ID V5IE64_IXORI Unreviewed; 510 AA.
AC V5IE64;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-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};
DE Flags: Fragment;
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB73736.1};
RN [1] {ECO:0000313|EMBL:JAB73736.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB73736.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
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; GANP01010732; JAB73736.1; -; mRNA.
DR AlphaFoldDB; V5IE64; -.
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:SF45; 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 2: Evidence at transcript level;
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 459..479
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 12..281
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 353..444
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB73736.1"
SQ SEQUENCE 510 AA; 58014 MW; B07C4D59BDB4B9ED CRC64;
ISDFYEDQVV FLTGGTGFIG KVLLEKLLRS CPGVKHVYLL VRGKGGEEPG ARLEAMLKSK
VFDRLKRERP GALERVSPVR GDLTQPNLGL SSADQATLLD RVSVVFHSAA TVKFDEPLKR
AVQLNVLGTR RVLDLCKHMP NLRALVHVST AYCNCDKPEV DELIYPPPVD PKKIIDAAQW
MDDKMMDTMS GFLLGQRPNT YTLTKALAES LVLDERERLP VAIVRPSIVT ASWREPFPGW
VDNYNGFTGI IVSCGLGILR SVLVDRDCIA DVIPVDVVAN MLISVAWHTS VTRPEHVRVY
NCTSGTLQRQ TWGDVTTTMH ELILSHPLPH VMRYPSVGLT RSRLWHSVSL LCLHYLPALA
LDLGLQLVGR KPRLVSMYHK VRKGIDAVQY FTTNGWLFRS NNVVALVDEL STTDKQLFNF
DVRTMQWYAY WEQYVLGIRK YLFKAEASKL PEARKHMKWL YAVHLFLNLL LITFVWRLLL
TRSQTARNLC YFMLTFATRL CRMLPLMQSQ
//
