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Electron transfer flavoprotein subunit alpha, mitochondrial (Alpha-ETF)

 ETFA_HUMAN              Reviewed;         333 AA.
P13804; B4DT43; Q53XN3;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
05-DEC-2018, entry version 203.
RecName: Full=Electron transfer flavoprotein subunit alpha, mitochondrial;
Short=Alpha-ETF;
Flags: Precursor;
Name=ETFA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3170610;
Finocchiaro G., Ito M., Ikeda Y., Tanaka K.;
"Molecular cloning and nucleotide sequence of cDNAs encoding the
alpha-subunit of human electron transfer flavoprotein.";
J. Biol. Chem. 263:15773-15780(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, FUNCTION, AND
VARIANT GA2A MET-266.
PubMed=12815589; DOI=10.1002/humu.10226;
Olsen R.K.J., Andresen B.S., Christensen E., Bross P., Skovby F.,
Gregersen N.;
"Clear relationship between ETF/ETFDH genotype and phenotype in
patients with multiple acyl-CoA dehydrogenation deficiency.";
Hum. Mutat. 22:12-23(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Chondrosarcoma, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
PROTEIN SEQUENCE OF 86-101 AND 170-203, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
REVIEW.
PubMed=17941859; DOI=10.1111/j.1742-4658.2007.06107.x;
Toogood H.S., Leys D., Scrutton N.S.;
"Dynamics driving function: new insights from electron transferring
flavoproteins and partner complexes.";
FEBS J. 274:5481-5504(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER PHE-19, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
FUNCTION, INTERACTION WITH ETFRF1, AND IDENTIFICATION IN A COMPLEX
WITH ETFB AND ETFRF1.
PubMed=27499296; DOI=10.1016/j.molcel.2016.06.033;
Floyd B.J., Wilkerson E.M., Veling M.T., Minogue C.E., Xia C.,
Beebe E.T., Wrobel R.L., Cho H., Kremer L.S., Alston C.L.,
Gromek K.A., Dolan B.K., Ulbrich A., Stefely J.A., Bohl S.L.,
Werner K.M., Jochem A., Westphall M.S., Rensvold J.W., Taylor R.W.,
Prokisch H., Kim J.J., Coon J.J., Pagliarini D.J.;
"Mitochondrial protein interaction mapping identifies regulators of
respiratory chain function.";
Mol. Cell 63:621-632(2016).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-333 IN COMPLEX WITH FAD
AND ETFB, SUBUNIT, COFACTOR, AND DOMAIN.
PubMed=8962055; DOI=10.1073/pnas.93.25.14355;
Roberts D.L., Frerman F.E., Kim J.-J.P.;
"Three-dimensional structure of human electron transfer flavoprotein
to 2.1-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 93:14355-14360(1996).
[16]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ETFB AND ACADM,
FUNCTION, AND SUBUNIT.
PubMed=15159392; DOI=10.1074/jbc.M404884200;
Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S.,
Leys D.;
"Extensive domain motion and electron transfer in the human electron
transferring flavoprotein.medium chain acyl-CoA dehydrogenase
complex.";
J. Biol. Chem. 279:32904-32912(2004).
[17]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH FAD; ETFB AND
ACADM, FUNCTION, COFACTOR, AND MUTAGENESIS OF ARG-249.
PubMed=15975918; DOI=10.1074/jbc.M505562200;
Toogood H.S., van Thiel A., Scrutton N.S., Leys D.;
"Stabilization of non-productive conformations underpins rapid
electron transfer to electron-transferring flavoprotein.";
J. Biol. Chem. 280:30361-30366(2005).
[18]
VARIANT GA2A GLY-157, AND FUNCTION.
PubMed=1882842;
Indo Y., Glassberg R., Yokota I., Tanaka K.;
"Molecular characterization of variant alpha-subunit of electron
transfer flavoprotein in three patients with glutaric acidemia type II
-- and identification of glycine substitution for valine-157 in the
sequence of the precursor, producing an unstable mature protein in a
patient.";
Am. J. Hum. Genet. 49:575-580(1991).
