ID A0A2Y9EN91_PHYMC Unreviewed; 265 AA.
AC A0A2Y9EN91;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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,
GN ECO:0000313|RefSeq:XP_007105911.1, ECO:0000313|RefSeq:XP_028347981.1,
GN ECO:0000313|RefSeq:XP_054942149.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007105911.1};
RN [1] {ECO:0000313|RefSeq:XP_007105911.1, ECO:0000313|RefSeq:XP_028347981.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007105911.1,
RC ECO:0000313|RefSeq:XP_028347981.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_007105911.1; XM_007105849.3.
DR RefSeq; XP_007105912.1; XM_007105850.1.
DR RefSeq; XP_028347981.1; XM_028492180.2.
DR RefSeq; XP_054942149.1; XM_055086174.1.
DR STRING; 9755.ENSPCTP00005004715; -.
DR Ensembl; ENSPCTT00005005192; ENSPCTP00005004715; ENSPCTG00005003362.
DR GeneID; 102976400; -.
DR KEGG; pcad:102976400; -.
DR CTD; 79071; -.
DR OrthoDB; 2312411at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000248484; Chromosome 7.
DR GO; GO:0009923; C:fatty acid elongase complex; IEA:Ensembl.
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:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
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:SF125; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 6; 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 Reference proteome {ECO:0000313|Proteomes:UP000248484};
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 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 63..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 139..156
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 162..183
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 195..220
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 232..251
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03206,
FT ECO:0000256|RuleBase:RU361115"
SQ SEQUENCE 265 AA; 31421 MW; DEFE104816813C45 CRC64;
MNMSVLTLQE YEFEKQFNEN EAIQWMQENW KKSFLFSALY AAFIFGGRHL MNKRAKFELR
KPLVLWSLTL AVFSIFGALR TGAYMVYILM TKGLKHSVCD QGFYNGPVSK FWAYAFVLSK
APELGDTIFI ILRKQKLIFL HWYHHITVLL YSWYSYKDMV AGGGWFMTMN YGVHSVMYSY
YALRAAGFRV SRKFAMFITL SQITQMLMGC VVNYLVFHWM QHDQCHSHFQ NIFWSSLMYL
SYLVLFCHFF FEAYIGKMRK TTKAD
//
