FACR4_ARATH
ID FACR4_ARATH Reviewed; 493 AA.
AC Q9LXN3; Q2V3Q9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable fatty acyl-CoA reductase 4 {ECO:0000305};
DE EC=1.2.1.84 {ECO:0000269|PubMed:20571114};
GN Name=FAR4 {ECO:0000303|PubMed:20571114}; OrderedLocusNames=At3g44540;
GN ORFNames=F14L2.90;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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:20571114). Catalyzes specifically the formation of C18:0 and
CC C20:0 fatty alcohols. Provides the fatty alcohols required for
CC synthesis of suberin in roots, seed coat and wound-induced leaf tissue
CC (PubMed:20571114). Provides the fatty alcohols required for synthesis
CC of alkyl hydroxycinnamates in root waxes (PubMed:22797656).
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:20571114};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LXN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LXN3-2; Sequence=VSP_037566, VSP_037567;
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 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}.
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; AL353818; CAB88536.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77912.1; -; Genomic_DNA.
DR EMBL; BT033118; ACF22894.1; -; mRNA.
DR EMBL; AK227396; BAE99400.1; -; mRNA.
DR PIR; T48934; T48934.
DR RefSeq; NP_190040.3; NM_114322.5. [Q9LXN3-1]
DR AlphaFoldDB; Q9LXN3; -.
DR STRING; 3702.AT3G44540.1; -.
DR PaxDb; Q9LXN3; -.
DR PRIDE; Q9LXN3; -.
DR ProteomicsDB; 222341; -. [Q9LXN3-1]
DR EnsemblPlants; AT3G44540.1; AT3G44540.1; AT3G44540. [Q9LXN3-1]
DR GeneID; 823579; -.
DR Gramene; AT3G44540.1; AT3G44540.1; AT3G44540. [Q9LXN3-1]
DR KEGG; ath:AT3G44540; -.
DR Araport; AT3G44540; -.
DR TAIR; locus:2076028; AT3G44540.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_4_1_1; -.
DR InParanoid; Q9LXN3; -.
DR OMA; FAHCNMR; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; Q9LXN3; -.
DR BioCyc; ARA:AT3G44540-MON; -.
DR BRENDA; 1.2.1.84; 399.
DR BRENDA; 1.2.1.B25; 399.
DR PRO; PR:Q9LXN3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXN3; baseline and differential.
DR Genevisible; Q9LXN3; 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; IBA:GO_Central.
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 Alternative splicing; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..493
FT /note="Probable fatty acyl-CoA reductase 4"
FT /id="PRO_0000378344"
FT VAR_SEQ 399..433
FT /note="MLRLIYVIYPWWNGNKYKDIDRKIKLAMRLVDLYR -> TLTARLSWRCGWS
FT TSTDLMSCLRAYLTIRILRNCG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_037566"
FT VAR_SEQ 434..493
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_037567"
SQ SEQUENCE 493 AA; 56218 MW; E372C264ED064E28 CRC64;
MDSNCIQFLH DKTILVTGVP GFLAKVFVEK ILRIQPKVKK LFLLLRAADN ESAMQRFHSE
VLEKDLFRVL KNALGDENLK AFITEKVVPI PGDISVDNLG VKGSDLLQHM WNEIDIIVNV
AATTNFDERY DVGLSVNTFG PLNVLNFAKK CVKGQLLLHV STAYVRGEKS GLLHEKTFHM
GETLNGHRKL VIETEMELMK QKLKELQKQN CSEEEISQSM KDLGMSRAKL HGWPNTYVFT
KSMGEMLLGN YRENLPIVII RPTMITSTFS EPFPGWIEGL RTIDSVIVAY GKGRLKCFLA
DPNSVLDLIP VDMVANAMVT AAAIHAGKLG SQTVYHVGSS CKNPITFEQI HDLAASYFTK
NPLVRRDGSS ILVSKGTILS TMAQFSFYMT LRYKLPLQML RLIYVIYPWW NGNKYKDIDR
KIKLAMRLVD LYRPYVLFKG IFDDTNTEKL RLKRKEINKE MYGLFEFDPK SIDWEDYMTT
IHIPGLITYV LKK