[19]
VARIANTS GA2A ARG-116 AND MET-266, FUNCTION, AND CHARACTERIZATION OF
VARIANT GA2A MET-266.
PubMed=1430199; DOI=10.1172/JCI116040;
Freneaux E., Sheffield V.C., Molin L., Shires A., Rhead W.;
"Glutaric acidemia type II. Heterogeneity in beta-oxidation flux,
polypeptide synthesis, and complementary DNA mutations in the alpha
subunit of electron transfer flavoprotein in eight patients.";
J. Clin. Invest. 90:1679-1686(1992).
[20]
CHARACTERIZATION OF VARIANTS GA2A ARG-116 AND MET-266, FUNCTION,
COFACTOR, AND SUBUNIT.
PubMed=9334218;
Salazar D., Zhang L., deGala G.D., Frerman F.E.;
"Expression and characterization of two pathogenic mutations in human
electron transfer flavoprotein.";
J. Biol. Chem. 272:26425-26433(1997).
[21]
VARIANT ILE-171, CHARACTERIZATION OF VARIANT ILE-171, AND FUNCTION.
PubMed=10356313; DOI=10.1006/mgme.1999.2856;
Bross P., Pedersen P., Winter V., Nyholm M., Johansen B.N.,
Olsen R.K., Corydon M.J., Andresen B.S., Eiberg H., Kolvraa S.,
Gregersen N.;
"A polymorphic variant in the human electron transfer flavoprotein
alpha-chain (alpha-T171) displays decreased thermal stability and is
overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient
patients with mild childhood presentation.";
Mol. Genet. Metab. 67:138-147(1999).
-!- FUNCTION: Heterodimeric electron transfer flavoprotein that
accepts electrons from several mitochondrial dehydrogenases,
including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine
dehydrogenase (PubMed:27499296, PubMed:15159392, PubMed:15975918,
PubMed:9334218, PubMed:10356313). It transfers the electrons to
the main mitochondrial respiratory chain via ETF-ubiquinone
oxidoreductase (ETF dehydrogenase) (PubMed:9334218). Required for
normal mitochondrial fatty acid oxidation and normal amino acid
metabolism (PubMed:12815589, PubMed:1882842, PubMed:1430199).
{ECO:0000269|PubMed:10356313, ECO:0000269|PubMed:12815589,
ECO:0000269|PubMed:1430199, ECO:0000269|PubMed:15159392,
ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:27499296,
ECO:0000269|PubMed:9334218, ECO:0000303|PubMed:17941859,
ECO:0000305|PubMed:1882842}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:8962055, ECO:0000269|PubMed:9334218};
Note=Binds 1 FAD per dimer. {ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:8962055};
-!- SUBUNIT: Heterodimer composed of ETFA and ETFB (PubMed:8962055,
PubMed:15159392, PubMed:15975918, PubMed:9334218). Identified in a
complex that contains ETFA, ETFB and ETFRF1 (PubMed:27499296).
Interaction with ETFRF1 promotes dissociation of the bound FAD and
loss of electron transfer activity (PubMed:27499296).
{ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:27499296, ECO:0000269|PubMed:8962055}.
-!- INTERACTION:
P38117:ETFB; NbExp=2; IntAct=EBI-1052886, EBI-1056543;
Q8IWL3:HSCB; NbExp=3; IntAct=EBI-1052886, EBI-1805738;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P13804-1; Sequence=Displayed;
Name=2;
IsoId=P13804-2; Sequence=VSP_043246;
Note=No experimental confirmation available.;
-!- DOMAIN: Domain I shares an identical polypeptide fold with the
beta subunit ETFB though there is no sequence similarity.
{ECO:0000269|PubMed:8962055}.
-!- PTM: The N-terminus is blocked.
-!- DISEASE: Glutaric aciduria 2A (GA2A) [MIM:231680]: An autosomal
recessively inherited disorder of fatty acid, amino acid, and
choline metabolism. It is characterized by multiple acyl-CoA
dehydrogenase deficiencies resulting in large excretion not only
of glutaric acid, but also of lactic, ethylmalonic, butyric,
isobutyric, 2-methyl-butyric, and isovaleric acids.
