ELOVL_DROME
ID ELOVL_DROME Reviewed; 329 AA.
AC Q9VHX7; Q8MS02;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Elongation of very long chain fatty acids protein {ECO:0000255|RuleBase:RU361115};
DE EC=2.3.1.199 {ECO:0000255|RuleBase:RU361115};
DE AltName: Full=Elongation of very long chain fatty acids elongase {ECO:0000312|FlyBase:FBgn0037534};
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase {ECO:0000255|RuleBase:RU361115};
GN Name=ELOVL {ECO:0000312|FlyBase:FBgn0037534};
GN ORFNames=CG2781 {ECO:0000312|FlyBase:FBgn0037534};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM51033.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM51033.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAM51033.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:AGV77164.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=29739804; DOI=10.1242/dmm.031286;
RA Gordon H.B., Valdez L., Letsou A.;
RT "Etiology and treatment of adrenoleukodystrophy: new insights from
RT Drosophila.";
RL Dis. Model. Mech. 11:0-0(2018).
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. {ECO:0000305}.
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|RuleBase:RU361115};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown leads to lethality before
CC eclosion (PubMed:29739804). RNAi-mediated knockdown in neurons leads to
CC neurodegeneration in the central nervous system including degeneration
CC of retina, defects in the fenestrated basement membrane and ommatidial
CC disarray (PubMed:29739804). Effects are probably due to altered levels
CC of very-long chain fatty acids (VLCFAs) (PubMed:29739804). In contrast,
CC glial-specific RNAi-mediated knockdown results in no defect
CC (PubMed:29739804). {ECO:0000269|PubMed:29739804}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000255|RuleBase:RU361115}.
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DR EMBL; AE014297; AAF54172.2; -; Genomic_DNA.
DR EMBL; AY119173; AAM51033.1; -; mRNA.
DR EMBL; BT150262; AGV77164.1; -; mRNA.
DR RefSeq; NP_649754.1; NM_141497.2.
DR AlphaFoldDB; Q9VHX7; -.
DR SMR; Q9VHX7; -.
DR IntAct; Q9VHX7; 26.
DR STRING; 7227.FBpp0081313; -.
DR PaxDb; Q9VHX7; -.
DR EnsemblMetazoa; FBtr0081823; FBpp0081313; FBgn0037534.
DR GeneID; 40943; -.
DR KEGG; dme:Dmel_CG2781; -.
DR UCSC; CG2781-RA; d. melanogaster.
DR CTD; 40943; -.
DR FlyBase; FBgn0037534; ELOVL.
DR VEuPathDB; VectorBase:FBgn0037534; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_0_1; -.
DR InParanoid; Q9VHX7; -.
DR OMA; TMFYDGW; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9VHX7; -.
DR Reactome; R-DME-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-DME-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-DME-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR BioGRID-ORCS; 40943; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40943; -.
DR PRO; PR:Q9VHX7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037534; Expressed in crop (Drosophila) and 35 other tissues.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0009922; F:fatty acid elongase activity; ISS:FlyBase.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; ISS:FlyBase.
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; IBA:GO_Central.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; ELO; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..329
FT /note="Elongation of very long chain fatty acids protein"
FT /id="PRO_0000447648"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 21
FT /note="P -> L (in Ref. 3; AAM51033)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="I -> V (in Ref. 3; AAM51033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 38355 MW; 489BCB8470322FBA CRC64;
MDYLTMFYDG WRDLMDNKSD PRTRDYPLMS SPFPTIAISL TYAYIVKVLG PKLMENRKPF
ELRKVLIVYN AAQVIFSAWL FYESCIGGWL NGYNLRCEPV NYSYSPKAIR TAEGCWWYYF
SKFTEFFDTF FFVMRKRYDQ VSTLHVIHHG IMPVSVWWGV KFTPGGHSTF FGFLNTFVHI
FMYAYYMLAA MGPKVQKYLW WKKYLTVMQM IQFVLVMVHS FQLFFKNDCN YPIGFAYFIG
AHAVMFYFLF SNFYKRAYVK RDGKDKASVK ANGHANGHVK ALKDGDVAPT SNGQANGFHN
TFSKFTTDMC NPALNSSTRQ RVLVNAGNK
