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The annotation and conditions in this rule are derived from the following entries: Q9H5J4 (ELOV6_HUMAN), Q920L5 (ELOV6_MOUSE), Q920L6 (ELOV6_RAT)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position -3 - 0 aligns to "K-x(2)-K>" in entry Q9H5J4
    • Subsequence at position @PLUS|@CTER|-3@ - @CTER@ aligns to "K-x(2)-K>" in entry Q9H5J4
    • Predicted transmembrane

... then these annotations are applied i

Protein namei

  • Recommended name:
    Elongation of very long chain fatty acids protein 6 (EC:2.3.1.199)
    Alternative name(s):
    3-keto acyl-CoA synthase @GENE_NAME@i
    Very long chain 3-ketoacyl-CoA synthase 6
    Very long chain 3-oxoacyl-CoA synthase 6
    ELOVL fatty acid elongase 6
    Short name:
    ELOVL FA elongase 6

Gene namei

  • Name:ELOVL6

Sequence similaritiesi

Catalytic activityi

  • A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.

Pathwayi

  • Pathwayi: fatty acid biosynthesis

    This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Post-translational modificationi

  • N-Glycosylated.

Functioni

  • Catalyzes the first and rate-limiting reaction of the four that constitute 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. Condensing enzyme that elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.

Domaini

  • The C-terminal di-lysine motif may confer endoplasmic reticulum localization.

Subcellular locationi

Transmembranei

  • Helical (to residues corresponding to positions @FROM@i - @TO@i)

Motifi

  • Di-lysine motif (to residues corresponding to positions @PLUS|@CTER|-3@i - @CTER@i)

Keywordsi

GO (Gene Ontology) termsi

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