{ECO:0000269|PubMed:12815589, ECO:0000269|PubMed:1430199,
ECO:0000269|PubMed:1882842, ECO:0000269|PubMed:9334218}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
{ECO:0000305}.
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EMBL; J04058; AAA52406.1; -; mRNA.
EMBL; S55815; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S55816; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AJ224002; CAA11802.1; -; Genomic_DNA.
EMBL; AF436657; AAN03712.1; -; Genomic_DNA.
EMBL; AF436646; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436647; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436648; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436649; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436650; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436651; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436652; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436653; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436654; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436655; AAN03712.1; JOINED; Genomic_DNA.
EMBL; AF436656; AAN03712.1; JOINED; Genomic_DNA.
EMBL; BT009796; AAP88798.1; -; mRNA.
EMBL; AK292979; BAF85668.1; -; mRNA.
EMBL; AK300044; BAG61855.1; -; mRNA.
EMBL; AC027243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471136; EAW99221.1; -; Genomic_DNA.
EMBL; BC015526; AAH15526.1; -; mRNA.
EMBL; BC095457; AAH95457.1; -; mRNA.
CCDS; CCDS32299.1; -. [P13804-1]
CCDS; CCDS45311.1; -. [P13804-2]
PIR; A31998; A31998.
RefSeq; NP_000117.1; NM_000126.3. [P13804-1]
RefSeq; NP_001121188.1; NM_001127716.1. [P13804-2]
UniGene; Hs.39925; -.
PDB; 1EFV; X-ray; 2.10 A; A=20-333.
PDB; 1T9G; X-ray; 2.90 A; R=1-333.
PDB; 2A1T; X-ray; 2.80 A; R=1-333.
PDB; 2A1U; X-ray; 2.11 A; A=1-333.
PDBsum; 1EFV; -.
PDBsum; 1T9G; -.
PDBsum; 2A1T; -.
PDBsum; 2A1U; -.
ProteinModelPortal; P13804; -.
SMR; P13804; -.
BioGrid; 108409; 84.
ComplexPortal; CPX-2731; Electron transfer flavoprotein complex.
DIP; DIP-6161N; -.
IntAct; P13804; 44.
MINT; P13804; -.
STRING; 9606.ENSP00000452762; -.
CarbonylDB; P13804; -.
iPTMnet; P13804; -.
PhosphoSitePlus; P13804; -.
SwissPalm; P13804; -.
BioMuta; ETFA; -.
DMDM; 119636; -.
UCD-2DPAGE; P13804; -.
EPD; P13804; -.
PaxDb; P13804; -.
PeptideAtlas; P13804; -.
PRIDE; P13804; -.
ProteomicsDB; 52989; -.
ProteomicsDB; 52990; -. [P13804-2]
TopDownProteomics; P13804-1; -. [P13804-1]
TopDownProteomics; P13804-2; -. [P13804-2]
DNASU; 2108; -.
Ensembl; ENST00000433983; ENSP00000399273; ENSG00000140374. [P13804-2]
Ensembl; ENST00000557943; ENSP00000452762; ENSG00000140374. [P13804-1]
GeneID; 2108; -.
KEGG; hsa:2108; -.
UCSC; uc002bbt.3; human. [P13804-1]
CTD; 2108; -.
DisGeNET; 2108; -.
EuPathDB; HostDB:ENSG00000140374.15; -.
GeneCards; ETFA; -.
HGNC; HGNC:3481; ETFA.
HPA; HPA018990; -.
HPA; HPA018993; -.
HPA; HPA018996; -.
HPA; HPA024089; -.
MalaCards; ETFA; -.
MIM; 231680; phenotype.
MIM; 608053; gene.
neXtProt; NX_P13804; -.
OpenTargets; ENSG00000140374; -.
Orphanet; 394532; Multiple acyl-CoA dehydrogenase deficiency, mild type.
Orphanet; 394529; Multiple acyl-CoA dehydrogenase deficiency, severe neonatal type.
