ID A0A084VFP2_ANOSI Unreviewed; 554 AA.
AC A0A084VFP2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=ZHAS_00003946 {ECO:0000313|EMBL:KFB36786.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB36786.1};
RN [1] {ECO:0000313|EMBL:KFB36786.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC003946-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; ATLV01012451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE524793; KFB36786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084VFP2; -.
DR STRING; 74873.A0A084VFP2; -.
DR EnsemblMetazoa; ASIC003946-RA; ASIC003946-PA; ASIC003946.
DR VEuPathDB; VectorBase:ASIC003946; -.
DR VEuPathDB; VectorBase:ASIS023117; -.
DR OMA; TNPITWQ; -.
DR Proteomes; UP000030765; 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:SF107; FATTY ACYL-COA REDUCTASE; 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:UP000030765};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 532..549
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 77..346
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 418..511
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 554 AA; 62664 MW; 4BDF126DA19128EB CRC64;
MIVKSLESTV SSVLSLKRPA LIAHGEQLHS KNARPLAVID ENNNEFLASG GEELELEPEP
ATTDTLRPFY DGKSVFVTGG TGFLGKVLIE KLLRACEGLR TIYILLRPKR GLTSEQRYRE
FVRHPVFDRL RSKTPQLLEK LVCVGGDISL PLLGLSERDH RTLLEQVQVV FHVAATVRFN
EGLIEAALLN TIGTKRLLDL CDNMQQLQSV VHVSTAYSNP CRSEVDEVVY PPPMDPEQFM
QCIQLLPGDV INAIAGKLQG THPNTYTLTK SITEQLVAQY ADRLPLCIVR PSIVTGAVAE
PYPGWIDNVY GITGIMMEIG RGTISSIMCD ERCTMDVIPV DIVCNTLIAA AWENAQKIAT
PIRVYNCTSG QVNGIKWHEY GRITQQCAVR NPTKYVMLYP GFRFRTNRLM HKLVELLLHF
LPAYLFDVLM RAQGAKPIMA KIAKRFQKAA DTGEYFAMHE WSFRNDNLLG LGRRVRRDRA
GADFPCDVRG LDWAAYIENY MLGIRRFVLK DELDSMSQAR SKLQRLLWLK RFLQLGALLL
LYYFCGLLFR MQHI
//