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Database: UniProt
Entry: A0A182YMH8_ANOST
LinkDB: A0A182YMH8_ANOST
Original site: A0A182YMH8_ANOST 
ID   A0A182YMH8_ANOST        Unreviewed;       528 AA.
AC   A0A182YMH8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE            EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS   Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI09664-PA, ECO:0000313|Proteomes:UP000076408};
RN   [1] {ECO:0000313|Proteomes:UP000076408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX   PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA   Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA   Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA   Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA   George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA   Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA   Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA   Sharakhov I.V., Tu Z.;
RT   "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT   stephensi.";
RL   Genome Biol. 15:459-459(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASTEI09664-PA}
RP   IDENTIFICATION.
RC   STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI09664-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   AlphaFoldDB; A0A182YMH8; -.
DR   STRING; 30069.A0A182YMH8; -.
DR   EnsemblMetazoa; ASTEI09664-RA; ASTEI09664-PA; ASTEI09664.
DR   VEuPathDB; VectorBase:ASTE002459; -.
DR   VEuPathDB; VectorBase:ASTEI09664; -.
DR   VEuPathDB; VectorBase:ASTEI20_045460; -.
DR   OMA; IMCMLKV; -.
DR   Proteomes; UP000076408; Unassembled WGS sequence.
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:SF81; 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}; NADP {ECO:0000256|RuleBase:RU363097};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076408}.
FT   DOMAIN          31..306
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          378..448
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
SQ   SEQUENCE   528 AA;  60540 MW;  812DB3B5A8E2AB3C CRC64;
     MAACSSGSGF DDELQPPDRV LSFYSNSTIL VTGGTGFLGK VLLEKILRCL NVRKVFLAVR
     SKDGRNADER LQDLLKDVIF DRLRMAYTVD QLLERIEAVE ISLEEPNGGE GLSMDSVKEG
     RLLVETELIF NVLASVKFNE CIKNAIGTNV GGTRRILQLA RRMHRLKSVV HVSTLYSNCD
     RTRIQERVYP DSPLNPDSVL QLSKMLSTDE MSQLQHCLLG ELPNTYTFSK KCAESLIQQE
     FADLPIGIFR PPIVLSTYRE PIAGWTDNLN GPAGLCLWTV KGYVRVIRGN GHKKANLVPV
     DYCVNALLVA CFDVAERSIG RRQQHDPEPV ESAEAWESPQ LVPVYNYMYE QANLTWGRYM
     SSVSMGFDGW IKRLCCYRRM VTKTNRFLET MAYFGLREWH IANENVVRLR TLLTPTEASM
     LEFDLSTIDW DEYFQSYIPG IRRYFLAERG LSKQPVGSGR VKSLQWHRSF MFFPVPHFPF
     DFYYSDPSKS RRAQFLYRLA CKLLWVYVCL KLGHRLYVVR NLFSILIS
//
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