FACR1_RAT
ID FACR1_RAT Reviewed; 515 AA.
AC Q66H50;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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:0000312|RGD:1306647};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC082015; AAH82015.1; -; mRNA.
DR RefSeq; NP_001011933.1; NM_001011933.1.
DR RefSeq; XP_006230082.1; XM_006230020.3.
DR AlphaFoldDB; Q66H50; -.
DR STRING; 10116.ENSRNOP00000068284; -.
DR jPOST; Q66H50; -.
DR PaxDb; Q66H50; -.
DR PRIDE; Q66H50; -.
DR Ensembl; ENSRNOT00000076756; ENSRNOP00000068069; ENSRNOG00000013176.
DR GeneID; 293173; -.
DR KEGG; rno:293173; -.
DR UCSC; RGD:1306647; rat.
DR CTD; 84188; -.
DR RGD; 1306647; Far1.
DR eggNOG; KOG1221; Eukaryota.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_0_1; -.
DR InParanoid; Q66H50; -.
DR Reactome; R-RNO-9640463; Wax biosynthesis.
DR PRO; PR:Q66H50; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013176; Expressed in stomach and 18 other tissues.
DR ExpressionAtlas; Q66H50; baseline and differential.
DR Genevisible; Q66H50; RN.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; ISO:RGD.
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:0046474; P:glycerophospholipid biosynthetic process; ISO:RGD.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISO:RGD.
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_0000261397"
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; 59268 MW; 8D08D7F8DF957173 CRC64;
MVSIPEYYEG KNILLTGATG FLGKVLLEKL LRSCPKVNSV YVLVRQKAGQ TPQERVEEIL
SGKLFDRLRD ENPDFRQKII AINSELTQPK LALSEEDKEI IIDSTNVIFH CAATVRFNEN
LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS
LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF
PGWIDNFNGP SGLFIAAGKG ILRTMRASNN ALADLVPVDV VVNTSLAAAW YSGVNRPRNI
MVYNCTTGST NPFHWGEVGD YLNHSFKTNP LNQVFRHPYV KFYSNNLMLH YWKGVKHTVP
ALLLDLALRL TGQKPWMMKT ITRLHKAMVF LEYFTSNSWV WNTDNVNMLM NQLNPEDKKT
FNIDVRQLHW AEYIENYCMG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR
IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY
