SCUBA

FADS3 — Fatty acid desaturase 3

FADS3 belongs to a gene co-expression module in 3 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

FADS3's module in each cell type

Cell typeModuleShares the module with
EndothelialInflammatory Kinase Signaling
Inflammation
ANKRD28, CBL, CDC123, CNN2, DGKH, EOGT, FYN, MAP4K4 +7 moreView in SCUBA
Glial cellsGlial Quiescence State
Development
AATK, CDKN1C, PPP1R10, RGCC, RSRP1, SLC38A2, SOX2, SRSF5View in SCUBA
Smooth muscle cellsNF-kB Stress Response
Stress
BHLHE40, CCNL1, HSP90AB1, IER3, MIDN, NFKBIZ, PPP1R15A, THBS1 +1 moreView in SCUBA

About the gene

SynonymsCYB5RP, LLCDL3
Chromosome11: 61873519-61892051
Predicted locationIntracellular, Membrane
Essential geneNo
Protein classMetabolic proteins, Predicted intracellular proteins, Predicted membrane proteins
Molecular functionOxidoreductase
Biological processElectron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Function

Mammals have different sphingoid bases that differ in their length and/or pattern of desaturation and hydroxyl groups. The predominant sphingoid base that comprises mammalian ceramides is sphing-4-enine (sphingosine or SPH) which has a trans (E) desaturation at carbon 4. FADS3 is a desaturase that introduces a cis (Z) double bond between carbon 14 and carbon 15 of the sphingoid base (also known as long chain base, LCB), producing LCBs such as sphinga-4,14-dienine (SPD, d18:2(4E,14Z)) from SPH. Prefers SPH- containing ceramides (N-acylsphing-4-enines) as substrates. Capable of metabolizing also the SPH in its free form. SPD ceramides occur widely in mammalian tissues and cells. Due to their unusual structure containing a cis double bond, SPD ceramides may have an opposite, negative role in lipid microdomain formation relative to conventional ceramides. Could be involved in the detoxification of 1-deoxy sphingolipids, by desaturating the cytotoxic 1-deoxysphinganine (1- deoxySA, m18:0), produced under pathological conditions, to 1- deoxysphingenine (1-deoxysphingosine, 1-deoxySO, m18:1) (Probable). Although prefers SPH-containing ceramides (N-acylsphing-4-enines) as substrates, it also exhibits activity toward dihydrosphingosine- containing CERs (N-acylsphinganines) and produces 14Z-SPH-containing sphingolipids,which can be found in patients with DEGS1 mutations. Its desaturase mechanism involves an electron transfer facilitated by cytochrome b5. FADS3 also acts as a methyl-end fatty acyl coenzyme A (CoA) desaturase that introduces a cis double bond between the preexisting double bond and the terminal methyl group of the fatty acyl chain (By similarity). Desaturates (11E)-octadecenoate (trans-vaccenoate, the predominant trans fatty acid in human milk) at carbon 13 to generate (11E,13Z)- octadecadienoate (also known as conjugated linoleic acid 11E,13Z-CLA) (By similarity).

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.