AC MF_03204; DC Protein; auto TR HAMAP; MF_03204; -; 1; level=0 XX Names: VLCF_elongase_4 XX ID ELOV4 DE RecName: Full=Elongation of very long chain fatty acids protein 4; DE EC=2.3.1.199; DE AltName: Full=3-keto acyl-CoA synthase ; DE AltName: Full=ELOVL fatty acid elongase 4; DE Short=ELOVL FA elongase 4; DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 4; DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 4; GN Name=ELOVL4; 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 specifically elongates C24:0 CC and C26:0 acyl-CoAs. May participate to the production of saturated and CC monounsaturated VLCFAs of different chain lengths that are involved in CC multiple biological processes as precursors of membrane lipids and CC lipid mediators. May play a critical role in early brain and skin CC development. 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 specifically elongates C24:0 CC and C26:0 acyl-CoAs. May participate to the production of saturated and CC monounsaturated VLCFAs of different chain lengths that are involved in CC multiple biological processes as precursors of membrane lipids and CC 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; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Oligomer. 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. ELOVL4 subfamily. XX DR PROSITE; PS00001; ASN_GLYCOSYLATION; 0-unlimited; trigger=yes DR PROSITE; PS01188; ELO; 1; trigger=no DR Pfam; PF01151; ELO; 1; trigger=no DR General; N_glycosylation; NetNGlyc; 0-unlimited; trigger=yes 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:0034626; P:fatty acid elongation, polyunsaturated 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: ELOV4_HUMAN (Q9GZR5) FT MOTIF Cter-4..Cter FT /note="Di-lysine motif" FT Tag: ERmotif; Condition: K-x-K-x(2)> XX Size: 272-320; Related: MF_03201; MF_03207; Template: Q9GZR5; Scope: Eukaryota; Vertebrata Fusion: Nter: None Cter: None Duplicate: in DANRE, ORENI Plasmid: None Comments: None XX # Revision 1.12 2022/09/29 //