FACR1_XENLA
ID FACR1_XENLA Reviewed; 515 AA.
AC Q7ZXF5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Fatty acyl-CoA reductase 1 {ECO:0000250|UniProtKB:Q8WVX9};
DE EC=1.2.1.84 {ECO:0000250|UniProtKB:Q8WVX9};
GN Name=far1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of saturated and unsaturated C16 or
CC C18 fatty acyl-CoA to fatty alcohols. It plays an essential role in the
CC production of ether lipids/plasmalogens which synthesis requires fatty
CC alcohols. In parallel, it is also required for wax monoesters
CC production since fatty alcohols also constitute a substrate for their
CC synthesis. {ECO:0000250|UniProtKB:Q8WVX9}.
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:0000250|UniProtKB:Q8WVX9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52717;
CC Evidence={ECO:0000250|UniProtKB:Q8WVX9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2
CC NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.84;
CC Evidence={ECO:0000250|UniProtKB:Q8WVX9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC Evidence={ECO:0000250|UniProtKB:Q8WVX9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) +
CC octadecan-1-ol; Xref=Rhea:RHEA:36319, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32154, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.84;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36320;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2 H(+) + 2 NADPH = (9Z)-octadecen-1-ol
CC + CoA + 2 NADP(+); Xref=Rhea:RHEA:36323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:73504;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36324;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 H(+) + 2 NADPH = (9Z,12Z)-
CC octadecadien-1-ol + CoA + 2 NADP(+); Xref=Rhea:RHEA:36363,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73534;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36364;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q8WVX9}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8WVX9}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
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DR EMBL; BC045017; AAH45017.1; -; mRNA.
DR RefSeq; NP_001079591.1; NM_001086122.1.
DR AlphaFoldDB; Q7ZXF5; -.
DR DNASU; 379278; -.
DR GeneID; 379278; -.
DR KEGG; xla:379278; -.
DR CTD; 379278; -.
DR Xenbase; XB-GENE-973782; far1.L.
DR OMA; CPMVIVR; -.
DR OrthoDB; 815047at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 379278; Expressed in ovary and 19 other tissues.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; ISS:UniProtKB.
DR GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010025; P:wax biosynthetic process; ISS:UniProtKB.
DR CDD; cd09071; FAR_C; 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; PTHR11011; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Peroxisome; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..515
FT /note="Fatty acyl-CoA reductase 1"
FT /id="PRO_0000261399"
FT TOPO_DOM 1..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8WVX9"
FT TRANSMEM 466..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..515
FT /note="Peroxisomal"
FT /evidence="ECO:0000250|UniProtKB:Q8WVX9"
SQ SEQUENCE 515 AA; 59316 MW; E28F12751777213B CRC64;
MLSIPEFYQG KNVLITGATG FMGKVLLEKL LRSCPNTKAV YVLVRHKAGQ KPRERVAEMM
SCKLFDKLRD EQPDCAQKVI AISSELTQPE LDMSKEDQDT LIDCIDIVFH CAATVRFNES
LRDAMQLNVI ATRQLLYLAQ KMKKLEVFIH VSTAYANCNR KQIEEVVYPP PVDPKKLIES
LEWMDDSLVN DITPKLIGDR PNTYTYTKAL AEYVVQQEGS KLNIAIVRPS IVGASWKEPF
PGWIDNFNGP SGLFIAAGKG ILRTMRASNN AVADLIPVDV VVNTTLAAAW YSGVNRPKNM
LVYNCTTGGT NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP
ALLYDVYLRI TGRSPRMMKT ITRLHRAMML LEYFTSNSWV WNNENTNMLM SQLSPEDKKV
FNFDVRQLHW AEYMENYCMG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVVLIWR
VFIARSQMAR NIWYFVVSMC FKFLSYFRAS STMRY
