ELOV6_HUMAN
ID ELOV6_HUMAN Reviewed; 265 AA.
AC Q9H5J4; Q4W5L0; Q8NCD1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Elongation of very long chain fatty acids protein 6 {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:25003994};
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=Fatty acid elongase 2;
DE Short=hELO2;
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19575253; DOI=10.1007/s11745-009-3320-8;
RA Kitazawa H., Miyamoto Y., Shimamura K., Nagumo A., Tokita S.;
RT "Development of a high-density assay for long-chain fatty acyl-CoA
RT elongases.";
RL Lipids 44:765-773(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=20937905; DOI=10.1073/pnas.1005572107;
RA Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y.,
RA Sassa T., Kihara A.;
RT "ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
RT synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND GLYCOSYLATION.
RX PubMed=25003994; DOI=10.1371/journal.pone.0101823;
RA Naganuma T., Kihara A.;
RT "Two modes of regulation of the fatty acid elongase ELOVL6 by the 3-
RT ketoacyl-CoA reductase KAR in the fatty acid elongation cycle.";
RL PLoS ONE 9:E101823-E101823(2014).
RN [7]
RP FUNCTION.
RX PubMed=26214738; DOI=10.1038/nature14601;
RA Senyilmaz D., Virtue S., Xu X., Tan C.Y., Griffin J.L., Miller A.K.,
RA Vidal-Puig A., Teleman A.A.;
RT "Regulation of mitochondrial morphology and function by stearoylation of
RT TFR1.";
RL Nature 525:124-128(2015).
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:19575253,
CC ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:25003994,
CC ECO:0000269|PubMed:26214738}.
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:19575253, ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:25003994};
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:19575253, ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:25003994};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000305|PubMed:20937905};
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:Q920L5};
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:0000269|PubMed:19575253};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168;
CC Evidence={ECO:0000305|PubMed:19575253};
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:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:25003994}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.22 uM for hexadecanoyl-CoA (at 37 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:25003994};
CC Vmax=0.79 pmol/min/ug enzyme with hexadecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:25003994};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03206, ECO:0000269|PubMed:20937905}.
CC -!- INTERACTION:
CC Q9H5J4; P09601: HMOX1; NbExp=3; IntAct=EBI-12821617, EBI-2806151;
CC Q9H5J4; Q13094: LCP2; NbExp=3; IntAct=EBI-12821617, EBI-346946;
CC Q9H5J4; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-12821617, EBI-10244780;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03206, ECO:0000269|PubMed:20937905}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03206}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:20937905}.
CC -!- PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03206,
CC ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:25003994}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03206}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11225.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK074813; BAC11225.1; ALT_INIT; mRNA.
DR EMBL; AK027031; BAB15632.1; -; mRNA.
DR EMBL; AC004050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093770; AAY40928.1; -; Genomic_DNA.
DR EMBL; BC001305; AAH01305.1; -; mRNA.
DR CCDS; CCDS3690.1; -.
DR RefSeq; NP_001124193.1; NM_001130721.1.
DR RefSeq; NP_076995.1; NM_024090.2.
DR RefSeq; XP_011530535.1; XM_011532233.2.
DR RefSeq; XP_011530536.1; XM_011532234.2.
DR AlphaFoldDB; Q9H5J4; -.
DR SMR; Q9H5J4; -.
DR BioGRID; 122522; 7.
DR IntAct; Q9H5J4; 5.
DR STRING; 9606.ENSP00000378105; -.
DR BindingDB; Q9H5J4; -.
DR ChEMBL; CHEMBL5704; -.
DR SwissLipids; SLP:000000254; -.
DR GlyGen; Q9H5J4; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H5J4; -.
DR PhosphoSitePlus; Q9H5J4; -.
DR BioMuta; ELOVL6; -.
DR DMDM; 74733585; -.
DR EPD; Q9H5J4; -.
DR MassIVE; Q9H5J4; -.
DR MaxQB; Q9H5J4; -.
DR PaxDb; Q9H5J4; -.
DR PeptideAtlas; Q9H5J4; -.
DR PRIDE; Q9H5J4; -.
DR ProteomicsDB; 80915; -.
DR Antibodypedia; 26395; 203 antibodies from 33 providers.
DR DNASU; 79071; -.
DR Ensembl; ENST00000302274.8; ENSP00000304736.3; ENSG00000170522.10.
DR Ensembl; ENST00000394607.7; ENSP00000378105.3; ENSG00000170522.10.
DR GeneID; 79071; -.
DR KEGG; hsa:79071; -.
DR MANE-Select; ENST00000302274.8; ENSP00000304736.3; NM_024090.3; NP_076995.1.
DR UCSC; uc003hzz.4; human.
DR CTD; 79071; -.
DR DisGeNET; 79071; -.
DR GeneCards; ELOVL6; -.
DR HGNC; HGNC:15829; ELOVL6.
DR HPA; ENSG00000170522; Tissue enhanced (liver).
DR MIM; 611546; gene.
DR neXtProt; NX_Q9H5J4; -.
DR OpenTargets; ENSG00000170522; -.
DR PharmGKB; PA134939058; -.
DR VEuPathDB; HostDB:ENSG00000170522; -.
DR eggNOG; KOG3072; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_1_1_1; -.
DR InParanoid; Q9H5J4; -.
DR OMA; PISWVPI; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9H5J4; -.
DR TreeFam; TF106467; -.
DR BioCyc; MetaCyc:HS10142-MON; -.
DR BRENDA; 2.3.1.16; 2681.
DR BRENDA; 2.3.1.199; 2681.
DR PathwayCommons; Q9H5J4; -.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; Q9H5J4; -.
DR SIGNOR; Q9H5J4; -.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 79071; 12 hits in 1079 CRISPR screens.
DR GenomeRNAi; 79071; -.
DR Pharos; Q9H5J4; Tchem.
DR PRO; PR:Q9H5J4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9H5J4; protein.
DR Bgee; ENSG00000170522; Expressed in right lobe of liver and 163 other tissues.
DR ExpressionAtlas; Q9H5J4; baseline and differential.
DR Genevisible; Q9H5J4; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0009923; C:fatty acid elongase complex; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0009922; F:fatty acid elongase activity; IMP:UniProtKB.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
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; PTHR11157; 1.
DR PANTHER; PTHR11157:SF125; PTHR11157:SF125; 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..265
FT /note="Elongation of very long chain fatty acids protein 6"
FT /id="PRO_0000282845"
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 232..252
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"
FT CONFLICT 10..11
FT /note="EY -> KN (in Ref. 1; BAC11225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 31376 MW; 01234E0EEF6CE341 CRC64;
MNMSVLTLQE YEFEKQFNEN EAIQWMQENW KKSFLFSALY AAFIFGGRHL MNKRAKFELR
KPLVLWSLTL AVFSIFGALR TGAYMVYILM TKGLKQSVCD QGFYNGPVSK FWAYAFVLSK
APELGDTIFI ILRKQKLIFL HWYHHITVLL YSWYSYKDMV AGGGWFMTMN YGVHAVMYSY
YALRAAGFRV SRKFAMFITL SQITQMLMGC VVNYLVFCWM QHDQCHSHFQ NIFWSSLMYL
SYLVLFCHFF FEAYIGKMRK TTKAE
