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The Delta4-sphingolipid Fatty Acid Desaturase (Delta4-sphingolipid-FADS)-like CD includes the integral-membrane enzymes, dihydroceramide Delta-4 desaturase, involved in the synthesis of sphingosine; and the human membrane fatty acid (lipid) desaturase (MLD), reported to modulate biosynthesis of the epidermal growth factor receptor; and other related proteins. These proteins are found in various eukaryotes including vertebrates, higher plants, and fungi. Studies show that MLD is localized to the endoplasmic reticulum. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.
No pairwise interactions are available for this conserved domain.
Tips:  If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position. The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs. Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below. Range on the Protein: Protein ID Protein Position Domain Position: 
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