FACR1_PONAB
ID FACR1_PONAB Reviewed; 515 AA.
AC Q5R834;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
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 {ECO:0000250|UniProtKB:Q8WVX9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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:Q922J9}.
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 -!- SUBUNIT: Interacts with PEX19; PEX19 mediates the targeting of FAR1 to
CC peroxisomes. {ECO:0000250|UniProtKB:Q8WVX9}.
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; CR859126; CAH91318.1; -; mRNA.
DR EMBL; CR859921; CAH92076.1; -; mRNA.
DR RefSeq; NP_001126210.1; NM_001132738.1.
DR AlphaFoldDB; Q5R834; -.
DR STRING; 9601.ENSPPYP00000003982; -.
DR Ensembl; ENSPPYT00000004135; ENSPPYP00000003982; ENSPPYG00000003470.
DR GeneID; 100173178; -.
DR KEGG; pon:100173178; -.
DR CTD; 84188; -.
DR eggNOG; KOG1221; Eukaryota.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_0_1; -.
DR InParanoid; Q5R834; -.
DR OMA; QPYTFYG; -.
DR OrthoDB; 815047at2759; -.
DR TreeFam; TF313011; -.
DR Proteomes; UP000001595; Chromosome 11.
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_0000261396"
FT TOPO_DOM 1..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8WVX9"
FT TRANSMEM 466..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..515
FT /note="Peroxisomal"
FT /evidence="ECO:0000250|UniProtKB:Q8WVX9"
FT REGION 451..507
FT /note="Necessary and sufficient for PEX19-mediated
FT localization into peroxisome membrane"
FT /evidence="ECO:0000250|UniProtKB:Q8WVX9"
SQ SEQUENCE 515 AA; 59357 MW; D689805D528345D0 CRC64;
MVSIPEYYEG KNVLLTGATG FLGKVLLEKL LRSCPKVNSV YVLVRQKAGQ TPQERVEEVL
SGKLFDRLRD ENPDFREKII AINSELTQPK LALSEEDKEV IIESTNIIFH CAATVRFNEN
LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS
LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF
PGWIDNFNGP SGLFIAAGKG ILRTIRASNN ALADLVPVDV VVNMSLAAAW YSGVNRPRNI
MVYNCTTGST NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP
AFLYDIYLRM TGRSPRMMKT ITRLHKAMVF LEYFTSNSWV WNTDNVNMLM NQLNPEDKKT
FNIDVRQLHW AEYIENYCLG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR
IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY
