DES2_SORBI
ID DES2_SORBI Reviewed; 385 AA.
AC A3F5L3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Fatty acid desaturase DES2 {ECO:0000303|PubMed:17178719};
DE Short=SbDES2 {ECO:0000303|PubMed:17178719};
DE EC=1.14.19.- {ECO:0000305};
GN Name=DES2 {ECO:0000303|PubMed:17178719};
GN OrderedLocusNames=Sb04g029900 {ECO:0000305};
GN ORFNames=SORBIDRAFT_04g029900 {ECO:0000312|EMBL:EES05625.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000312|EMBL:ABN49520.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17178719; DOI=10.1074/jbc.m606343200;
RA Pan Z., Rimando A.M., Baerson S.R., Fishbein M., Duke S.O.;
RT "Functional characterization of desaturases involved in the formation of
RT the terminal double bond of an unusual 16:3Delta(9,12,150) fatty acid
RT isolated from Sorghum bicolor root hairs.";
RL J. Biol. Chem. 282:4326-4335(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623;
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M.,
RA Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [3]
RP INDUCTION BY AUXIN.
RX PubMed=22087851; DOI=10.1021/jf2024402;
RA Uddin M.R., Park W.T., Kim Y.K., Pyon J.Y., Park S.U.;
RT "Effects of auxins on sorgoleone accumulation and genes for sorgoleone
RT biosynthesis in sorghum roots.";
RL J. Agric. Food Chem. 59:12948-12953(2011).
RN [4]
RP INDUCTION BY JASMONATE AND METHYL JASMONATE.
RX PubMed=23702703; DOI=10.1007/s10886-013-0299-7;
RA Uddin M.R., Thwe A.A., Kim Y.B., Park W.T., Chae S.C., Park S.U.;
RT "Effects of jasmonates on sorgoleone accumulation and expression of genes
RT for sorgoleone biosynthesis in sorghum roots.";
RL J. Chem. Ecol. 39:712-722(2013).
CC -!- FUNCTION: Delta(12) fatty acid desaturase converting palmitoleic acid
CC (16:1(9)) to hexadecadienoic acid (16:2(9,12)). No detectable
CC Delta(12)linoleate desaturase activity. Involved in the biosynthesis of
CC the aliphatic side chain of sorgoleone, a phytotoxic secondary
CC metabolite playing a direct role in allelopathic interactions.
CC {ECO:0000269|PubMed:17178719}.
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in root hair cells. Barely
CC detected in panicle, shoot apex, stems and leaves.
CC {ECO:0000269|PubMed:17178719}.
CC -!- INDUCTION: Up-regulated upon auxin treatment (PubMed:22087851). Up-
CC regulated by jasmonate and methyl jasmonate (PubMed:23702703).
CC {ECO:0000269|PubMed:22087851, ECO:0000269|PubMed:23702703}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; EF206347; ABN49520.1; -; mRNA.
DR EMBL; CM000763; EES05625.1; -; Genomic_DNA.
DR RefSeq; XP_002452649.1; XM_002452604.1.
DR AlphaFoldDB; A3F5L3; -.
DR STRING; 4558.Sb04g029900.1; -.
DR EnsemblPlants; EES05625; EES05625; SORBI_3004G260600.
DR GeneID; 8066368; -.
DR Gramene; EES05625; EES05625; SORBI_3004G260600.
DR KEGG; sbi:8066368; -.
DR eggNOG; ENOG502QQNB; Eukaryota.
DR HOGENOM; CLU_033094_0_1_1; -.
DR InParanoid; A3F5L3; -.
DR OMA; AHCNERS; -.
DR OrthoDB; 577374at2759; -.
DR BioCyc; MetaCyc:MON-14102; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000000768; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:InterPro.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR Pfam; PF11960; DUF3474; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..385
FT /note="Fatty acid desaturase DES2"
FT /id="PRO_0000434402"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 110..114
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 146..150
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 321..325
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 44209 MW; E8DFD8C01A9E46D3 CRC64;
MGAGGKMTEQ EREKQEQQLA RGASTMQRSP VEKPPFTVGQ IKKAIPPHCF QRSVLKSFSY
VVRDLVIAAA LLYFALAIIP ALPSPLHYAA WPLYWIAQGC VCFAMWVIAH ECGHHAFSDY
QLLDDIVGLV LHSSLMVPYF SWKYSHRRHH SNTGSLERDE VFVPKTKGAL AWYAPYVYNN
PVGRLVHIVV QLTLGWPLYL ATNVSGRPYP RFACHYDPYG PIYNDRERAQ IFVSDAGVMA
VSFGLYKLAA TLGFWWVVRV YAVPLLIVNV WLVLVTYLHH THPALPHYDS REWDWLRGAL
STVDRDYGVF NRFFHNITDT HVVHHLFSTL PHFHATEATK AIKPILGEYY QFDPTPIAKA
TWREARECIF VEPEEGRGVF WYNKF
