ELOV7_HUMAN
ID ELOV7_HUMAN Reviewed; 281 AA.
AC A1L3X0; Q589T3; Q9H5D0; Q9NT66;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Elongation of very long chain fatty acids protein 7 {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL7 {ECO:0000255|HAMAP-Rule:MF_03207};
DE AltName: Full=ELOVL fatty acid elongase 7 {ECO:0000255|HAMAP-Rule:MF_03207};
DE Short=ELOVL FA elongase 7 {ECO:0000255|HAMAP-Rule:MF_03207};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 7 {ECO:0000255|HAMAP-Rule:MF_03207};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 7 {ECO:0000255|HAMAP-Rule:MF_03207};
GN Name=ELOVL7 {ECO:0000255|HAMAP-Rule:MF_03207};
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 [MRNA].
RC TISSUE=Prostate;
RA Tamura K., Nakagawa H., Nakamura Y.;
RT "Overexpressed gene in prostate cancer.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-281.
RC TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-281.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION.
RX PubMed=19826053; DOI=10.1158/0008-5472.can-09-0775;
RA Tamura K., Makino A., Hullin-Matsuda F., Kobayashi T., Furihata M.,
RA Chung S., Ashida S., Miki T., Fujioka T., Shuin T., Nakamura Y.,
RA Nakagawa H.;
RT "Novel lipogenic enzyme ELOVL7 is involved in prostate cancer growth
RT through saturated long-chain fatty acid metabolism.";
RL Cancer Res. 69:8133-8140(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP 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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF HIS-150 AND HIS-151.
RX PubMed=21959040; DOI=10.1016/j.febslet.2011.09.024;
RA Naganuma T., Sato Y., Sassa T., Ohno Y., Kihara A.;
RT "Biochemical characterization of the very long-chain fatty acid elongase
RT ELOVL7.";
RL FEBS Lett. 585:3337-3341(2011).
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 with higher activity toward C18
CC acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also
CC active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly
CC toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or
CC C26:0-CoAs. May participate in the production of saturated and
CC polyunsaturated VLCFAs of different chain lengths that are involved in
CC multiple biological processes as precursors of membrane lipids and
CC lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03207,
CC ECO:0000269|PubMed:19826053, ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:21959040}.
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_03207,
CC ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000305|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + malonyl-CoA = 3-oxodocosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:35327, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71451;
CC Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328;
CC Evidence={ECO:0000305|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA =
CC (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:73852; Evidence={ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000305|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:71481; Evidence={ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380;
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, ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000305|PubMed:20937905};
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, ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000305|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + octadecanoyl-CoA = 3-oxoeicosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:35319, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65115;
CC Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35320;
CC Evidence={ECO:0000305|PubMed:20937905};
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:20937905, ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
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 ECO:0000269|PubMed:21959040};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000305|PubMed:20937905};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for (9Z,12Z,15Z)-octadecatrienoyl-CoA/C18:3(n-3)-CoA
CC {ECO:0000269|PubMed:21959040};
CC KM=11.7 uM for malonyl-CoA {ECO:0000269|PubMed:21959040};
CC Vmax=0.33 pmol/min/ug enzyme with (9Z,12Z,15Z)-octadecatrienoyl-
CC CoA/C18:3(n-3)-CoA as substrate {ECO:0000269|PubMed:21959040};
CC Vmax=0.31 pmol/min/ug enzyme with malonyl-CoA as substrate
CC {ECO:0000269|PubMed:21959040};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03207, ECO:0000269|PubMed:20937905,
CC ECO:0000269|PubMed:21959040}.
CC -!- INTERACTION:
CC A1L3X0; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-10285373, EBI-11277970;
CC A1L3X0; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-10285373, EBI-465804;
CC A1L3X0; P54852: EMP3; NbExp=3; IntAct=EBI-10285373, EBI-3907816;
CC A1L3X0; O75427: LRCH4; NbExp=3; IntAct=EBI-10285373, EBI-718707;
CC A1L3X0; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-10285373, EBI-10244780;
CC A1L3X0; O75920: SERF1B; NbExp=3; IntAct=EBI-10285373, EBI-2115181;
CC A1L3X0; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-10285373, EBI-12266234;
CC A1L3X0; P57105: SYNJ2BP; NbExp=3; IntAct=EBI-10285373, EBI-1049004;
CC A1L3X0; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-10285373, EBI-2339195;
CC A1L3X0; Q8N2K1: UBE2J2; NbExp=3; IntAct=EBI-10285373, EBI-2340110;
CC A1L3X0; P23763-3: VAMP1; NbExp=3; IntAct=EBI-10285373, EBI-12097582;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:20937905}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues except heart and skeletal
CC muscle. {ECO:0000269|PubMed:20937905}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000255|HAMAP-Rule:MF_03207}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL7 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03207}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15697.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15697.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15697.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB181393; BAD93238.1; -; mRNA.
DR EMBL; BC130310; AAI30311.1; -; mRNA.
DR EMBL; BC130312; AAI30313.1; -; mRNA.
DR EMBL; AK027216; BAB15697.1; ALT_SEQ; mRNA.
DR EMBL; AL137506; CAB70777.1; -; mRNA.
DR CCDS; CCDS34164.1; -.
DR PIR; T46257; T46257.
DR RefSeq; NP_001098028.1; NM_001104558.1.
DR RefSeq; NP_001284546.1; NM_001297617.1.