PharmGKB; PA27897; -.
eggNOG; KOG3954; Eukaryota.
eggNOG; COG2025; LUCA.
GeneTree; ENSGT00390000013422; -.
HOGENOM; HOG000247865; -.
HOVERGEN; HBG002317; -.
InParanoid; P13804; -.
KO; K03522; -.
OMA; SQFKFTH; -.
OrthoDB; EOG091G0EQM; -.
PhylomeDB; P13804; -.
TreeFam; TF105763; -.
Reactome; R-HSA-611105; Respiratory electron transport.
ChiTaRS; ETFA; human.
EvolutionaryTrace; P13804; -.
GeneWiki; ETFA; -.
GenomeRNAi; 2108; -.
PRO; PR:P13804; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140374; Expressed in 232 organ(s), highest expression level in oocyte.
CleanEx; HS_ETFA; -.
ExpressionAtlas; P13804; baseline and differential.
Genevisible; P13804; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:UniProtKB.
CDD; cd01715; ETF_alpha; 1.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR014730; ETF_a/b_N.
InterPro; IPR001308; ETF_a/FixB.
InterPro; IPR033947; ETF_alpha_N.
InterPro; IPR014731; ETF_asu_C.
InterPro; IPR018206; ETF_asu_C_CS.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01012; ETF; 1.
Pfam; PF00766; ETF_alpha; 1.
PIRSF; PIRSF000089; Electra_flavoP_a; 1.
SMART; SM00893; ETF; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS00696; ETF_ALPHA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Electron transport; FAD;
Flavoprotein; Glutaricaciduria; Mitochondrion; Phosphoprotein;
Polymorphism; Reference proteome; Transit peptide; Transport.
TRANSIT 1 19 Mitochondrion.
{ECO:0000244|PubMed:25944712,
ECO:0000255}.
CHAIN 20 333 Electron transfer flavoprotein subunit
alpha, mitochondrial.
/FTId=PRO_0000008650.
NP_BIND 263 266 FAD. {ECO:0000244|PDB:1EFV,
ECO:0000244|PDB:2A1T,
ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:8962055}.
NP_BIND 281 286 FAD. {ECO:0000244|PDB:1EFV,
ECO:0000244|PDB:2A1T,
ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:8962055}.
NP_BIND 318 319 FAD. {ECO:0000244|PDB:1EFV,
ECO:0000244|PDB:2A1T,
ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:8962055}.
REGION 20 204 Domain I. {ECO:0000269|PubMed:8962055}.
REGION 205 333 Domain II. {ECO:0000269|PubMed:8962055}.
BINDING 223 223 FAD. {ECO:0000244|PDB:1EFV,
ECO:0000244|PDB:2A1T,
ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:8962055}.
BINDING 248 248 FAD. {ECO:0000244|PDB:1EFV,
ECO:0000244|PDB:2A1T,
ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:8962055}.
BINDING 300 300 FAD. {ECO:0000244|PDB:1EFV,
ECO:0000244|PDB:2A1T,
ECO:0000269|PubMed:15975918,
ECO:0000269|PubMed:8962055}.
MOD_RES 59 59 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 59 59 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 62 62 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 69 69 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 69 69 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 75 75 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 85 85 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 85 85 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 93 93 Phosphothreonine.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 101 101 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 139 139 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 158 158 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 158 158 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 164 164 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 187 187 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 203 203 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 203 203 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 216 216 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 226 226 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 226 226 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 232 232 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 232 232 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LC5}.
MOD_RES 301 301 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99LC5}.
VAR_SEQ 14 62 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043246.
VARIANT 116 116 G -> R (in GA2A; impaired protein
stability and loss of electron transfer
activity; dbSNP:rs119458971).
{ECO:0000269|PubMed:1430199,
ECO:0000269|PubMed:9334218}.
/FTId=VAR_002366.
VARIANT 157 157 V -> G (in GA2A; dbSNP:rs119458969).
{ECO:0000269|PubMed:1882842}.
/FTId=VAR_002367.
