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UniProtKB/Swiss-Prot entry P38117


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ETFB_HUMAN
Primary accession number P38117
Secondary accession numbers B3KNY2 Q6IBH7 Q71RF6 Q9Y3S7
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 103)
Name and origin of the protein
Protein name Electron transfer flavoprotein subunit beta
Synonym Beta-ETF
Gene name
Name: ETFB
ORFNames: FP585
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
DOI=10.1111/j.1432-1033.1993.tb17847.x; PubMed=8504797 [NCBI, ExPASy, EBI, Israel, Japan]
Finocchiaro G., Colombo I., Garavaglia B., Gellera C., Valdameri G., Garbuglio N., Didonato S.;
"cDNA cloning and mitochondrial import of the beta-subunit of the human electron-transfer flavoprotein.";
Eur. J. Biochem. 213:1003-1008(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GA2B ASN-128.
DOI=10.1002/humu.10226; PubMed=12815589 [NCBI, ExPASy, EBI, Israel, Japan]
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 2), AND VARIANT MET-154.
DOI=10.1073/pnas.0404089101; PubMed=15498874 [NCBI, ExPASy, EBI, Israel, Japan]
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-199, AND VARIANT GA2B GLN-164.
DOI=10.1093/hmg/3.3.429; PubMed=7912128 [NCBI, ExPASy, EBI, Israel, Japan]
Colombo I., Finocchiaro G., Garavaglia B., Garbuglio N., Yamaguchi S., Frerman F., Berra B., Didonato S.;
"Mutations and polymorphisms of the gene encoding the beta-subunit of the electron transfer flavoprotein in three patients with glutaric acidemia type II.";
Hum. Mol. Genet. 3:429-435(1994).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1073/pnas.93.25.14355; PubMed=8962055 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
VARIANT MET-154.
DOI=10.1006/mgme.1999.2856; PubMed=10356313 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • FUNCTION: 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).
  • COFACTOR: Binds 1 FAD per dimer.
  • COFACTOR: Binds 1 AMP per subunit.
  • SUBUNIT: Heterodimer of an alpha and a beta subunit.
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDP38117-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDP38117-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_017850.
  • TISSUE SPECIFICITY: Abundant in liver, heart and skeletal muscle. A weak expression is seen in the brain, placenta, lung, kidney and pancreas.
  • DISEASE: Defects in ETFB are the cause of glutaric aciduria type 2B (GA2B) [MIM:231680]. GA2B is 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.
  • SIMILARITY: Belongs to the ETF beta-subunit/fixA family.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ETFB";.
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
X71129; CAA50441.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF436663; AAN03713.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF436658; AAN03713.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF436659; AAN03713.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF436660; AAN03713.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF436661; AAN03713.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF436662; AAN03713.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF370381; AAQ15217.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456827; CAG33108.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK055285; BAG51494.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093961; AAH93961.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093963; AAH93963.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76067; CAB37832.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00004902; -.
IPI00556451; -.
PIR S32482; S32482.
RefSeq NP_001014763.1; -.
NP_001976.1; -.
UniGene Hs.654553
3D structure databases
PDB
1EFV; X-ray; 2.10 A; B=1-255.[ExPASy / RCSB / EBI]
1T9G; X-ray; 2.90 A; S=1-255.[ExPASy / RCSB / EBI]
2A1T; X-ray; 2.80 A; S=1-255.[ExPASy / RCSB / EBI]
