GenomeNet

Database: UniProt
Entry: A0A182QPB4_9DIPT
LinkDB: A0A182QPB4_9DIPT
Original site: A0A182QPB4_9DIPT 
ID   A0A182QPB4_9DIPT        Unreviewed;       493 AA.
AC   A0A182QPB4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-MAY-2023, entry version 27.
DE   RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE            EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF014175-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF014175-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF014175-PA};
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; AXCN02001909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182QPB4; -.
DR   STRING; 69004.A0A182QPB4; -.
DR   EnsemblMetazoa; AFAF014175-RA; AFAF014175-PA; AFAF014175.
DR   VEuPathDB; VectorBase:AFAF014175; -.
DR   OrthoDB; 1434498at2759; -.
DR   Proteomes; UP000075886; 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:SF24; 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   Transmembrane {ECO:0000256|RuleBase:RU363097};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT   TRANSMEM        352..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   TRANSMEM        470..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   DOMAIN          19..288
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          362..453
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
SQ   SEQUENCE   493 AA;  56219 MW;  96DDDAF9B065A501 CRC64;
     MQQKFVDIPA VFAGADVFIT GGSGFMGKVL VEKLLRSCPQ IARVFVLMRP KRGKSLEDRL
     KTITDGVLFD TLKSEHPDAL RKVHPIEGDC TQLKLGMSAE SMERMSDVQF VFHAAASVRF
     DDPLKDAILT NTRSTRELLD WAKTLRKLRA VVHISTTYCN PELLRVEEKI YPPKMDWRDA
     IRMAETLDMP TLETFKDKLT QFAPNTYTYT KGLAEQICHD YRNDVPLVVF RPSIVTNTER
     EPVAGWVDNF NGPMGLLLGC ASGVVRTGLL DLKKRINCIP VDVSIKAIIV AAWKRAITEP
     DTGILPVYNS AAEPDKTINY GTLLYDGKVL FDRIPLTNML WAPGGTATSS KYIFYLLFFC
     CQLVPALFAD ALLRIGGKAP FLLKLNRKIF DAQVSLRYFM NNEWVFVNEN FKQLEYALSN
     ADRKNFSTNY FVQGMMEYYE IAILGGRRYL MKEPDENIDM ALRKYRRLRV LNYLLKSVLA
     FLLAYCVYRK YAL
//
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