VARIANT 171 171 T -> I (decreased protein stability;
dbSNP:rs1801591).
{ECO:0000269|PubMed:10356313}.
/FTId=VAR_008547.
VARIANT 266 266 T -> M (in GA2A; decreased electron
transfer activity; dbSNP:rs119458970).
{ECO:0000269|PubMed:12815589,
ECO:0000269|PubMed:1430199}.
/FTId=VAR_002368.
MUTAGEN 249 249 R->A: Loss of electron transfer activity.
{ECO:0000269|PubMed:15975918}.
STRAND 21 25 {ECO:0000244|PDB:1EFV}.
STRAND 28 31 {ECO:0000244|PDB:2A1U}.
HELIX 36 45 {ECO:0000244|PDB:1EFV}.
STRAND 49 58 {ECO:0000244|PDB:1EFV}.
HELIX 61 69 {ECO:0000244|PDB:1EFV}.
STRAND 75 80 {ECO:0000244|PDB:1EFV}.
HELIX 82 84 {ECO:0000244|PDB:1EFV}.
HELIX 89 103 {ECO:0000244|PDB:1EFV}.
STRAND 106 113 {ECO:0000244|PDB:1EFV}.
HELIX 114 127 {ECO:0000244|PDB:1EFV}.
STRAND 132 135 {ECO:0000244|PDB:1EFV}.
STRAND 137 140 {ECO:0000244|PDB:1EFV}.
STRAND 143 148 {ECO:0000244|PDB:1EFV}.
TURN 149 152 {ECO:0000244|PDB:1EFV}.
STRAND 153 159 {ECO:0000244|PDB:1EFV}.
STRAND 162 168 {ECO:0000244|PDB:1EFV}.
HELIX 170 172 {ECO:0000244|PDB:1EFV}.
STRAND 178 180 {ECO:0000244|PDB:1EFV}.
STRAND 184 187 {ECO:0000244|PDB:1EFV}.
STRAND 196 204 {ECO:0000244|PDB:1EFV}.
HELIX 212 214 {ECO:0000244|PDB:1EFV}.
STRAND 216 221 {ECO:0000244|PDB:1EFV}.
HELIX 223 225 {ECO:0000244|PDB:1EFV}.
HELIX 229 231 {ECO:0000244|PDB:1EFV}.
HELIX 232 241 {ECO:0000244|PDB:1EFV}.
STRAND 244 247 {ECO:0000244|PDB:1EFV}.
HELIX 249 253 {ECO:0000244|PDB:1EFV}.
HELIX 259 261 {ECO:0000244|PDB:1EFV}.
STRAND 262 264 {ECO:0000244|PDB:1EFV}.
STRAND 273 279 {ECO:0000244|PDB:1EFV}.
HELIX 284 287 {ECO:0000244|PDB:1EFV}.
TURN 288 292 {ECO:0000244|PDB:1EFV}.
STRAND 294 301 {ECO:0000244|PDB:1EFV}.
HELIX 306 309 {ECO:0000244|PDB:1EFV}.
STRAND 312 317 {ECO:0000244|PDB:1EFV}.
HELIX 319 329 {ECO:0000244|PDB:1EFV}.
SEQUENCE 333 AA; 35080 MW; 2EC6D1ADE68CBDB5 CRC64;
MFRAAAPGQL RRAASLLRFQ STLVIAEHAN DSLAPITLNT ITAATRLGGE VSCLVAGTKC
DKVAQDLCKV AGIAKVLVAQ HDVYKGLLPE ELTPLILATQ KQFNYTHICA GASAFGKNLL
PRVAAKLEVA PISDIIAIKS PDTFVRTIYA GNALCTVKCD EKVKVFSVRG TSFDAAATSG
GSASSEKASS TSPVEISEWL DQKLTKSDRP ELTGAKVVVS GGRGLKSGEN FKLLYDLADQ
LHAAVGASRA AVDAGFVPND MQVGQTGKIV APELYIAVGI SGAIQHLAGM KDSKTIVAIN
KDPEAPIFQV ADYGIVADLF KVVPEMTEIL KKK


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