Very-long-chain enoyl-CoA reductase (TECR)
The protein contains 308 amino acids for an estimated molecular weight of 36034 Da.
Involved in both the production of very long-chain fatty acids for sphingolipid synthesis and the degradation of the sphingosine moiety in sphingolipids through the sphingosine 1-phosphate metabolic pathway (PubMed:25049234). Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle (PubMed:12482854). This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle (PubMed:12482854). This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation (PubMed:12482854). Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators (PubMed:12482854). Catalyzes the saturation step of the sphingosine 1-phosphate metabolic pathway, the conversion of trans-2-hexadecenoyl-CoA to palmitoyl-CoA (PubMed:25049234). (updated: July 3, 2019)
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.
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.
(right-click above to access to more options from the contextual menu)
| Variant | Description |
|---|---|
| MRT14 |
Biological Process
Fatty acid elongation
Long-chain fatty-acyl-CoA biosynthetic process
Sphingolipid metabolic process
Very long-chain fatty acid biosynthetic process
The reference OMIM entry for this protein is 610057
Trans-2,3-enoyl-coa reductase; tecr
Glycoprotein, synaptic, 2; gpsn2
Ter
Sc2
DESCRIPTION
Microsomal long and very long chain fatty acid elongation uses malonyl-CoA as the 2-carbon donor and consists of 4 sequential reactions. TECR catalyzes the final step, reducing trans-2,3-enoyl-CoA to saturated acyl-CoA (Moon and Horton, 2003).CLONING
By sequencing cDNAs obtained from umbilical cord blood CD34 (142230)-positive hematopoietic stem/progenitor cells, Mao et al. (1998) identified TECR, which they called GPSN2. By searching databases for homologs of yeast Tsc13, followed by PCR of a human adipose tissue cDNA library, Moon and Horton (2003) cloned TECR, which they called TER. The deduced 308-amino acid protein contains 5 transmembrane domains. It shares 95% amino acid identity with mouse Tecr and 34% identity with yeast Tsc13. Northern blot analysis detected a 1.2-kb transcript in all human and mouse tissues examined. Epitope-tagged TECR colocalized predominantly with long chain fatty acid elongase (ELOVL6; 611546) in the endoplasmic reticulum of transfected Chinese hamster ovary cells. A small amount colocalized with GM130 (GOLGA2; 602580) in the Golgi. Abe et al. (2013) stated that, based on the structures of yeast and Arabidopsis homologs, TECR is likely to be an integral endoplasmic reticulum (ER) membrane protein with 6 membrane-spanning domains, 3 luminal loops, and cytosolic N and C termini.GENE STRUCTURE
Caliskan et al. (2011) determined that the TECR gene contains 13 exons.MAPPING
Caliskan et al. (2011) stated that the TECR gene maps to chromosome 19p13. Hartz (2015) mapped the TECR gene to chromosome 19q13.12 based on an alignment of the TECR sequence (GenBank GENBANK AF038958) with the genomic sequence (GRCh38).GENE FUNCTION
Moon and Horton (2003) found that cotransfection of TECR with ELOVL6 in human embryonic kidney cells resulted in the disappearance of trans-2,3-stearoyl-CoA, indicating that TECR is a trans-2,3-enoyl-CoA reductase. They confirmed this finding by RNA interference experiments in human hepatoma cells.MOLECULAR GENETICS
In all affected members of a large Hutterite family in which autosomal recessive nonsyndromic mental retardation was mapped by Nolan et al. (2008) to chromosome 19p13, Caliskan et al. (2011) detected a homozygous pro182-to-leu mutation in the TECR gene (610057.0001). ... More on the omim web site
July 4, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Nov. 17, 2018: Protein entry updated
Automatic update: OMIM entry 610057 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).