GenomeNet

Database: UniProt
Entry: A0A084VFP2_ANOSI
LinkDB: A0A084VFP2_ANOSI
Original site: A0A084VFP2_ANOSI 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system