ID FACR1_MOUSE Reviewed; 515 AA.
AC Q922J9; Q8BZS2; Q9CXE8; Q9D0Q1; Q9DAU2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Fatty acyl-CoA reductase 1 {ECO:0000305|PubMed:15220348};
DE EC=1.2.1.84 {ECO:0000269|PubMed:15220348};
GN Name=Far1 {ECO:0000312|MGI:MGI:1914670};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cecum, Embryo, Liver, Placenta, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15220348; DOI=10.1074/jbc.m406225200;
RA Cheng J.B., Russell D.W.;
RT "Mammalian wax biosynthesis: I. Identification of two fatty acyl-coenzyme A
RT reductases with different substrate specificities and tissue
RT distributions.";
RL J. Biol. Chem. 279:37789-37797(2004).
RN [4]
RP FUNCTION.
RX PubMed=15220349; DOI=10.1074/jbc.m406226200;
RA Cheng J.B., Russell D.W.;
RT "Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs
RT encoding a member of the acyltransferase enzyme family.";
RL J. Biol. Chem. 279:37798-37807(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the reduction of saturated and unsaturated C16 or
CC C18 fatty acyl-CoA to fatty alcohols (PubMed:15220348,
CC PubMed:15220349). It plays an essential role in the production of ether
CC lipids/plasmalogens which synthesis requires fatty alcohols (By
CC similarity). In parallel, it is also required for wax monoesters
CC production since fatty alcohols also constitute a substrate for their
CC synthesis (PubMed:15220349). {ECO:0000250|UniProtKB:Q8WVX9,
CC ECO:0000269|PubMed:15220348, ECO:0000269|PubMed:15220349}.
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:0000269|PubMed:15220348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52717;
CC Evidence={ECO:0000305|PubMed:15220348};
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:0000269|PubMed:15220348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC Evidence={ECO:0000305|PubMed:15220348};
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:0000269|PubMed:15220348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36320;
CC Evidence={ECO:0000305|PubMed:15220348};
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:0000269|PubMed:15220348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36324;
CC Evidence={ECO:0000305|PubMed:15220348};
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:0000269|PubMed:15220348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36364;
CC Evidence={ECO:0000305|PubMed:15220348};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:15220348};
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:0000269|PubMed:15220348}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8WVX9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q922J9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q922J9-2; Sequence=VSP_021678, VSP_021679;
CC Name=3;
CC IsoId=Q922J9-3; Sequence=VSP_021680;
CC Name=4;
CC IsoId=Q922J9-4; Sequence=VSP_021681;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in all tissues
CC examined. Highest expression seen in preputial gland. Expressed in the
CC brain where large quantities of ether lipids are synthesized.
CC {ECO:0000269|PubMed:15220348}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
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DR EMBL; AK005531; BAB24102.1; -; mRNA.
DR EMBL; AK011187; BAB27453.1; -; mRNA.
DR EMBL; AK014486; BAB29388.1; -; mRNA.
DR EMBL; AK033674; BAC28423.1; -; mRNA.
DR EMBL; AK030067; BAC26766.1; -; mRNA.
DR EMBL; BC007178; AAH07178.1; -; mRNA.
DR CCDS; CCDS40093.1; -. [Q922J9-1]
DR CCDS; CCDS72024.1; -. [Q922J9-3]
DR RefSeq; NP_001272760.1; NM_001285831.1. [Q922J9-3]
DR RefSeq; NP_081655.2; NM_027379.3. [Q922J9-1]
DR RefSeq; XP_006508190.1; XM_006508127.3.
DR RefSeq; XP_006508191.1; XM_006508128.3.
DR RefSeq; XP_006508192.1; XM_006508129.3. [Q922J9-1]
DR RefSeq; XP_006508193.1; XM_006508130.3. [Q922J9-1]
DR RefSeq; XP_006508194.1; XM_006508131.3. [Q922J9-1]
DR AlphaFoldDB; Q922J9; -.
DR SMR; Q922J9; -.
DR BioGRID; 212175; 12.
DR IntAct; Q922J9; 2.
DR MINT; Q922J9; -.
DR STRING; 10090.ENSMUSP00000033018; -.
DR SwissLipids; SLP:000000210; -.
DR iPTMnet; Q922J9; -.
DR PhosphoSitePlus; Q922J9; -.
DR SwissPalm; Q922J9; -.
