FACR1_DROME
ID FACR1_DROME Reviewed; 625 AA.
AC A1ZAI5;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Putative fatty acyl-CoA reductase CG5065 {ECO:0000250|UniProtKB:Q8WVX9, ECO:0000312|EMBL:AAF57974.1};
DE EC=1.2.1.84 {ECO:0000250|UniProtKB:Q8WVX9};
GN ORFNames=CG5065;
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;
RN [1] {ECO:0000312|EMBL:AAF57974.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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:0000305, ECO:0000312|EMBL:AAF57974.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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).
CC -!- FUNCTION: Catalyzes the reduction of C16 or C18 fatty acyl-CoA to fatty
CC alcohols. {ECO:0000250|UniProtKB:Q8WVX9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC Evidence={ECO:0000250|UniProtKB:Q8WVX9};
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q8WVX9}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8WVX9}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000255}.
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DR EMBL; AE013599; AAF57974.1; -; Genomic_DNA.
DR RefSeq; NP_001163168.1; NM_001169697.3.
DR RefSeq; NP_001163169.1; NM_001169698.3.
DR RefSeq; NP_001246370.1; NM_001259441.2.
DR RefSeq; NP_001246371.1; NM_001259442.2.
DR RefSeq; NP_611143.1; NM_137299.4.
DR AlphaFoldDB; A1ZAI5; -.
DR BioGRID; 62573; 2.
DR STRING; 7227.FBpp0086254; -.
DR PaxDb; A1ZAI5; -.
DR PRIDE; A1ZAI5; -.
DR EnsemblMetazoa; FBtr0087108; FBpp0086254; FBgn0034145.
DR EnsemblMetazoa; FBtr0302205; FBpp0291415; FBgn0034145.
DR EnsemblMetazoa; FBtr0302206; FBpp0291416; FBgn0034145.
DR EnsemblMetazoa; FBtr0306249; FBpp0297359; FBgn0034145.
DR EnsemblMetazoa; FBtr0306250; FBpp0297360; FBgn0034145.
DR GeneID; 36860; -.
DR KEGG; dme:Dmel_CG5065; -.
DR UCSC; CG5065-RA; d. melanogaster.
DR FlyBase; FBgn0034145; CG5065.
DR VEuPathDB; VectorBase:FBgn0034145; -.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_0_2_1; -.
DR InParanoid; A1ZAI5; -.
DR OMA; YCNCDRT; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; A1ZAI5; -.
DR BioGRID-ORCS; 36860; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36860; -.
DR PRO; PR:A1ZAI5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034145; Expressed in crop (Drosophila) and 27 other tissues.
DR ExpressionAtlas; A1ZAI5; baseline and differential.
DR Genevisible; A1ZAI5; DM.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; ISM:FlyBase.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; ISS:UniProtKB.
DR GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; ISS:UniProtKB.
DR CDD; cd09071; FAR_C; 1.
DR InterPro; IPR026055; FAR.
DR InterPro; IPR033640; FAR_C.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11011; PTHR11011; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Peroxisome; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..625
FT /note="Putative fatty acyl-CoA reductase CG5065"
FT /id="PRO_0000376019"
FT TOPO_DOM 1..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8WVX9"
FT TRANSMEM 578..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..625
FT /note="Peroxisomal"
FT /evidence="ECO:0000250|UniProtKB:Q8WVX9"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 69683 MW; 8C12CD780F96D5E0 CRC64;
MSHAVANKTE TEAAPNSSLK QSAAPQPANS HDAKLLNGTL ARTNGLTHAA SVATSSSGSY
GSSSAAGSNA GSGGPTSSAS LSIAAGVASS TALPLPPSSN GLQMPYERFR ADDTSYVPIA
QFYAGRSVFI TGGTGFMGKV LVEKLLRSCP EIRNIYLLIR PKRGQEVSAR LTELLNAPLF
ESLRQEKPKE LSKVIPISGD ITSEELGISE KDQNLLCRNV SVVFHSAATV KFDEKLKLSV
TINMLGTKRL VELCHRMLSL DALIHVSTAY CNCDRTDVSE VIYAPPYNPD DIISLINWLP
EDILDQLTPR LIGKRPNTYT FTKALAEHML LKEAGNLPVA IVRPSIVTAS LNEPFAGWVD
NFNGPTGLVS ALAKGMFRTM MCEKNYVADM VPVDIVINLM IAAAWRTATR KSNNLLIYNC
CTGQRNPIIW SEFVKHAMTS VRKHPLEGCL WYPTGDLRMN RPMNTLNCIA KHFLPAYILD
GVARIMGKKP FVVNVQNKIA KAVECLEYFA TRQWRFKDDN VHALLHTLSP KDREIFVFDV
RHINWDKYVE RYVLGFREFL FKQRPESLPA SRKRMLRLYY LHQLTKLVAV LLTWRFLMSR
SKRLNDLWSS FLENALRMAR LIPFL
