FACR2_ARATH
ID FACR2_ARATH Reviewed; 616 AA.
AC Q08891; B9TSP6; Q9LHM3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Fatty acyl-CoA reductase 2, chloroplastic {ECO:0000305|PubMed:19062129};
DE Short=AtFAR2 {ECO:0000303|PubMed:27274541};
DE EC=1.2.1.84 {ECO:0000269|PubMed:19062129, ECO:0000269|PubMed:21813653, ECO:0000269|PubMed:27274541};
DE AltName: Full=Fatty acid reductase 2 {ECO:0000303|PubMed:8390620};
DE AltName: Full=Male sterility protein 2 {ECO:0000303|PubMed:9351246};
DE Flags: Precursor;
GN Name=FAR2 {ECO:0000303|PubMed:8390620};
GN Synonyms=MS2 {ECO:0000303|PubMed:9351246};
GN OrderedLocusNames=At3g11980 {ECO:0000312|Araport:AT3G11980};
GN ORFNames=MEC18.11 {ECO:0000312|EMBL:BAB03110.1},
GN T21B14.18 {ECO:0000312|EMBL:AAG51054.1}, T21B14_123;
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], AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RX PubMed=8390620; DOI=10.1038/363715a0;
RA Aarts M.G.M., Dirkse W.G., Stiekema W.J., Pereira A.;
RT "Transposon tagging of a male sterility gene in Arabidopsis.";
RL Nature 363:715-717(1993).
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, ACTIVE SITES, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=21813653; DOI=10.1104/pp.111.181693;
RA Chen W., Yu X.-H., Zhang K., Shi J., De Oliveira S., Schreiber L.,
RA Shanklin J., Zhang D.;
RT "Male Sterile2 encodes a plastid-localized fatty acyl carrier protein
RT reductase required for pollen exine development in Arabidopsis.";
RL Plant Physiol. 157:842-853(2011).
RN [8]
RP FUNCTION [LARGE SCALE ANALYSIS], AND DISRUPTION PHENOTYPE [LARGE SCALE
RP ANALYSIS].
RX PubMed=21849515; DOI=10.1104/pp.111.179523;
RA Dobritsa A.A., Geanconteri A., Shrestha J., Carlson A., Kooyers N.,
RA Coerper D., Urbanczyk-Wochniak E., Bench B.J., Sumner L.W., Swanson R.,
RA Preuss D.;
RT "A large-scale genetic screen in Arabidopsis to identify genes involved in
RT pollen exine production.";
RL Plant Physiol. 157:947-970(2011).
RN [9]
RP REVIEW ON ACYL-LIPID METABOLISM.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
RN [10]
RP REVIEW ON POLLEN WALL DEVELOPMENT.
RX PubMed=23252839; DOI=10.1111/j.1438-8677.2012.00706.x;
RA Jiang J., Zhang Z., Cao J.;
RT "Pollen wall development: the associated enzymes and metabolic pathways.";
RL Plant Biol. 15:249-263(2013).
RN [11]
RP REPRESSION BY IMAZETHAPYR.
RC STRAIN=cv. Columbia;
RX PubMed=25348600; DOI=10.1007/s10646-014-1369-5;
RA Qian H., Li Y., Sun C., Lavoie M., Xie J., Bai X., Fu Z.;
RT "Trace concentrations of imazethapyr (IM) affect floral organs development
RT and reproduction in Arabidopsis thaliana: IM-induced inhibition of key
RT genes regulating anther and pollen biosynthesis.";
RL Ecotoxicology 24:163-171(2015).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27274541; DOI=10.18388/abp.2016_1245;
RA Doan T.T., Carlsson A.S., Stymne S., Hofvander P.;
RT "Biochemical characteristics of AtFAR2, a fatty acid reductase from
RT Arabidopsis thaliana that reduces fatty acyl-CoA and -ACP substrates into
RT fatty alcohols.";
RL Acta Biochim. Pol. 63:565-570(2016).
CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA and -ACP (acyl
CC carrier protein) substrates to fatty alcohols (PubMed:19062129,
CC PubMed:27274541). Triggers the accumulation of C16 and C18 fatty
CC alcohols; converts palmitoyl-acyl carrier protein to the corresponding
CC C16:0 alcohol with NAD(P)H as electron donor, but seems inactive toward
CC palmitoyl- or other acyl-coenzyme A (PubMed:21813653). Triggers also
CC the formation of some C16:0 aldehydes (PubMed:27274541). Involved in
CC the synthesis of the lipid component in sporopollenin
CC (PubMed:19062129). Required for exine patterning of pollen grain by
CC mediating the formation of pollen wall substances (PubMed:9351246,
CC PubMed:21813653, PubMed:21849515). {ECO:0000269|PubMed:19062129,
CC ECO:0000269|PubMed:21813653, ECO:0000269|PubMed:21849515,
CC ECO:0000269|PubMed:27274541, ECO:0000269|PubMed:9351246}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2
CC NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.84;
CC Evidence={ECO:0000269|PubMed:27274541};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC Evidence={ECO:0000269|PubMed:27274541};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-[ACP] + 2 NADPH = hexadecan-1-ol + holo-
CC [ACP] + 2 NADP(+); Xref=Rhea:RHEA:54328, Rhea:RHEA-COMP:9652,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78483; Evidence={ECO:0000269|PubMed:21813653,
CC ECO:0000269|PubMed:27274541};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54329;
CC Evidence={ECO:0000269|PubMed:21813653, ECO:0000269|PubMed:27274541};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23.3 uM for hexadecanoyl-[ACP] (at pH 6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:21813653};
CC KM=5.31 uM for hexadecanoyl-CoA (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27274541};
CC Vmax=38.3 nmol/min/mg enzyme with hexadecanoyl-[ACP] as substrate (at
CC pH 6 and 30 degrees Celsius) {ECO:0000269|PubMed:21813653};
CC Vmax=6.72 nmol/min/mg enzyme with hexadecanoyl-CoA as substrate (at
CC pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:27274541};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:21813653,
CC ECO:0000269|PubMed:27274541};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:21813653};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21813653}.
