FACR8_ARATH
ID FACR8_ARATH Reviewed; 496 AA.
AC Q1PEI6; A0MF04; Q9LXN1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Fatty acyl-CoA reductase 8 {ECO:0000305};
DE EC=1.2.1.84 {ECO:0000269|PubMed:19062129, ECO:0000269|PubMed:24005667};
GN Name=FAR8; OrderedLocusNames=At3g44560; ORFNames=F14L2.110;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ILE-347; LEU-355; SER-363
RP AND MET-377.
RX PubMed=24005667; DOI=10.1074/jbc.m113.499715;
RA Chacon M.G., Fournier A.E., Tran F., Dittrich-Domergue F., Pulsifer I.P.,
RA Domergue F., Rowland O.;
RT "Identification of amino acids conferring chain length substrate
RT specificities on fatty alcohol-forming reductases FAR5 and FAR8 from
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 288:30345-30355(2013).
CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols
CC (PubMed:19062129, PubMed:24005667). Catalyzes specifically the
CC formation of C16:0 fatty alcohol (PubMed:24005667).
CC {ECO:0000269|PubMed:19062129, ECO:0000269|PubMed:24005667}.
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, ECO:0000269|PubMed:24005667};
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28586.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB88538.1; Type=Erroneous gene model prediction; Evidence={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; EU280153; ABZ10955.1; -; mRNA.
DR EMBL; AL353818; CAB88538.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77915.1; -; Genomic_DNA.
DR EMBL; DQ446732; ABE65991.1; -; mRNA.
DR EMBL; DQ653127; ABK28586.1; ALT_SEQ; mRNA.
DR PIR; T48936; T48936.
DR RefSeq; NP_190042.2; NM_114324.3.
DR AlphaFoldDB; Q1PEI6; -.
DR STRING; 3702.AT3G44560.1; -.
DR PaxDb; Q1PEI6; -.
DR PRIDE; Q1PEI6; -.
DR EnsemblPlants; AT3G44560.1; AT3G44560.1; AT3G44560.
DR GeneID; 823581; -.
DR Gramene; AT3G44560.1; AT3G44560.1; AT3G44560.
DR KEGG; ath:AT3G44560; -.
DR Araport; AT3G44560; -.
DR TAIR; locus:2076038; AT3G44560.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_4_1_1; -.
DR InParanoid; Q1PEI6; -.
DR OMA; ALDWDSY; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; Q1PEI6; -.
DR BioCyc; ARA:AT3G44560-MON; -.
DR BRENDA; 1.2.1.50; 399.
DR PRO; PR:Q1PEI6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1PEI6; baseline and differential.
DR Genevisible; Q1PEI6; AT.
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 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..496
FT /note="Fatty acyl-CoA reductase 8"
FT /id="PRO_0000378348"
FT MUTAGEN 347
FT /note="I->T: Increases protein stability and enzymatic
FT activity. Catalyzes the formation of C18:0 fatty alcohol
FT instead of C16:0; when associated with A-355 and V-377."
FT /evidence="ECO:0000269|PubMed:24005667"
FT MUTAGEN 355
FT /note="L->A: Catalyzes the formation of C18:0 fatty alcohol
FT instead of C16:0; when associated with T-347 and V-377."
FT /evidence="ECO:0000269|PubMed:24005667"
FT MUTAGEN 363
FT /note="S->P: Increases protein stability and enzymatic
FT activity."
FT /evidence="ECO:0000269|PubMed:24005667"
FT MUTAGEN 377
FT /note="M->V: Catalyzes the formation of C18:0 fatty alcohol
FT instead of C16:0; when associated with T-347 and A-355."
FT /evidence="ECO:0000269|PubMed:24005667"
SQ SEQUENCE 496 AA; 56473 MW; C8182F173321061F CRC64;
MEFSCVHFLQ NKTILVTGAT GFLAKVFVEK ILRVQPNVNK LYLVVRASDN EAATKRLRTE
AFEKDLFKVL RDNLGDEKLN TLLSEKVVPV AGDIAMDHLG MKDSNLRERM QKEIDIVVNV
AATTNFDERY DIGLGINTFG ALNVLNFAKK CVKAQLLLHV STAYVCGEKP GLLPEKPFVM
EEICNENGLQ LDINLERELM KQRLKELNEQ GCSEEGTTFY MKELGMERAK LHGWPNTYVF
TKSMGEMLLG NHKENLPLVI IRPTMITSTL FEPFPGWIEG LRTVDSVIIA YGKGVLKCFL
VDVNSVCDMI PADMVANAMI AAAATHAGGS KVHMVYQVGS SHQNPIIYGE IREILFCYFT
KNSLRSRNGS MITVSKMKLI PTLALFSLYM TIRYKLPVQL LKLVDIIYPS REGDEYKNKN
RKIDMVMRLV KLYEPYVLFK GIFDDRNTKN LCAKQKEEDN RNSENFMFDF DPKIIKWKDY
LINVHIPGLI THVLKK
