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Fatty acyl-CoA reductase 2 (EC 1.2.1.84) (Fatty acid reductase 2) (Male sterility protein 2)

 FACR2_ARATH             Reviewed;         616 AA.
Q08891; B9TSP6; Q9LHM3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
10-OCT-2018, entry version 127.
RecName: Full=Fatty acyl-CoA reductase 2 {ECO:0000305};
EC=1.2.1.84 {ECO:0000269|PubMed:19062129};
AltName: Full=Fatty acid reductase 2;
AltName: Full=Male sterility protein 2;
Name=FAR2; Synonyms=MS2; OrderedLocusNames=At3g11980;
ORFNames=MEC18.1, T21B14.18, T21B14_123;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta; TISSUE=Flower;
PubMed=8390620; DOI=10.1038/363715a0;
Aarts M.G.M., Dirkse W.G., Stiekema W.J., Pereira A.;
"Transposon tagging of a male sterility gene in Arabidopsis.";
Nature 363:715-717(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=19062129; DOI=10.1016/j.jplph.2008.10.003;
Doan T.P.T., Carlsson A.S., Hamberg M., Buelow L., Stymne S.,
Olsson P.;
"Functional expression of five Arabidopsis fatty acyl-CoA reductase
genes in Escherichia coli.";
J. Plant Physiol. 166:787-796(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=9351246; DOI=10.1046/j.1365-313X.1997.00615.x;
Aarts M.G.M., Hodge R.P., Kalantidis K., Florack D., Wilson Z.A.,
Mulligan B.J., Stiekema W.J., Scott R., Pereira A.;
"The Arabidopsis MALE STERILITY 2 protein shares similarity with
reductases in elongation/condensation complexes.";
Plant J. 12:615-623(1997).
-!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty
alcohols. Involved in the synthesis of the lipid component in
sporopollenin. {ECO:0000269|PubMed:19062129,
ECO:0000269|PubMed:9351246}.
-!- CATALYTIC ACTIVITY: A long-chain acyl-CoA + 2 NADPH = CoA + a
long-chain alcohol + 2 NADP(+). {ECO:0000269|PubMed:19062129}.
-!- TISSUE SPECIFICITY: Expressed in tapetum.
{ECO:0000269|PubMed:9351246}.
-!- DEVELOPMENTAL STAGE: Expressed during microsporogenesis when
microspores are released from tetrads.
{ECO:0000269|PubMed:9351246}.
-!- DISRUPTION PHENOTYPE: Male sterility. {ECO:0000269|PubMed:8390620,
ECO:0000269|PubMed:9351246}.
-!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
{ECO:0000305}.
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EMBL; X73652; CAA52019.1; -; mRNA.
EMBL; EU280150; ABZ10952.1; -; mRNA.
EMBL; AP002040; BAB03110.1; -; Genomic_DNA.
EMBL; AC069473; AAG51054.1; -; Genomic_DNA.
EMBL; CP002686; AEE75132.1; -; Genomic_DNA.
PIR; S33804; S33804.
RefSeq; NP_187805.1; NM_112032.3.
UniGene; At.5397; -.
ProteinModelPortal; Q08891; -.
STRING; 3702.AT3G11980.1; -.
SwissLipids; SLP:000001749; -.
PaxDb; Q08891; -.
PRIDE; Q08891; -.
EnsemblPlants; AT3G11980.1; AT3G11980.1; AT3G11980.
GeneID; 820372; -.
Gramene; AT3G11980.1; AT3G11980.1; AT3G11980.
KEGG; ath:AT3G11980; -.
Araport; AT3G11980; -.
TAIR; locus:2088664; AT3G11980.
eggNOG; KOG1221; Eukaryota.
eggNOG; ENOG410XS7R; LUCA.
HOGENOM; HOG000242967; -.
KO; K13356; -.
OMA; QPYTFYG; -.
OrthoDB; EOG093609GH; -.
PhylomeDB; Q08891; -.
BioCyc; ARA:AT3G11980-MONOMER; -.
BioCyc; MetaCyc:AT3G11980-MONOMER; -.
BRENDA; 1.2.1.42; 399.
BRENDA; 1.2.1.50; 399.
Reactome; R-ATH-8848584; Wax biosynthesis.
PRO; PR:Q08891; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q08891; baseline and differential.
Genevisible; Q08891; AT.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IDA:TAIR.
GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:TAIR.
GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
GO; GO:0010345; P:suberin biosynthetic process; IBA:GO_Central.
CDD; cd09071; FAR_C; 1.
InterPro; IPR026055; FAR.
InterPro; IPR033640; FAR_C.
InterPro; IPR013120; Male_sterile_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR11011; PTHR11011; 1.
Pfam; PF07993; NAD_binding_4; 1.
Pfam; PF03015; Sterile; 1.
SUPFAM; SSF51735; SSF51735; 2.
1: Evidence at protein level;
Complete proteome; Lipid biosynthesis; Lipid metabolism; NADP;
Oxidoreductase; Reference proteome.
CHAIN 1 616 Fatty acyl-CoA reductase 2.
/FTId=PRO_0000096582.
COMPBIAS 7 12 Poly-Ser.
COMPBIAS 46 52 Poly-Gly.
CONFLICT 15 15 A -> G (in Ref. 1; CAA52019).
{ECO:0000305}.
CONFLICT 59 59 R -> S (in Ref. 1; CAA52019).
{ECO:0000305}.
CONFLICT 530 530 V -> A (in Ref. 1; CAA52019).
{ECO:0000305}.
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


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