CC -!- TISSUE SPECIFICITY: Expressed in the tapetum of anthers.
CC {ECO:0000269|PubMed:9351246}.
CC -!- DEVELOPMENTAL STAGE: Expressed during microsporogenesis when
CC microspores are released from tetrads. {ECO:0000269|PubMed:9351246}.
CC -!- INDUCTION: Repressed by imazethapyr (IM), an herbicide of the
CC imidazolines family. {ECO:0000269|PubMed:25348600}.
CC -!- DISRUPTION PHENOTYPE: Male sterility (PubMed:8390620, PubMed:9351246).
CC Very thin pollen wall with abnormal exine patterning (PubMed:9351246,
CC PubMed:21813653, PubMed:21849515). {ECO:0000269|PubMed:21813653,
CC ECO:0000269|PubMed:21849515, ECO:0000269|PubMed:8390620,
CC ECO:0000269|PubMed:9351246}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
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DR EMBL; X73652; CAA52019.1; -; mRNA.
DR EMBL; EU280150; ABZ10952.1; -; mRNA.
DR EMBL; AP002040; BAB03110.1; -; Genomic_DNA.
DR EMBL; AC069473; AAG51054.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75132.1; -; Genomic_DNA.
DR PIR; S33804; S33804.
DR RefSeq; NP_187805.1; NM_112032.3.
DR AlphaFoldDB; Q08891; -.
DR STRING; 3702.AT3G11980.1; -.
DR SwissLipids; SLP:000001749; -.
DR PaxDb; Q08891; -.
DR PRIDE; Q08891; -.
DR EnsemblPlants; AT3G11980.1; AT3G11980.1; AT3G11980.
DR GeneID; 820372; -.
DR Gramene; AT3G11980.1; AT3G11980.1; AT3G11980.
DR KEGG; ath:AT3G11980; -.
DR Araport; AT3G11980; -.
DR TAIR; locus:2088664; AT3G11980.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_4_1_1; -.
DR OMA; QPYTFYG; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; Q08891; -.
DR BioCyc; ARA:AT3G11980-MON; -.
DR BioCyc; MetaCyc:AT3G11980-MON; -.
DR BRENDA; 1.2.1.42; 399.
DR BRENDA; 1.2.1.50; 399.
DR PRO; PR:Q08891; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q08891; baseline and differential.
DR Genevisible; Q08891; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:TAIR.
DR GO; GO:1903175; P:fatty alcohol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0010584; P:pollen exine formation; IMP:UniProtKB.
DR GO; GO:0009635; P:response to herbicide; IEP:UniProtKB.
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 Chloroplast; Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..14
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:21813653"
FT CHAIN 15..616
FT /note="Fatty acyl-CoA reductase 2, chloroplastic"
FT /id="PRO_0000096582"
FT MOTIF 133..143
FT /note="NAD(P)H-binding"
FT /evidence="ECO:0000303|PubMed:21813653"
FT ACT_SITE 357
FT /evidence="ECO:0000303|PubMed:21813653"
FT ACT_SITE 361
FT /evidence="ECO:0000303|PubMed:21813653"
FT CONFLICT 15
FT /note="A -> G (in Ref. 1; CAA52019)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="R -> S (in Ref. 1; CAA52019)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="V -> A (in Ref. 1; CAA52019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 616 AA; 68416 MW; BEB411E0642BECBE CRC64;
MEALFLSSSS SSIVASNKLT RLHNHCVWST VIRDKKRFGP TWCRVGGGGD GGRNSNAERP
IRVSSLLKDR GQVLIREQSS PAMDAETLVL SPNGNGRTIE INGVKTLMPF SGASMVGMKE
GLGIISFLQG KKFLITGSTG FLAKVLIEKV LRMAPDVSKI YLLIKAKSKE AAIERLKNEV
LDAELFNTLK ETHGASYMSF MLTKLIPVTG NICDSNIGLQ ADSAEEIAKE VDVIINSAAN
TTFNERYDVA LDINTRGPGN LMGFAKKCKK LKLFLQVSTA YVNGQRQGRI MEKPFSMGDC
IATENFLEGN RKALDVDREM KLALEAARKG TQNQDEAQKM KDLGLERARS YGWQDTYVFT
KAMGEMMINS TRGDVPVVII RPSVIESTYK DPFPGWMEGN RMMDPIVLCY GKGQLTGFLV
DPKGVLDVVP ADMVVNATLA AIAKHGMAMS DPEPEINVYQ IASSAINPLV FEDLAELLYN
HYKTSPCMDS KGDPIMVRLM KLFNSVDDFS DHLWRDAQER SGLMSGMSSV DSKMMQKLKF
ICKKSVEQAK HLATIYEPYT FYGGRFDNSN TQRLMENMSE DEKREFGFDV GSINWTDYIT
NVHIPGLRRH VLKGRA
