ID W5JNX0_ANODA Unreviewed; 513 AA.
AC W5JNX0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=AND_002137 {ECO:0000313|EMBL:ETN66082.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN66082.1};
RN [1] {ECO:0000313|EMBL:ETN66082.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN66082.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN66082.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC002137-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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; ADMH02000529; ETN66082.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JNX0; -.
DR STRING; 43151.W5JNX0; -.
DR EnsemblMetazoa; ADAC002137-RA; ADAC002137-PA; ADAC002137.
DR VEuPathDB; VectorBase:ADAC002137; -.
DR VEuPathDB; VectorBase:ADAR2_004969; -.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_0_0_1; -.
DR OMA; KWDNLEQ; -.
DR OrthoDB; 3608418at2759; -.
DR Proteomes; UP000000673; 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:UP000000673};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 355..376
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 477..494
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 25..294
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 364..456
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 513 AA; 59164 MW; E728CB0B257BE812 CRC64;
MASLEEFRNY RSPLKDFYEG KTVLLTGGSG FIGKLLLEKL VKCNVAQILL IVRRKKGIEP
TDRLEQLLAK EPVFVNYAKH PELYLPRIKV IEGDISKPGL AISNDDLEYI YSHTNIILHA
AADVRFDEPL RSLIHSNVRG TRDLMTIALQ CRNLRIFLYI STAFSHCVRE EIGEQFYEPK
LDPSLLITIA ERESDADALE VLSGKLFEPW PNAYAFTKSL SEELVRRYRS KLPVAIIRPS
IITTTKEDPL AGWTDNLYGF NGVVCGAATG VLRIFHIRMD CKASIVPADT VTNSTLATAW
YAADHPQEEN IFNCTTDENP VSWNDTQHQL EKWKDRIVFD KSLWISTYNT TRYQLVADFL
AIFYHLLPAL LFDLVLRLRG QKPQVLRIYQ KVHRFSAVLR FFTNNEWRFR SDRMRTVLNA
LSADDQRYFP CDPKAISWSE FLDDQIKGLR VYLMRDPMES LKWTIPRHRK RQLAHRCLLV
LIYGGLFYLA LYVADALGLE KLFQIPKDDS TGM
//
