ID A0A182G8H5_AEDAL Unreviewed; 516 AA.
AC A0A182G8H5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=RP20_CCG005163 {ECO:0000313|EMBL:KXJ78213.1};
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160 {ECO:0000313|EnsemblMetazoa:AALF005163-PA.1, ECO:0000313|Proteomes:UP000069940};
RN [1] {ECO:0000313|EMBL:KXJ78213.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ78213.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ78213.1};
RX PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA Yan G., Tu Z.J., Fang X., James A.A.;
RT "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT insights into its biology, genetics, and evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN [2] {ECO:0000313|EMBL:KXJ78213.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ78213.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ78213.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:AALF005163-PA.1}
RP IDENTIFICATION.
RC STRAIN=Foshan {ECO:0000313|EnsemblMetazoa:AALF005163-PA.1};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
CC {ECO:0000256|RuleBase:RU363097}.
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:0000256|RuleBase:RU363097};
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000256|ARBA:ARBA00005928, ECO:0000256|RuleBase:RU363097}.
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DR EMBL; JXUM01047962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KQ561540; KXJ78213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182G8H5; -.
DR EnsemblMetazoa; AALF005163-RA; AALF005163-PA; AALF005163.
DR VEuPathDB; VectorBase:AALC636_006985; -.
DR VEuPathDB; VectorBase:AALF005163; -.
DR VEuPathDB; VectorBase:AALFPA_079576; -.
DR Proteomes; UP000069940; Unplaced.
DR Proteomes; UP000249989; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0102965; F:alcohol-forming long-chain fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:alcohol-forming very long-chain fatty acyl-CoA reductase activity; IEA:InterPro.
DR GO; GO:1901568; P:fatty acid derivative metabolic process; IEA:UniProt.
DR CDD; cd05236; FAR-N_SDR_e; 1.
DR CDD; cd09071; FAR_C; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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:SF60; FATTY ACYL-COA REDUCTASE-RELATED; 1.
DR PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU363097};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU363097}; Membrane {ECO:0000256|RuleBase:RU363097};
KW NADP {ECO:0000256|RuleBase:RU363097};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW Reference proteome {ECO:0000313|Proteomes:UP000249989};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 362..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 486..507
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 25..292
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 373..465
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 516 AA; 59019 MW; B802F701EFDAA19E CRC64;
MNLWEEEPIH PSPVADYYRG KVVLLTGATG FLGKLYMVKL VRLGVKELIV IVREKKGVQP
KERMVKILEK EKLFKVHGLG EKQYMKTLTV IAGDMDVPGL GLSPEDLEYI RERTEIVLHA
AADVRFDEAL NKIIITNVQG TLEMLNLCVS LRKMELMIYV STAYANCVTN TVYEKFYDPP
VDPLKMMELM KTVDDDQSEV LTDMIIRPWP NTYTYAKSLA ENLVKMYFDR MNIVIIRPTI
VATTMDDPIQ GWTDNLYGLN GVIVGAGCGV LRVLHASDSI KIDIIPADFV INGTLVAAYR
AAEDYRHNAP STDPDKVHIY HLGSAVDNPL TNAMISRYTK TIGASNPPLR SLWIGSYVST
KYATFSMILS ILLHLIPGVI IDAILRFKGE RPMLMKIYRK VRKFTTMIEF FAGQEFIFVN
DKMRQVMDSM TPGDKEQFQC DMKSLPWDDY FNIYFPGLKT YILKEKTDTW EKARQRYIRL
DMITNFVLRG SVVLSVYWVI YYVYIVISQN ILGDSM
//
