HAMAP rule MF_03206

General rule information [?]

Accession	MF_03206
Dates	16-DEC-2013 (Created) 29-SEP-2022 (Last updated, Version 11)
Name	VLCF_elongase_6
Scope(s)	Eukaryota Vertebrata
Template(s)	Q9H5J4 (ELOV6_HUMAN); Q920L5 (ELOV6_MOUSE); Q920L6 (ELOV6_RAT); [ Recover all ]
Triggered by	HAMAP; MF_03206 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier	ELOV6
Protein name	RecName: Full=Elongation of very long chain fatty acids protein 6; EC=2.3.1.199; AltName: Full=3-keto acyl-CoA synthase ; AltName: Full=ELOVL fatty acid elongase 6; Short=ELOVL FA elongase 6; AltName: Full=Very long chain 3-ketoacyl-CoA synthase 6; AltName: Full=Very long chain 3-oxoacyl-CoA synthase 6;
Gene name	Name=ELOVL6;

Comments [?]

FUNCTION	Catalyzes the first and rate-limiting reaction of the four reactions 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.
CATALYTIC ACTIVITY	Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long- chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199;
PATHWAY	Lipid metabolism; fatty acid biosynthesis.
SUBCELLULAR LOCATION	Endoplasmic reticulum membrane; Multi-pass membrane protein.
case <FTTag:ERmotif>
DOMAIN	The C-terminal di-lysine motif may confer endoplasmic reticulum localization.
end case
PTM	N-Glycosylated.
SIMILARITY	Belongs to the ELO family. ELOVL6 subfamily.

Keywords [?]

Gene Ontology [?]

GO:0005789; Cellular component:endoplasmic reticulum membrane

GO:0016020; Cellular component:membrane

GO:0009922; Molecular function:fatty acid elongase activity

GO:0006636; Biological process:unsaturated fatty acid biosynthetic process

GO:0019367; Biological process:fatty acid elongation, saturated fatty acid

GO:0034625; Biological process:fatty acid elongation, monounsaturated fatty acid

GO:0035338; Biological process:long-chain fatty-acyl-CoA biosynthetic process

Cross-references [?]

PROSITE	PS00001; ASN_GLYCOSYLATION; 0-unlimited;
PROSITE	PS01188; ELO; 1;
Pfam	PF01151; ELO; 1;
General	N_glycosylation; NetNGlyc; 0-unlimited;
General	Transmembrane; -; 7;

Features [?]

From: ELOV6_HUMAN (Q9H5J4)

Key

From

Description

Tag

Condition

FTGroup

MOTIF

Cter-3

Cter

/note="Di-lysine motif"

ERmotif

K-x(2)-K>

Additional information [?]