Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial (ECH1)
The protein contains 328 amino acids for an estimated molecular weight of 35816 Da.
Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs9419 | |
| dbSNP:rs2229259 |
Cellular Component
Cytosol
Extracellular exosome
Membrane
Mitochondrion
Peroxisomal matrix
Peroxisome
The reference OMIM entry for this protein is 600696
Enoyl-coa hydratase 1, peroxisomal; ech1
Delta-3,5-delta-2,4-dienoyl coa isomerase
CLONING
Certain hypolipidemic agents ('cholesterol-lowering agents'), e.g., fibrates, and industrial plasticizers are known to activate the transcription of genes encoding proteins involved in peroxisomal beta-oxidation and to induce peroxisome proliferation in rodent hepatocytes. The molecular basis of the transcriptional response to these agents involves their interaction with peroxisome proliferator-activated receptors (PPARs) that bind as homo- or heterodimers to a peroxisomal proliferator response element (PPRE) identified in the promoter region of several upregulated genes. As a means of identifying new genes involved in peroxisomal biogenesis and function, FitzPatrick et al. (1995) used a subtractive hybridization method to identify cDNAs that were transcriptionally activated by treatment of rats with peroxisome proliferators. They identified a novel rat liver cDNA encoding Ech1, which was induced more than 20-fold. Using rat Ech1 as probe, FitzPatrick et al. (1995) cloned ECH1 from a human retina cDNA library. The deduced 329-amino acid protein shares sequence similarity with enoyl-CoA hydratases of several species, and it has a C-terminal SKL peroxisome targeting signal. Rat and human ECH1 share 74% amino acid identity. Northern blot analysis detected a 1.4-kb transcript in all human tissues and cell lines examined, with highest expression in skeletal muscle. Epitope-tagged ECH1 was targeted to peroxisomes in transfected HEK293 cells. Filppula et al. (1998) found that rat Ech1 has an N-terminal mitochondrial targeting signal, in addition to a C-terminal peroxisomal targeting signal. Subcellular fractionation and electron microscopy of rat liver localized Ech1 to the matrix of both mitochondria and peroxisomes.GENE FUNCTION
Using recombinant rat protein, Filppula et al. (1998) found that Ech1 did not function as an enoyl-CoA hydratase, but instead isomerized double bonds in a fatty acid substrate. With the substrate 3,5,8,11,14-eicosapentenoyl-CoA, Ech1 switched the double bonds from delta-3,5 to delta-2,4, creating a substrate for 2,4-dienoyl-CoA reductase (DECR1; 222745).MAPPING
FitzPatrick et al. (1995) mapped the human ECH1 gene to chromosome 19q13.1 by Southern blot analysis of rodent/human somatic cell hybrids containing different combinations of human chromosomes followed by hybridization to high-density filter arrays of chromosome 19-specific cosmids. The human ECH1 gene was found to map to a contig 3-prime to the ryanodine receptor (RYR1; 180901). ... More on the omim web site
Feb. 23, 2019: Protein entry updated
Automatic update: comparative model was added.
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: OMIM entry 600696 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).