ID ELOV6_RAT Reviewed; 267 AA.
AC Q920L6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 125.
DE RecName: Full=Very long chain fatty acid elongase 6 {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:12005057, ECO:0000269|PubMed:20228221};
DE AltName: Full=3-keto acyl-CoA synthase Elovl6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=ELOVL fatty acid elongase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE Short=ELOVL FA elongase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=Elongation of very long chain fatty acids protein 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=Fatty acid elongase 2;
DE Short=rELO2;
DE AltName: Full=Fatty acyl-CoA elongase;
DE AltName: Full=Long-chain fatty-acyl elongase;
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 6 {ECO:0000255|HAMAP-Rule:MF_03206};
GN Name=Elovl6 {ECO:0000255|HAMAP-Rule:MF_03206}; Synonyms=Face, Lce;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=12005057; DOI=10.1271/bbb.66.613;
RA Inagaki K., Aki T., Fukuda Y., Kawamoto S., Shigeta S., Ono K., Suzuki O.;
RT "Identification and expression of a rat fatty acid elongase involved in the
RT biosynthesis of C18 fatty acids.";
RL Biosci. Biotechnol. Biochem. 66:613-621(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=20228221; DOI=10.1194/jlr.m004747;
RA Green C.D., Ozguden-Akkoc C.G., Wang Y., Jump D.B., Olson L.K.;
RT "Role of fatty acid elongases in determination of de novo synthesized
RT monounsaturated fatty acid species.";
RL J. Lipid Res. 51:1871-1877(2010).
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 in 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:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:12005057,
CC ECO:0000269|PubMed:20228221}.
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:0000255|HAMAP-Rule:MF_03206,
CC ECO:0000269|PubMed:12005057, ECO:0000269|PubMed:20228221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000269|PubMed:20228221};
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:0000269|PubMed:20228221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000269|PubMed:20228221};
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:0000250|UniProtKB:Q920L5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
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:0000250|UniProtKB:Q920L5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60141;
CC Evidence={ECO:0000250|UniProtKB:Q920L5};
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:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
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:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
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:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
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:0000250|UniProtKB:Q9H5J4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000250|UniProtKB:Q9H5J4};
CC -!- ACTIVITY REGULATION: The reaction is stimulated by the presence of
CC HSD17B12, the enzyme catalyzing the second step of the elongation
CC cycle. {ECO:0000250|UniProtKB:Q9H5J4}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03206, ECO:0000269|PubMed:20228221}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03206}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03206}.
CC -!- TISSUE SPECIFICITY: Expressed in liver and barely in brain.
CC {ECO:0000269|PubMed:12005057}.
CC -!- PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03206}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03206}.
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DR EMBL; AB071986; BAB69888.1; -; mRNA.
DR RefSeq; NP_599210.1; NM_134383.2.
DR RefSeq; XP_008759707.1; XM_008761485.1.
DR RefSeq; XP_017452388.1; XM_017596899.1.
DR AlphaFoldDB; Q920L6; -.
DR SMR; Q920L6; -.
DR STRING; 10116.ENSRNOP00000014155; -.
DR SwissLipids; SLP:000000453; -.
DR GlyCosmos; Q920L6; 1 site, No reported glycans.
DR GlyGen; Q920L6; 1 site.
DR PhosphoSitePlus; Q920L6; -.
DR PaxDb; 10116-ENSRNOP00000014155; -.
DR Ensembl; ENSRNOT00000014155.6; ENSRNOP00000014155.2; ENSRNOG00000048949.2.
DR Ensembl; ENSRNOT00055047384; ENSRNOP00055038964; ENSRNOG00055027369.
DR Ensembl; ENSRNOT00060004180; ENSRNOP00060002945; ENSRNOG00060002609.
DR Ensembl; ENSRNOT00065023521; ENSRNOP00065018294; ENSRNOG00065014253.
DR GeneID; 171402; -.
DR KEGG; rno:171402; -.
DR UCSC; RGD:620585; rat.
DR AGR; RGD:620585; -.
DR CTD; 79071; -.
DR RGD; 620585; Elovl6.
DR eggNOG; KOG3072; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_1_1_1; -.
DR InParanoid; Q920L6; -.
DR OMA; EWVPISL; -.
DR OrthoDB; 2312411at2759; -.
DR PhylomeDB; Q920L6; -.
DR TreeFam; TF106467; -.
DR Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q920L6; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010468; Expressed in duodenum and 13 other cell types or tissues.
DR Genevisible; Q920L6; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0009923; C:fatty acid elongase complex; ISO:RGD.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; ISO:RGD.
DR GO; GO:0009922; F:fatty acid elongase activity; IDA:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; ISO:RGD.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IDA:UniProtKB.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IDA:UniProtKB.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISS:UniProtKB.
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; ISS:YuBioLab.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..267
FT /note="Very long chain fatty acid elongase 6"
FT /id="PRO_0000282847"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03206"
SQ SEQUENCE 267 AA; 31624 MW; 4026C9CB33ED0743 CRC64;
MNMSVLTLQE YEFEKQFNEN EAIQWMQENW KKSFLFSALY AAFIFGGRHL MNKRAKFELR
KPLVLWSLTL AVFSIFGALR TGAYMLYILM TKGLKQSVCD QSFYNGPVSK FWAYAFVLSK
APELGDTIFI ILRKQKLIFL HWYHHITVLL YSWYSYKDMV AGGGWFMTMN YGVHAVMYSY
YALRAAGFRV SRKFAMFITL SQITQMLMGC VINYLVFNWM QHDNDQCYSH FQNIFWSSLM
YLSYLLLFCH FFFEAYIGKV KKATKAE
//
