AC MF_03201; DC Protein; auto TR HAMAP; MF_03201; -; 1; level=0 XX Names: VLCF_elongase_1 XX ID ELOV1 DE RecName: Full=Elongation of very long chain fatty acids protein 1; DE EC=2.3.1.199; DE AltName: Full=3-keto acyl-CoA synthase ; DE AltName: Full=ELOVL fatty acid elongase 1; DE Short=ELOVL FA elongase 1; DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 1; DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 1; GN Name=ELOVL1; XX case CC -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four CC reactions that constitute the long-chain fatty acids elongation cycle. CC This endoplasmic reticulum-bound enzymatic process allows the addition CC of 2 carbons to the chain of long- and very long-chain fatty acids CC (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward CC saturated C18 to C26 acyl-CoA substrates, with the highest activity CC towards C22:0 acyl-CoA. May participate to the production of both CC saturated and monounsaturated VLCFAs of different chain lengths that CC are involved in multiple biological processes as precursors of membrane CC lipids and lipid mediators. Important for saturated C24:0 and CC monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits CC @gn(RPE65) via production of VLCFAs. else CC -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four CC reactions that constitute the long-chain fatty acids elongation cycle. CC This endoplasmic reticulum-bound enzymatic process allows the addition CC of 2 carbons to the chain of long- and very long-chain fatty acids CC (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward CC saturated C18 to C26 acyl-CoA substrates, with the highest activity CC towards C22:0 acyl-CoA. May participate to the production of both CC saturated and monounsaturated VLCFAs of different chain lengths that CC are involved in multiple biological processes as precursors of membrane CC lipids and lipid mediators. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long- CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; CC EC=2.3.1.199; case CC -!- SUBUNIT: Interacts with @gn(LASS2), @gn(TECR) and @gn(HSD17B12). end case CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. case CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum CC localization. end case CC -!- SIMILARITY: Belongs to the ELO family. ELOVL1 subfamily. XX DR PROSITE; PS01188; ELO; 1; trigger=no DR Pfam; PF01151; ELO; 1; trigger=no DR General; Transmembrane; -; 7; trigger=yes XX KW Endoplasmic reticulum KW Fatty acid biosynthesis KW Fatty acid metabolism KW Lipid biosynthesis KW Lipid metabolism KW Membrane KW Transferase XX GO GO:0005789; C:endoplasmic reticulum membrane GO GO:0016020; C:membrane GO GO:0009922; F:fatty acid elongase activity GO GO:0006636; P:unsaturated fatty acid biosynthetic process GO GO:0019367; P:fatty acid elongation, saturated fatty acid GO GO:0034625; P:fatty acid elongation, monounsaturated fatty acid GO GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process GO GO:0042761; P:very long-chain fatty acid biosynthetic process XX FT From: ELOV1_HUMAN (Q9BW60) FT MOTIF Cter-4..Cter FT /note="Di-lysine motif" FT Tag: ERmotif; Condition: K-x-K-x(2)> XX Size: 276-368; Related: MF_03204; MF_03207; Template: Q9BW60; Q9JLJ5; Scope: Eukaryota; Vertebrata Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.14 2022/09/29 //