DR RefSeq; NP_001284547.1; NM_001297618.1.
DR RefSeq; NP_079206.2; NM_024930.2.
DR RefSeq; XP_005248663.1; XM_005248606.4.
DR RefSeq; XP_006714758.1; XM_006714695.3.
DR RefSeq; XP_011541953.1; XM_011543651.2.
DR RefSeq; XP_016865374.1; XM_017009885.1.
DR PDB; 6Y7F; X-ray; 2.05 A; A/B=1-281.
DR PDBsum; 6Y7F; -.
DR AlphaFoldDB; A1L3X0; -.
DR SMR; A1L3X0; -.
DR BioGRID; 123056; 22.
DR IntAct; A1L3X0; 13.
DR STRING; 9606.ENSP00000424123; -.
DR SwissLipids; SLP:000000250; -.
DR iPTMnet; A1L3X0; -.
DR PhosphoSitePlus; A1L3X0; -.
DR BioMuta; ELOVL7; -.
DR EPD; A1L3X0; -.
DR MassIVE; A1L3X0; -.
DR MaxQB; A1L3X0; -.
DR PaxDb; A1L3X0; -.
DR PeptideAtlas; A1L3X0; -.
DR PRIDE; A1L3X0; -.
DR ProteomicsDB; 143; -.
DR Antibodypedia; 23642; 154 antibodies from 24 providers.
DR DNASU; 79993; -.
DR Ensembl; ENST00000425382.5; ENSP00000402634.1; ENSG00000164181.14.
DR Ensembl; ENST00000508821.6; ENSP00000424123.1; ENSG00000164181.14.
DR GeneID; 79993; -.
DR KEGG; hsa:79993; -.
DR MANE-Select; ENST00000508821.6; ENSP00000424123.1; NM_024930.3; NP_079206.2.
DR UCSC; uc003jsi.5; human.
DR CTD; 79993; -.
DR DisGeNET; 79993; -.
DR GeneCards; ELOVL7; -.
DR HGNC; HGNC:26292; ELOVL7.
DR HPA; ENSG00000164181; Low tissue specificity.
DR MIM; 614451; gene.
DR neXtProt; NX_A1L3X0; -.
DR OpenTargets; ENSG00000164181; -.
DR PharmGKB; PA134934034; -.
DR VEuPathDB; HostDB:ENSG00000164181; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR InParanoid; A1L3X0; -.
DR OMA; YKAKYLN; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; A1L3X0; -.
DR TreeFam; TF323454; -.
DR BioCyc; MetaCyc:ENSG00000164181-MON; -.
DR BRENDA; 2.3.1.199; 2681.
DR PathwayCommons; A1L3X0; -.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SABIO-RK; A1L3X0; -.
DR SignaLink; A1L3X0; -.
DR SIGNOR; A1L3X0; -.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 79993; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; ELOVL7; human.
DR GenomeRNAi; 79993; -.
DR Pharos; A1L3X0; Tbio.
DR PRO; PR:A1L3X0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A1L3X0; protein.
DR Bgee; ENSG00000164181; Expressed in upper arm skin and 161 other tissues.
DR ExpressionAtlas; A1L3X0; baseline and differential.
DR Genevisible; A1L3X0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0009922; F:fatty acid elongase activity; EXP:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IDA:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
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; IDA:UniProtKB.
DR HAMAP; MF_03207; VLCF_elongase_7; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033670; ELOVL7.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR PANTHER; PTHR11157:SF118; PTHR11157:SF118; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..281
FT /note="Elongation of very long chain fatty acids protein 7"
FT /id="PRO_0000311988"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT MOTIF 277..281
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT MUTAGEN 150
FT /note="H->A: Loss of activity; when associated with A-151."
FT /evidence="ECO:0000269|PubMed:21959040"
FT MUTAGEN 151
FT /note="H->A: Loss of activity; when associated with A-150."
FT /evidence="ECO:0000269|PubMed:21959040"
FT CONFLICT 16
FT /note="N -> K (in Ref. 3; BAB15697)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="Q -> H (in Ref. 3; BAB15697)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="V -> E (in Ref. 3; BAB15697)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="S -> C (in Ref. 3; BAB15697)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="L -> P (in Ref. 1; BAD93238)"
FT /evidence="ECO:0000305"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 65..88
FT /evidence="ECO:0007829|PDB:6Y7F"
FT TURN 89..94
FT /evidence="ECO:0007829|PDB:6Y7F"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 145..164
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 172..192
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 204..227
FT /evidence="ECO:0007829|PDB:6Y7F"
FT HELIX 237..260
FT /evidence="ECO:0007829|PDB:6Y7F"
SQ SEQUENCE 281 AA; 33356 MW; 33C3DA79704F6E9F CRC64;
MAFSDLTSRT VHLYDNWIKD ADPRVEDWLL MSSPLPQTIL LGFYVYFVTS LGPKLMENRK
PFELKKAMIT YNFFIVLFSV YMCYEFVMSG WGIGYSFRCD IVDYSRSPTA LRMARTCWLY
YFSKFIELLD TIFFVLRKKN SQVTFLHVFH HTIMPWTWWF GVKFAAGGLG TFHALLNTAV
HVVMYSYYGL SALGPAYQKY LWWKKYLTSL QLVQFVIVAI HISQFFFMED CKYQFPVFAC
IIMSYSFMFL LLFLHFWYRA YTKGQRLPKT VKNGTCKNKD N
