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Database: UniProt
Entry: Q8L4V2_WHEAT
LinkDB: Q8L4V2_WHEAT
Original site: Q8L4V2_WHEAT 
ID   Q8L4V2_WHEAT            Unreviewed;       522 AA.
AC   Q8L4V2;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE            EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN   Name=TAA1b {ECO:0000313|EMBL:CAD30694.1};
GN   Synonyms=FAR5 {ECO:0000313|EMBL:AID81988.1};
GN   ORFNames=CFC21_060053 {ECO:0000313|EMBL:KAF7051861.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EMBL:CAD30694.1};
RN   [1] {ECO:0000313|EMBL:CAD30694.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Anther {ECO:0000313|EMBL:CAD30694.1};
RX   PubMed=12061894; DOI=10.1046/j.1365-313X.2002.01313.x;
RA   Wang A., Xia Q., Xie W., Dumonceaux T., Zou J., Datla R., Selvaraj G.;
RT   "Male gametophyte development in bread wheat (Triticum aestivum L.):
RT   molecular, cellular, and biochemical analyses of a sporophytic contribution
RT   to pollen wall ontogeny.";
RL   Plant J. 30:613-623(2002).
RN   [2] {ECO:0000313|EMBL:AID81988.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25468933;
RA   Wang Y., Wang M., Sun Y., Wang Y., Li T., Chai G., Jiang W., Shan L.,
RA   Li C., Xiao E., Wang Z.;
RT   "FAR5, a fatty acyl-coenzyme A reductase, is involved in primary alcohol
RT   biosynthesis of the leaf blade cuticular wax in wheat (Triticum aestivum
RT   L.).";
RL   J. Exp. Bot. 66:1165-1178(2015).
RN   [3] {ECO:0000313|EMBL:KAF7051861.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7051861.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [4] {ECO:0000313|EnsemblPlants:TraesCS4D02G008300.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS4D02G008300.1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [5] {ECO:0000313|EnsemblPlants:TraesCS4D02G008300.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [6] {ECO:0000313|EMBL:KAF7051861.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7051861.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
CC       {ECO:0000256|RuleBase:RU363097}.
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:0000256|RuleBase:RU363097};
CC   -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC       {ECO:0000256|ARBA:ARBA00005928, ECO:0000256|RuleBase:RU363097}.
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DR   EMBL; KJ725345; AID81988.1; -; Genomic_DNA.
DR   EMBL; AJ459251; CAD30694.1; -; mRNA.
DR   EMBL; AJ459252; CAD30695.1; -; Genomic_DNA.
DR   EMBL; CM022222; KAF7051861.1; -; Genomic_DNA.
DR   SMR; Q8L4V2; -.
DR   STRING; 4565.Q8L4V2; -.
DR   PaxDb; 4565-Traes_4DS_849C911C9-1; -.
DR   EnsemblPlants; TraesCS4D02G008300.1; TraesCS4D02G008300.1; TraesCS4D02G008300.
DR   Gramene; TraesCAD_scaffold_049960_01G000200.1; TraesCAD_scaffold_049960_01G000200.1; TraesCAD_scaffold_049960_01G000200.
DR   Gramene; TraesCLE_scaffold_041864_01G000200.1; TraesCLE_scaffold_041864_01G000200.1; TraesCLE_scaffold_041864_01G000200.
DR   Gramene; TraesCS4D02G008300.1; TraesCS4D02G008300.1; TraesCS4D02G008300.
DR   Gramene; TraesCS4D03G0014500.1; TraesCS4D03G0014500.1.CDS; TraesCS4D03G0014500.
DR   Gramene; TraesKAR4D01G0003430.1; cds.TraesKAR4D01G0003430.1; TraesKAR4D01G0003430.
DR   Gramene; TraesPAR_scaffold_044657_01G000100.1; TraesPAR_scaffold_044657_01G000100.1; TraesPAR_scaffold_044657_01G000100.
DR   Gramene; TraesRN4D0100015600.1; TraesRN4D0100015600.1; TraesRN4D0100015600.
DR   Gramene; TraesROB_scaffold_046527_01G000100.1; TraesROB_scaffold_046527_01G000100.1; TraesROB_scaffold_046527_01G000100.
DR   Gramene; TraesWEE_scaffold_046193_01G000200.1; TraesWEE_scaffold_046193_01G000200.1; TraesWEE_scaffold_046193_01G000200.
DR   eggNOG; KOG1221; Eukaryota.
DR   HOGENOM; CLU_024661_4_1_1; -.
DR   OMA; ALDWDSY; -.
DR   OrthoDB; 3060211at2759; -.
DR   BRENDA; 1.2.1.84; 6500.
DR   Proteomes; UP000019116; Chromosome 4D.
DR   Proteomes; UP000815260; Chromosome 4D.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0102965; F:alcohol-forming long-chain fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080019; F:alcohol-forming very long-chain fatty acyl-CoA reductase activity; IBA:GO_Central.
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; cd05236; FAR-N_SDR_e; 1.
DR   CDD; cd09071; FAR_C; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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:SF116; FATTY ACYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF03015; Sterile; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU363097};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU363097}; Membrane {ECO:0000256|RuleBase:RU363097};
KW   NADP {ECO:0000256|RuleBase:RU363097};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW   Transmembrane {ECO:0000256|RuleBase:RU363097};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT   TRANSMEM        428..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   DOMAIN          21..327
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          422..522
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
FT   REGION          334..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  58396 MW;  3DCCB0032A2DF0AC CRC64;
     MVGTLDEGKI VDYFRNKSVL ITGATGFLGK IMVEKILRVQ PDVKRIYLPV RAADAAAARR
     RVETEVVGKE LFCVLRERHG AGFDAFVADK VVGLAGDVMR EGFGVDPATL RDLRLADELN
     VIVNGAATTN FYERYDVALD VNVVGVKHMC DFARRCPNLE VLMHVSTAYV AGEKQGLVPE
     RPFRDGETLR DDGTQLDIDA EMRLAKDLRK QMEADDDVDP KAQRKAMKDL GLTRARHFGW
     PNTYVFTKSM GEMMLAQMMR GGDVPVVIVR PSIITSVQND PLPGWIEGTR TIDAILIGYA
     KQSLSCFLAD LDLTMDVMPG DMVVNAMMAA TVAHASSTQT SEPEKKPPPQ QQHPHSVPAA
     PTVYHVSSSL RHPAPYAVLY RTGIRYFEEH PRVGPDGRPV RTRKVRFLGS IAAFHLFMVL
     KYRVPLELLR LLSILCCGLF GLAALYHDLA RKYRFVMQLV DLYGPFSLFK GCFDDVNLNK
     LRLAMADGDH ADSAFNFDPK TIDWDDYFFK VHIPGVMKYV HK
//
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