FACR1_ARATH
ID FACR1_ARATH Reviewed; 491 AA.
AC Q39152;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Fatty acyl-CoA reductase 1 {ECO:0000305};
DE EC=1.2.1.84 {ECO:0000269|PubMed:19062129, ECO:0000269|PubMed:20571114};
GN Name=FAR1 {ECO:0000303|PubMed:20571114}; OrderedLocusNames=At5g22500;
GN ORFNames=MQJ16.4;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9351246; DOI=10.1046/j.1365-313x.1997.00615.x;
RA Aarts M.G.M., Hodge R.P., Kalantidis K., Florack D., Wilson Z.A.,
RA Mulligan B.J., Stiekema W.J., Scott R., Pereira A.;
RT "The Arabidopsis MALE STERILITY 2 protein shares similarity with reductases
RT in elongation/condensation complexes.";
RL Plant J. 12:615-623(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], 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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20571114; DOI=10.1104/pp.110.158238;
RA Domergue F., Vishwanath S.J., Joubes J., Ono J., Lee J.A., Bourdon M.,
RA Alhattab R., Lowe C., Pascal S., Lessire R., Rowland O.;
RT "Three Arabidopsis fatty acyl-coenzyme A reductases, FAR1, FAR4, and FAR5,
RT generate primary fatty alcohols associated with suberin deposition.";
RL Plant Physiol. 153:1539-1554(2010).
RN [7]
RP FUNCTION.
RX PubMed=22797656; DOI=10.1104/pp.112.201822;
RA Kosma D.K., Molina I., Ohlrogge J.B., Pollard M.;
RT "Identification of an Arabidopsis fatty alcohol:caffeoyl-Coenzyme A
RT acyltransferase required for the synthesis of alkyl hydroxycinnamates in
RT root waxes.";
RL Plant Physiol. 160:237-248(2012).
CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols
CC (PubMed:19062129, PubMed:20571114). Catalyzes specifically the
CC formation of C18:0 and C22:0 fatty alcohols. Provides the fatty
CC alcohols required for synthesis of suberin in roots, seed coat and
CC wound-induced leaf tissue (PubMed:20571114). Provides the fatty
CC alcohols required for synthesis of alkyl hydroxycinnamates in root
CC waxes (PubMed:22797656). {ECO:0000269|PubMed:19062129,
CC ECO:0000269|PubMed:20571114, ECO:0000269|PubMed:22797656}.
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:19062129};
CC -!- TISSUE SPECIFICITY: Expressed in the endodermal cell layer surrounding
CC the central vasculature in roots. Expressed in the hilum region of
CC seeds. Expressed in lateral root tips, cotyledons, the shoot apex,
CC young leaves, petals, stamen filaments, and receptacle of siliques.
CC {ECO:0000269|PubMed:20571114}.
CC -!- INDUCTION: Induced by wounding and salt stress.
CC {ECO:0000269|PubMed:20571114}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
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DR EMBL; X99923; CAA68191.1; -; mRNA.
DR EMBL; EU280149; ABZ10951.1; -; mRNA.
DR EMBL; AB012244; BAB09122.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93034.1; -; Genomic_DNA.
DR EMBL; AY035042; AAK59547.1; -; mRNA.
DR EMBL; AY051075; AAK93752.1; -; mRNA.
DR RefSeq; NP_197642.1; NM_122155.4.
DR AlphaFoldDB; Q39152; -.
DR STRING; 3702.AT5G22500.1; -.
DR PaxDb; Q39152; -.
DR PRIDE; Q39152; -.
DR ProteomicsDB; 222372; -.
DR EnsemblPlants; AT5G22500.1; AT5G22500.1; AT5G22500.
DR GeneID; 832311; -.
DR Gramene; AT5G22500.1; AT5G22500.1; AT5G22500.
DR KEGG; ath:AT5G22500; -.
DR Araport; AT5G22500; -.
DR TAIR; locus:2171107; AT5G22500.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_4_1_1; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; Q39152; -.
DR BioCyc; ARA:AT5G22500-MON; -.
DR BRENDA; 1.2.1.42; 399.
DR BRENDA; 1.2.1.50; 399.
DR BRENDA; 1.2.1.84; 399.
DR BRENDA; 1.2.1.B25; 399.
DR PRO; PR:Q39152; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39152; baseline and differential.
DR Genevisible; Q39152; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0050062; F:long-chain-fatty-acyl-CoA reductase 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:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:TAIR.
DR GO; GO:0010345; P:suberin 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 Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..491
FT /note="Fatty acyl-CoA reductase 1"
FT /id="PRO_0000378342"
SQ SEQUENCE 491 AA; 55481 MW; 762CB33A017C65CC CRC64;
MESNCVQFLG NKTILITGAP GFLAKVLVEK ILRLQPNVKK IYLLLRAPDE KSAMQRLRSE
VMEIDLFKVL RNNLGEDNLN ALMREKIVPV PGDISIDNLG LKDTDLIQRM WSEIDIIINI
AATTNFDERY DIGLGINTFG ALNVLNFAKK CVKGQLLLHV STAYISGEQP GLLLEKPFKM
GETLSGDREL DINIEHDLMK QKLKELQDCS DEEISQTMKD FGMARAKLHG WPNTYVFTKA
MGEMLMGKYR ENLPLVIIRP TMITSTIAEP FPGWIEGLKT LDSVIVAYGK GRLKCFLADS
NSVFDLIPAD MVVNAMVAAA TAHSGDTGIQ AIYHVGSSCK NPVTFGQLHD FTARYFAKRP
LIGRNGSPII VVKGTILSTM AQFSLYMTLR YKLPLQILRL INIVYPWSHG DNYSDLSRKI
KLAMRLVELY QPYLLFKGIF DDLNTERLRM KRKENIKELD GSFEFDPKSI DWDNYITNTH
IPGLITHVLK Q
