ID FACR2_MOUSE Reviewed; 515 AA.
AC Q7TNT2; B2KFC6; Q3TTT7; Q8BH72; Q8CAK7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Fatty acyl-CoA reductase 2 {ECO:0000305|PubMed:15220348};
DE EC=1.2.1.84 {ECO:0000269|PubMed:15220348};
GN Name=Far2 {ECO:0000312|MGI:MGI:2687035};
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 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, Head, and Hypothalamus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR 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).
CC -!- FUNCTION: Catalyzes the reduction of saturated but not unsaturated C16
CC or C18 fatty acyl-CoA to fatty alcohols. A lower activity can be
CC observed with shorter fatty acyl-CoA substrates (PubMed:15220348). It
CC may play a role in the production of ether lipids/plasmalogens and wax
CC monoesters which synthesis requires fatty alcohols as substrates (By
CC similarity). {ECO:0000250|UniProtKB:Q8WVX9,
CC ECO:0000269|PubMed:15220348}.
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 -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:15220348}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96K12}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TNT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TNT2-2; Sequence=VSP_021682;
CC -!- TISSUE SPECIFICITY: Specifically expressed in the meibomian glands of
CC the eyelid and the sebaceous glands of the skin. Also 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK038584; BAC30056.1; -; mRNA.
DR EMBL; AK043388; BAC31532.1; -; mRNA.
DR EMBL; AK043589; BAC31590.1; -; mRNA.
DR EMBL; AK161201; BAE36237.1; -; mRNA.
DR EMBL; CU207318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055759; AAH55759.1; -; mRNA.
DR CCDS; CCDS39718.1; -. [Q7TNT2-2]
DR CCDS; CCDS85188.1; -. [Q7TNT2-1]
DR RefSeq; NP_001334445.1; NM_001347516.1. [Q7TNT2-1]
DR RefSeq; NP_848912.1; NM_178797.3. [Q7TNT2-2]
DR RefSeq; XP_006507133.1; XM_006507070.3. [Q7TNT2-1]
DR AlphaFoldDB; Q7TNT2; -.
DR SMR; Q7TNT2; -.
DR STRING; 10090.ENSMUSP00000032443; -.
DR SwissLipids; SLP:000000211; -.
DR iPTMnet; Q7TNT2; -.
DR PhosphoSitePlus; Q7TNT2; -.
DR MaxQB; Q7TNT2; -.
DR PaxDb; 10090-ENSMUSP00000107234; -.
DR PeptideAtlas; Q7TNT2; -.
DR ProteomicsDB; 267705; -. [Q7TNT2-1]
DR ProteomicsDB; 267706; -. [Q7TNT2-2]
DR Antibodypedia; 2982; 106 antibodies from 19 providers.
DR Ensembl; ENSMUST00000032443.14; ENSMUSP00000032443.8; ENSMUSG00000030303.16. [Q7TNT2-1]
DR Ensembl; ENSMUST00000111607.4; ENSMUSP00000107234.4; ENSMUSG00000030303.16. [Q7TNT2-2]
DR GeneID; 330450; -.
DR KEGG; mmu:330450; -.
DR UCSC; uc009etb.1; mouse. [Q7TNT2-1]
DR UCSC; uc009etc.1; mouse. [Q7TNT2-2]
DR AGR; MGI:2687035; -.
DR CTD; 55711; -.
DR MGI; MGI:2687035; Far2.
DR VEuPathDB; HostDB:ENSMUSG00000030303; -.
DR eggNOG; KOG1221; Eukaryota.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_0_1; -.
DR InParanoid; Q7TNT2; -.
DR OMA; NCILKHF; -.
DR OrthoDB; 1434498at2759; -.
DR PhylomeDB; Q7TNT2; -.
DR TreeFam; TF313011; -.
DR BRENDA; 1.2.1.84; 3474.
DR Reactome; R-MMU-9640463; Wax biosynthesis.
DR BioGRID-ORCS; 330450; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Far2; mouse.
DR PRO; PR:Q7TNT2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q7TNT2; Protein.
DR Bgee; ENSMUSG00000030303; Expressed in tail skin and 141 other cell types or tissues.
DR Genevisible; Q7TNT2; 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:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0010025; P:wax biosynthetic process; TAS:MGI.
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:SF117; FATTY ACYL-COA REDUCTASE 2; 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 2"
FT /id="PRO_0000261402"
FT TOPO_DOM 1..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96K12"
FT TRANSMEM 465..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..515
FT /note="Peroxisomal"
FT /evidence="ECO:0000250|UniProtKB:Q96K12"
FT VAR_SEQ 497..515
FT /note="VSFCYKFISYFRASSTLKV -> CPLFKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021682"
FT CONFLICT 84
FT /note="A -> T (in Ref. 1; BAC30056)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="P -> H (in Ref. 1; BAE36237)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="Q -> E (in Ref. 1; BAE36237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 59167 MW; 86CBE93ECC4116C2 CRC64;
MSMIAAFYSN KSILITGATG FLGKVLMEKL FRTSPHLKVI YILVRPKSGQ TLQERVFQIL
NSKLFEKVKE VCPNVHEKIR PISADLNQRD FAISKEDVQE LLSCTNIIFH CAATVRFDAH
LREAVQLNVT ATQQLLLMAS QMPKLEAFIH ISTAFSNCNL SHIDEVIYPC PVEPRKIIDS
MEWLDDSIIE EITPKLIGDR PNTYTYTKAL GEIVVQQESG NLNVAIVRPS IVGATWQEPF
PGWVDNLNGP SGLIIATGKG FLRSIKATPM AVADVIPVDT VVNLTIAVGW YTAVHRPKST
LIYHSTSGNL NPCNWYKMGL QVLATIEKIP FESAFRRPNA DFTTSNFTTH YWNTVSHRVP
AIIYDFYLRL TGRKPRMLKL MNRLLKTISM LEYFINHSWE WSTNNTEMLL SELSPEDQRV
FNFDVRQLNW LEYIENYVLG VKKYLLKEDL AGIPKAKQHL RRLRNIHYLF NTALFLIIWR
LLIARSQMAR NVWFFIVSFC YKFISYFRAS STLKV
//
