FACR5_ARATH
ID FACR5_ARATH Reviewed; 496 AA.
AC Q0WRB0; Q9LXN2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable fatty acyl-CoA reductase 5 {ECO:0000305};
DE EC=1.2.1.84 {ECO:0000269|PubMed:20571114, ECO:0000269|PubMed:24005667};
GN Name=FAR5 {ECO:0000303|PubMed:20571114}; OrderedLocusNames=At3g44550;
GN ORFNames=F14L2.100;
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].
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 [4]
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 [5]
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-238; LYS-242; THR-347;
RP ALA-355; PRO-363 AND VAL-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:20571114, PubMed:24005667). Catalyzes specifically the
CC formation of C18:0 fatty alcohol (PubMed:20571114, PubMed:24005667).
CC Provides the fatty alcohols required for synthesis of suberin in roots,
CC seed coat and wound-induced leaf tissue (PubMed:20571114). Provides the
CC fatty alcohols required for synthesis of alkyl hydroxycinnamates in
CC root waxes (PubMed:22797656). {ECO:0000269|PubMed:20571114,
CC ECO:0000269|PubMed:22797656, 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:20571114, ECO:0000269|PubMed:24005667};
CC -!- TISSUE SPECIFICITY: Expressed in the endodermal cell layer surrounding
CC the central vasculature in roots. Expressed in floral organs of very
CC young unopened buds 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; AL353818; CAB88537.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77914.1; -; Genomic_DNA.
DR EMBL; AK228404; BAF00339.1; -; mRNA.
DR PIR; T48935; T48935.
DR RefSeq; NP_190041.2; NM_114323.4.
DR AlphaFoldDB; Q0WRB0; -.
DR STRING; 3702.AT3G44550.1; -.
DR PaxDb; Q0WRB0; -.
DR PRIDE; Q0WRB0; -.
DR ProteomicsDB; 230848; -.
DR EnsemblPlants; AT3G44550.1; AT3G44550.1; AT3G44550.
DR GeneID; 823580; -.
DR Gramene; AT3G44550.1; AT3G44550.1; AT3G44550.
DR KEGG; ath:AT3G44550; -.
DR Araport; AT3G44550; -.
DR TAIR; locus:2076023; AT3G44550.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_4_1_1; -.
DR InParanoid; Q0WRB0; -.
DR OMA; TNPITWQ; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; Q0WRB0; -.
DR BioCyc; ARA:AT3G44550-MON; -.
DR BRENDA; 1.2.1.84; 399.
DR BRENDA; 1.2.1.B25; 399.
DR PRO; PR:Q0WRB0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WRB0; baseline and differential.
DR Genevisible; Q0WRB0; 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; IEP: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..496
FT /note="Probable fatty acyl-CoA reductase 5"
FT /id="PRO_0000378345"
FT MUTAGEN 238
FT /note="Y->F: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24005667"
FT MUTAGEN 242
FT /note="K->I: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24005667"
FT MUTAGEN 347
FT /note="T->I: Decreases protein stability and enzymatic
FT activity."
FT /evidence="ECO:0000269|PubMed:24005667"
FT MUTAGEN 355
FT /note="A->L: Catalyzes the formation of C16:0 fatty alcohol
FT instead of C18:0; when associated with M-377."
FT /evidence="ECO:0000269|PubMed:24005667"
FT MUTAGEN 363
FT /note="P->S: Decreases protein stability and enzymatic
FT activity."
FT /evidence="ECO:0000269|PubMed:24005667"
FT MUTAGEN 377
FT /note="V->M: Catalyzes the formation of C16:0 fatty alcohol
FT instead of C18:0; when associated with L-355."
FT /evidence="ECO:0000269|PubMed:24005667"
SQ SEQUENCE 496 AA; 56429 MW; 151011CEFAECE457 CRC64;
MELNCVQFLR NKTILVTGAT GFLAKVFVEK ILRVQPNVKK LYLLVRASDN EAATKRLRTE
VFEKELFKVL RQNLGDEKLN TLLYEKVVSV PGDIATDQLG INDSHLRERM QKEIDIVVNV
AATTNFDERY DVGLGINTFG ALNVLNFAKK CVKVQLLLHV STAYVCGEKP GLIPEKPFIM
EEIRNENGLQ LDINLERELM KQRLKELNEQ DCSEEDITLS MKELGMERAK LHGWPNTYVF
TKSMGEMLLG KHKENLPLVI IRPTMITSTL SEPFPGWIEG LRTVDSVIIA YGKGVLKCFL
VDVNSVCDMI PVDMVANAMI TAAAKHAGGS GVHMVYHVGS SHQNPVTFGE IHEIAVRYFT
KNPLRSRNGS LITVSKVRFI PTMALFSLYM TLRYKLPLQL LKLVDIIYPW RNGDKYGDKN
RKIELVMRLV ELYEPYVLFK GIFDDRNTKS LCANQKEEEI KNTEKLMFDF DPKGINWGDY
LTNIHISGLV THVLKK
