> V (in Ref. 2; CAD98030).`

Sequence information

Length: 617 AA [This is the length of the unprocessed precursor]

Molecular weight: 68507 Da [This is the MW of the unprocessed precursor]

CRC64: 776E8EA544C12957 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLVPLAKLSC LAYQCFHALK IKKNYLPLCA IRWSSTSTVP RITTHYTIYP RDKDKRWEGV 

        70         80         90        100        110        120 
NMERFAEEAD VVIVGAGPAG LSAAVRLKQL AVAHEKDIRV CLVEKAAQIG AHTLSGACLD 

       130        140        150        160        170        180 
PGAFKELFPD WKEKGAPLNT PVTEDRFGIL TEKYRIPVPI LPGLPMNNHG NYIVRLGHLV 

       190        200        210        220        230        240 
SWMGEQAEAL GVEVYPGYAA AEVLFHDDGS VKGIATNDVG IQKDGAPKAT FERGLELHAK 

       250        260        270        280        290        300 
VTIFAEGCHG HLAKQLYKKF DLRANCEPQT YGIGLKELWV IDEKNWKPGR VDHTVGWPLD 

       310        320        330        340        350        360 
RHTYGGSFLY HLNEGEPLVA LGLVVGLDYQ NPYLSPFREF QRWKHHPSIR PTLEGGKRIA 

       370        380        390        400        410        420 
YGARALNEGG FQSIPKLTFP GGLLIGCSPG FMNVPKIKGT HTAMKSGILA AESIFNQLTS 

       430        440        450        460        470        480 
ENLQSKTIGL HVTEYEDNLK NSWVWKELYS VRNIRPSCHG VLGVYGGMIY TGIFYWILRG 

       490        500        510        520        530        540 
MEPWTLKHKG SDFERLKPAK DCTPIEYPKP DGQISFDLLS SVALSGTNHE HDQPAHLTLR 

       550        560        570        580        590        600 
DDSIPVNRNL SIYDGPEQRF CPAGVYEFVP VEQGDGFRLQ INAQNCVHCK TCDIKDPSQN 

       610 
INWVVPEGGG GPAYNGM

Q16134 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools