FACR3_ARATH
ID FACR3_ARATH Reviewed; 493 AA.
AC Q93ZB9; O81895; Q9M071;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Fatty acyl-CoA reductase 3 {ECO:0000305};
DE EC=1.2.1.84 {ECO:0000269|PubMed:16980563, ECO:0000269|PubMed:19062129};
DE AltName: Full=Protein ECERIFERUM 4;
GN Name=FAR3; Synonyms=CER4; OrderedLocusNames=At4g33790; ORFNames=T16L1.280;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16980563; DOI=10.1104/pp.106.086785;
RA Rowland O., Zheng H., Hepworth S.R., Lam P., Jetter R., Kunst L.;
RT "CER4 encodes an alcohol-forming fatty acyl-coenzyme A reductase involved
RT in cuticular wax production in Arabidopsis.";
RL Plant Physiol. 142:866-877(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=18470011; DOI=10.1139/g93-082;
RA McNevin J.P., Woodward W., Hannoufa A., Feldmann K.A., Lemieux B.;
RT "Isolation and characterization of eceriferum (cer) mutants induced by T-
RT DNA insertions in Arabidopsis thaliana.";
RL Genome 36:610-618(1993).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=12228482; DOI=10.1104/pp.108.1.369;
RA Jenks M.A., Tuttle H.A., Eigenbrode S.D., Feldmann K.A.;
RT "Leaf epicuticular waxes of the eceriferum mutants in Arabidopsis.";
RL Plant Physiol. 108:369-377(1995).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19062129; DOI=10.1016/j.jplph.2008.10.003;
RA Doan T.P.T., Carlsson A.S., Hamberg M., Buelow L., Stymne S., Olsson P.;
RT "Functional expression of five Arabidopsis fatty acyl-CoA reductase genes
RT in Escherichia coli.";
RL J. Plant Physiol. 166:787-796(2009).
CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
CC The preferred substrates are C24:0 and C26:0. May be unable to use
CC saturated and monounsaturated C16 and C18 acyl-CoA as substrates.
CC Involved in cuticular wax formation. {ECO:0000269|PubMed:16980563,
CC ECO:0000269|PubMed:19062129}.
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:16980563, ECO:0000269|PubMed:19062129};
CC -!- INTERACTION:
CC Q93ZB9; Q9LEZ3: BIM1; NbExp=3; IntAct=EBI-25514661, EBI-617095;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000305|PubMed:16980563}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, siliques and
CC roots. Detected in epidermal cells of leaves and stems, in trichomes
CC and in the elongation zone of young roots.
CC {ECO:0000269|PubMed:16980563}.
CC -!- DISRUPTION PHENOTYPE: Glossy stem wax. Major decreases in primary
CC alcohols and wax esters, and slightly elevated levels of aldehydes,
CC alkanes, secondary alcohols, and ketones. {ECO:0000269|PubMed:12228482,
CC ECO:0000269|PubMed:16980563, ECO:0000269|PubMed:18470011}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20592.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL031394; CAA20592.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80096.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86278.1; -; Genomic_DNA.
DR EMBL; AY057657; AAL15288.1; -; mRNA.
DR EMBL; AY070065; AAL49822.1; -; mRNA.
DR PIR; G85397; G85397.
DR PIR; T04996; T04996.
DR RefSeq; NP_567936.5; NM_119537.7.
DR AlphaFoldDB; Q93ZB9; -.
DR BioGRID; 14803; 1.
DR IntAct; Q93ZB9; 1.
DR STRING; 3702.AT4G33790.1; -.
DR PaxDb; Q93ZB9; -.
DR PRIDE; Q93ZB9; -.
DR ProteomicsDB; 222340; -.
DR EnsemblPlants; AT4G33790.1; AT4G33790.1; AT4G33790.
DR GeneID; 829521; -.
DR Gramene; AT4G33790.1; AT4G33790.1; AT4G33790.
DR KEGG; ath:AT4G33790; -.
DR Araport; AT4G33790; -.
DR TAIR; locus:2134278; AT4G33790.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_4_1_1; -.
DR InParanoid; Q93ZB9; -.
DR OMA; WLEYTEN; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; Q93ZB9; -.
DR BioCyc; MetaCyc:AT4G33790-MON; -.
DR BRENDA; 1.2.1.50; 399.
DR BRENDA; 1.2.1.84; 399.
DR PRO; PR:Q93ZB9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93ZB9; baseline and differential.
DR Genevisible; Q93ZB9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; IDA:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0010345; P:suberin biosynthetic process; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..493
FT /note="Fatty acyl-CoA reductase 3"
FT /id="PRO_0000378343"
SQ SEQUENCE 493 AA; 56035 MW; 82CB4DCCC92E0688 CRC64;
MSTEMEVVSV LKYLDNKSIL VVGAAGFLAN IFVEKILRVA PNVKKLYLLL RASKGKSATQ
RFNDEILKKD LFKVLKEKYG PNLNQLTSEK ITIVDGDICL EDLGLQDFDL AHEMIHQVDA
IVNLAATTKF DERYDVALGI NTLGALNVLN FAKRCAKVKI LVHVSTAYVC GEKSGLIMET
PYRMGETLNG TTGLDINYEK KLVQEKLDQL RVIGAAPETI TETMKDLGLR RAKMYGWPNT
YVFTKAMGEM MVGTKRENLS LVLLRPSIIT STFKEPFPGW TEGIRTIDSL AVGYGKGKLT
CFLCDLDAVS DVMPADMVVN SILVSMAAQA GKQEEIIYHV GSSLRNPMKN SKFPELAYRY
FSIKPWTNKE GKVVKVGAIE ILSSMRSFHR YMTIRYLIAL KGLELVNIIL CKLFEKEFQY
FNKKINFIFR LVDLYQPYLF FYGIFDDSNT EKLRKMVSKT GVENEMFYFD PKVLDWDDYF
LNTHVIGLLK YVF
