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Overview

Uniprot IDQ9NZ01
Protein NameVery-long-chain enoyl-CoA reductase
Gene NameTECR
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
12 EVEILDAKTREKLCF
16 LDAKTREKLCFLDKV
2 ******MKHYEVEIL
224 DLRPAGSKTRKIPYP
38 EIKNLFTKTHPQWYP
57 LRLDPKGKSLKDEDV

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 (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)

Protein Sequence

10 MKHYEVEILD 20 AKTREKLCFL 30 DKVEPHATIA 40 EIKNLFTKTH 50 PQWYPARQSL 60 RLDPKGKSLK 70 DEDVLQKLPV 80 GTTATLYFRD 90 LGAQISWVTV 100 FLTEYAGPLF 110 IYLLFYFRVP 120 FIYGHKYDFT 130 SSRHTVVHLA 140 CICHSFHYIK 150 RLLETLFVHR 160 FSHGTMPLRN 170 IFKNCTYYWG 180 FAAWMAYYIN 190 HPLYTPPTYG 200 AQQVKLALAI 210 FVICQLGNFS 220 IHMALRDLRP 230 AGSKTRKIPY 240 PTKNPFTWLF 250 LLVSCPNYTY 260 EVGSWIGFAI 270 MTQCLPVALF 280 SLVGFTQMTI 290 WAKGKHRSYL 300 KEFRDYPPLR MPIIPFLL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0005634 nucleus
Molecular Function GO:0102758 very-long-chain enoyl-CoA reductase activity
Molecular Function GO:0017099 very-long-chain fatty acyl-CoA dehydrogenase activity
Biological Process GO:0030497 fatty acid elongation
Biological Process GO:0035338 long-chain fatty-acyl-CoA biosynthetic process
Biological Process GO:0006665 sphingolipid metabolic process
Biological Process GO:0042761 very long-chain fatty acid biosynthetic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.