ELOF_DROME
ID ELOF_DROME Reviewed; 257 AA.
AC Q9VH58; Q0E5H2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Elongation of very long chain fatty acids protein F {ECO:0000305|PubMed:17360514};
DE EC=2.3.1.199 {ECO:0000255|RuleBase:RU361115, ECO:0000269|PubMed:17360514};
GN Name=eloF {ECO:0000303|PubMed:17360514};
GN ORFNames=CG16905 {ECO:0000312|FlyBase:FBgn0037762};
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|EMBL:CAL23476.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S {ECO:0000312|EMBL:CAL23476.1};
RX PubMed=17360514; DOI=10.1073/pnas.0608142104;
RA Chertemps T., Duportets L., Labeur C., Ueda R., Takahashi K., Saigo K.,
RA Wicker-Thomas C.;
RT "A female-biased expressed elongase involved in long-chain hydrocarbon
RT biosynthesis and courtship behavior in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4273-4278(2007).
RN [2] {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 [3] {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 [4] {ECO:0000312|EMBL:ABE01223.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Condensing enzyme that elongates saturated and
CC monounsaturated very long chain fatty acids, to yield products up to 30
CC carbons in length. May also elongate diunsaturated fatty acids.
CC Important for courtship behavior where it probably has a role in female
CC pheromone biosynthesis. {ECO:0000269|PubMed:17360514}.
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 ECO:0000269|PubMed:17360514};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:17360514}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:17360514}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in females. Little or no
CC expression detected in males. {ECO:0000269|PubMed:17360514}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an altered
CC hydrocarbon profile in females, with significantly increased levels of
CC C25 7,11-dienes and reduced levels of C27 7,11-dienes. Monounsaturated
CC and saturated hydrocarbon levels are also affected with increased
CC levels of C23 fatty acids and reduced levels of C27 fatty acids. Males
CC have a normal hydrocarbon profile. RNAi-mediated knockdown in females
CC (mated to wild-type males) results in impaired courtship behavior with
CC reduced numbers of copulation attempts and increased copulation
CC latency. {ECO:0000269|PubMed:17360514}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; AM292552; CAL23476.1; -; mRNA.
DR EMBL; AE014297; AAF54461.1; -; Genomic_DNA.
DR EMBL; BT024993; ABE01223.1; -; mRNA.
DR RefSeq; NP_649956.1; NM_141699.3.
DR AlphaFoldDB; Q9VH58; -.
DR SMR; Q9VH58; -.
DR STRING; 7227.FBpp0081622; -.
DR PaxDb; Q9VH58; -.
DR DNASU; 41211; -.
DR EnsemblMetazoa; FBtr0082144; FBpp0081622; FBgn0037762.
DR GeneID; 41211; -.
DR KEGG; dme:Dmel_CG16905; -.
DR UCSC; CG16905-RA; d. melanogaster.
DR CTD; 41211; -.
DR FlyBase; FBgn0037762; eloF.
DR VEuPathDB; VectorBase:FBgn0037762; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_2_1; -.
DR InParanoid; Q9VH58; -.
DR OMA; VAFPQCL; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9VH58; -.
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 UniPathway; UPA00094; -.
DR BioGRID-ORCS; 41211; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41211; -.
DR PRO; PR:Q9VH58; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037762; Expressed in adult abdomen and 9 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; IDA:FlyBase.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0007619; P:courtship behavior; IMP:FlyBase.
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:0042810; P:pheromone metabolic process; IMP:FlyBase.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:FlyBase.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 1: Evidence at protein level;
KW Behavior; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..257
FT /note="Elongation of very long chain fatty acids protein F"
FT /id="PRO_0000438397"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 193
FT /note="I -> T (in Ref. 1; CAL23476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 29923 MW; 25FEF94C8919F9E5 CRC64;
MFAPIDPVKI PVVSNPWITM GTLIGYLLFV LKLGPKIMEH RKPFHLNGVI RIYNIFQILY
NGLILVLGVH FLFVLKAYQI SCIVSLPMDH KYKDRERLIC TLYLVNKFVD LVETIFFVLR
KKDRQISFLH VFHHFAMAFF GYLYYCFHGY GGVAFPQCLL NTAVHVIMYA YYYLSSISKE
VQRSLWWKKY ITIAQLVQFA IILLHCTITL AQPNCAVNRP LTYGCGSLSA FFAVIFSQFY
YHNYIKPGKK SAKQNKN