2A1U; X-ray; 2.11 A; B=1-255.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EFV; -.
1T9G; -.
2A1T; -.
2A1U; -.
ModBase P38117.
Protein-protein interaction databases
DIP DIP:6162N; -.
IntAct P38117; 2.
PTM databases
PhosphoSite P38117; -.
Enzyme and pathway databases
Reactome REACT_6305; Electron Transport Chain.
2D gel databases
REPRODUCTION-2DPAGE IPI00004902; -.
Organism-specific databases
GeneCards GC19M056540; -.
H-InvDB HIX0015381; -.
HGNC HGNC:3482; ETFB.
GenAtlas ETFB.
MIM 130410; gene. [NCBI / EBI]
231680; phenotype. [NCBI / EBI]
Orphanet 25; Glutaryl-CoA dehydrogenase deficiency.
26791; Multiple FAD dehydrogenase deficiency.
PharmGKB PA27898; -.
Gene expression databases
ArrayExpress P38117; -.
Bgee P38117; -.
CleanEx HS_ETFB; -.
GermOnline ENSG00000105379; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (traceable author statement from ProtInc).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from ProtInc).
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 IPR014730; ETF_a/b_N.
IPR012255; ETF_b.
IPR000049; ETF_b_core.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
PANTHER PTHR21294; Beta-ETF; 1.
Pfam PF01012; ETF; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000090; Beta-ETF; 1.
ProDom PD003528; ETF_beta; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS01065; ETF_BETA; 1.
Proteomic databases
PeptideAtlas P38117; -.
PRIDE P38117; -.
Genome annotation databases
Ensembl ENSG00000105379; Homo sapiens. [Contig view]
GeneID 2109; -.
Phylogenomic databases
HOVERGEN P38117; -.
OMA P38117; KNEAGVI.
Other
NextBio 8527; -.
SOURCE ETFB; Homo sapiens.
ProtoNet P38117.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Disease mutation; Electron transport; FAD; Flavoprotein; Glutaricaciduria; Mitochondrion; Polymorphism; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   255  254     Electron transfer flavoprotein subunit beta. PRO_0000167870
MOD_RES   2     2        N-acetylalanine (By similarity). 
VAR_SEQ   1    19        MAELRVLVAVKRVIDYAVK -> MYLSLWVTINTVNLRNTLSGLRGAVTTVGMIKSDVPGTQE WLDERRRQGDLPLPTNSNPVLSLELCDPGQGPAPFQAVVV LIQPGRGLALRPPPSCLFPPDPTPSPPAGQ (in isoform 2). VSP_017850
VARIANT   128   128  1     D -> N (in GA2B). VAR_025804 [3D]
VARIANT   154   154  1     T -> M (in dbSNP:rs1130426 [NCBI]). VAR_008548 [3D]
VARIANT   164   164  1     R -> Q (in GA2B). VAR_002369 [3D]
CONFLICT   198   198        I -> S (in Ref. 3). 
STRAND   5     9  5      
STRAND   12    14  3      
STRAND   26    29  4      
STRAND   36    38  3      
HELIX   40    54  15      
STRAND   59    68  10      
HELIX   71    81  11      
STRAND   84    90  7      
HELIX   93    96  4      
HELIX   101   115  15      
STRAND   118   124  7      
TURN   127   129  3      
HELIX   134   142  9      
STRAND   146   156  11      
STRAND   159   166  8      
STRAND   169   183  15      
HELIX   185   187  3      
HELIX   195   200  6      
TURN   201   203  3      
STRAND   206   209  4      
HELIX   211   214  4      
STRAND   221   228  8      
HELIX   242   251  10      
Sequence information
Length: 255 AA [This is the length of the unprocessed precursor] Molecular weight: 27844 Da [This is the MW of the unprocessed precursor] CRC64: 47E6EAEF50EB2C80 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAELRVLVAV KRVIDYAVKI RVKPDRTGVV TDGVKHSMNP FCEIAVEEAV RLKEKKLVKE 

        70         80         90        100        110        120 
VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPPAEAERLG PLQVARVLAK LAEKEKVDLV 

       130        140        150        160        170        180 
LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA SQVTLEGDKL KVEREIDGGL ETLRLKLPAV 

       190        200        210        220        230        240 
VTADLRLNEP RYATLPNIMK AKKKKIEVIK PGDLGVDLTS KLSVISVEDP PQRTAGVKVE 

       250 
TTEDLVAKLK EIGRI 

P38117 in FASTA format

View entry in raw text format (no links)
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