DR EPD; Q922J9; -.
DR jPOST; Q922J9; -.
DR MaxQB; Q922J9; -.
DR PaxDb; 10090-ENSMUSP00000064334; -.
DR PeptideAtlas; Q922J9; -.
DR ProteomicsDB; 271853; -. [Q922J9-1]
DR ProteomicsDB; 271854; -. [Q922J9-2]
DR ProteomicsDB; 271855; -. [Q922J9-3]
DR ProteomicsDB; 271856; -. [Q922J9-4]
DR Pumba; Q922J9; -.
DR Antibodypedia; 2735; 65 antibodies from 17 providers.
DR DNASU; 67420; -.
DR Ensembl; ENSMUST00000033018.15; ENSMUSP00000033018.9; ENSMUSG00000030759.17. [Q922J9-1]
DR Ensembl; ENSMUST00000067929.15; ENSMUSP00000064334.9; ENSMUSG00000030759.17. [Q922J9-3]
DR Ensembl; ENSMUST00000164745.8; ENSMUSP00000128695.2; ENSMUSG00000030759.17. [Q922J9-1]
DR GeneID; 67420; -.
DR KEGG; mmu:67420; -.
DR UCSC; uc009jhn.2; mouse. [Q922J9-2]
DR UCSC; uc009jho.2; mouse. [Q922J9-1]
DR UCSC; uc009jhq.2; mouse. [Q922J9-3]
DR AGR; MGI:1914670; -.
DR CTD; 84188; -.
DR MGI; MGI:1914670; Far1.
DR VEuPathDB; HostDB:ENSMUSG00000030759; -.
DR eggNOG; KOG1221; Eukaryota.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_2_1; -.
DR InParanoid; Q922J9; -.
DR OMA; NLMLHYW; -.
DR OrthoDB; 1434498at2759; -.
DR PhylomeDB; Q922J9; -.
DR TreeFam; TF313011; -.
DR BRENDA; 1.2.1.84; 3474.
DR Reactome; R-MMU-9640463; Wax biosynthesis.
DR BioGRID-ORCS; 67420; 6 hits in 79 CRISPR screens.
DR ChiTaRS; Far1; mouse.
DR PRO; PR:Q922J9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q922J9; Protein.
DR Bgee; ENSMUSG00000030759; Expressed in epithelium of stomach and 244 other cell types or tissues.
DR ExpressionAtlas; Q922J9; baseline and differential.
DR Genevisible; Q922J9; MM.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; ISO:MGI.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0010025; P:wax biosynthetic process; IDA:UniProtKB.
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:SF118; FATTY ACYL-COA REDUCTASE 1; 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 1: Evidence at protein level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane; NADP;
KW Oxidoreductase; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..515
FT /note="Fatty acyl-CoA reductase 1"
FT /id="PRO_0000261395"
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"
FT VAR_SEQ 242..260
FT /note="GWIDNFNGPSGLFIAAGKG -> VSSSKLLSSWDSEFQVRTV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021678"
FT VAR_SEQ 261..515
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021679"
FT VAR_SEQ 319..376
FT /note="EYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAPAFLYDIYLRM
FT TGRSPR -> GDYLNHSFKMNPLNQVFRHPYVKFCSNNLMLHYWKGVKHTVPALLLDLA
FT LRLTGQKPW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021680"
FT VAR_SEQ 515
FT /note="Y -> RRPRI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021681"
FT CONFLICT 35
FT /note="P -> R (in Ref. 1; BAB24102)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="Y -> H (in Ref. 1; BAB24102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 59435 MW; 6A9E9EF9A2F835A4 CRC64;
MVSIPEYYEG KNILLTGATG FLGKVLLEKL LRSCPRVNSV YVLVRQKAGQ TPQERVEEIL
SSKLFDRLRD ENPDFREKII AINSELTQPK LALSEEDKEI IIDSTNVIFH CAATVRFNEN
LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS
LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF
PGWIDNFNGP SGLFIAAGKG ILRTMRASNN ALADLVPVDV VVNTSLAAAW YSGVNRPRNI
MVYNCTTGST NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP
AFLYDIYLRM TGRSPRMMKT ITRLHKAMVF LEYFTSNSWV WNTDNVNMLM NQLNPEDKKT
FNIDVRQLHW AEYIENYCMG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR
IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY
//
