Overview
| Uniprot ID | A0A5G2QTJ4 |
| Protein Name | Very-long-chain enoyl-CoA reductase |
| Gene Name | TECR |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 248 |
DLRPAGSKTRKIPYP |
| 56 |
LDAKTREKLCFLDKV |
Function
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. Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. 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. 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. 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. Catalyzes the saturation step of the sphingosine 1-phosphate metabolic pathway, the conversion of trans-2-hexadecenoyl-CoA to palmitoyl-CoA
Protein Sequence
10
MDLSMSMVAR
20
ETSQGLGPAF
30
GLNGLPRPAP
40
PKTTKKPKKA
50
VLFFEVEILD
60
AKTREKLCFL
70
DKVEPQATIA
80
EIKNLFTKSH
90
PQWYPARQSL
100
RLDPKGKSLK
110
DEDVLQKLPV
120
GTTATLYFRD
130
LGAQISWVTV
140
FLTEYAGPLF
150
IYLLFYFRVP
160
FIYGHKYDFT
170
SSRHTVVHLA
180
CICHSFHYIK
190
RLLETLFVHR
200
FSHGTMPLRN
210
IFKAFLSASS
220
SAYGAQQVKL
230
ALAIFVICQL
240
GNFSIHMALR
250
DLRPAGSKTR
260
KIPYPTKNPF
270
TWLFLLVSCP
280
NYTYEVGSWI
290
GFAIMTQCLP
300
VALFSLVGFT
310
QMTIWAKGKH
320
RSYLKEFRDY
330
PPLRMPIIPF
LL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005789 |
endoplasmic reticulum membrane |
| Molecular Function |
GO:0102758 |
very-long-chain enoyl-CoA reductase activity |
| Biological Process |
GO:0006633 |
fatty acid biosynthetic process |
| Biological Process |
GO:0006665 |
sphingolipid metabolic process |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.