ID A0A3B4WKG2_SERLL Unreviewed; 273 AA.
AC A0A3B4WKG2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Elongation of very long chain fatty acids protein 6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03206};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE AltName: Full=ELOVL fatty acid elongase 6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE Short=ELOVL FA elongase 6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 6 {ECO:0000256|HAMAP-Rule:MF_03206};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 6 {ECO:0000256|HAMAP-Rule:MF_03206};
GN Name=ELOVL6 {ECO:0000256|HAMAP-Rule:MF_03206};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000004946.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000004946.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 elongates fatty acids with
CC 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs.
CC Catalyzes the synthesis of unsaturated C16 long chain fatty acids and,
CC to a lesser extent, C18:0 and those with low desaturation degree. May
CC participate to the production of saturated and monounsaturated VLCFAs
CC of different chain lengths that are involved in multiple biological
CC processes as precursors of membrane lipids and lipid mediators.
CC {ECO:0000256|HAMAP-Rule:MF_03206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-
CC octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555;
CC Evidence={ECO:0000256|ARBA:ARBA00001297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000256|ARBA:ARBA00001297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-
CC oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011;
CC Evidence={ECO:0000256|ARBA:ARBA00001347};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000256|ARBA:ARBA00001347};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-
CC 3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012;
CC Evidence={ECO:0000256|ARBA:ARBA00000592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000256|ARBA:ARBA00000592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:74054; Evidence={ECO:0000256|ARBA:ARBA00001158};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000256|ARBA:ARBA00001158};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71407;
CC Evidence={ECO:0000256|ARBA:ARBA00001211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000256|ARBA:ARBA00001211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:39167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57349,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000256|ARBA:ARBA00001634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168;
CC Evidence={ECO:0000256|ARBA:ARBA00001634};
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; Evidence={ECO:0000256|HAMAP-Rule:MF_03206,
CC ECO:0000256|RuleBase:RU361115};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + malonyl-CoA = 3-oxotetradecanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:60140, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:62543;
CC Evidence={ECO:0000256|ARBA:ARBA00001237};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60141;
CC Evidence={ECO:0000256|ARBA:ARBA00001237};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_03206}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03206}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03206}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- PTM: N-Glycosylated. {ECO:0000256|HAMAP-Rule:MF_03206}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL6 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03206}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03206}.
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DR AlphaFoldDB; A0A3B4WKG2; -.
DR STRING; 1841481.ENSSLDP00000004946; -.
DR Ensembl; ENSSLDT00000005106.1; ENSSLDP00000004946.1; ENSSLDG00000003931.1.
DR GeneTree; ENSGT01050000244965; -.
DR OrthoDB; 2312411at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IEA:InterPro.
DR HAMAP; MF_03206; VLCF_elongase_6; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033675; ELOVL6.
DR PANTHER; PTHR11157:SF175; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03206};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03206};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03206};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP-
KW Rule:MF_03206};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03206,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03206,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03206};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03206};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03206};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03206}.
FT TRANSMEM 39..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 68..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 167..188
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 200..225
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 237..256
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
SQ SEQUENCE 273 AA; 31387 MW; 7E26497837D26F5B CRC64;
MLQVNGTDFH LPLSEYSFER RFDERGAIEW MQANWSKSFV FSALYAALVF GGQHYMKPRP
KMNLRRPLVL WSLSLALFSI VGAVRTGSYM IHILSSSGFR QSICDQSFYS GPVSKFWAYA
FVLSKAPELG DTAFVVLRKQ KLLFLHWYHH ITVLLYSWYS YKDMVAGGGW FMTMNYAVHA
LMYSYYALRA AGLRVPRPFA VLITSAQISQ MAMGLTVSGL VYRWMQAGDC PSHIDNIAWA
ALMYLSYLLL FSNFFYQTYL RRRGAEAKTS KTD
//
