DES3_SORBI
ID DES3_SORBI Reviewed; 389 AA.
AC Q594P3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Fatty acid desaturase DES3 {ECO:0000303|PubMed:17178719};
DE Short=SbDES3 {ECO:0000303|PubMed:17178719};
DE EC=1.14.19.13 {ECO:0000269|PubMed:17178719};
GN Name=DES3 {ECO:0000303|PubMed:17178719};
GN Synonyms=SOR1 {ECO:0000303|PubMed:15361534};
GN OrderedLocusNames=Sb05g000390 {ECO:0000305};
GN ORFNames=SORBIDRAFT_05g000390 {ECO:0000312|EMBL:EES09078.1};
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:AAT72937.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15361534; DOI=10.1093/jxb/erh252;
RA Yang X., Scheffler B.E., Weston L.A.;
RT "SOR1, a gene associated with bioherbicide production in sorghum root
RT hairs.";
RL J. Exp. Bot. 55:2251-2259(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP 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 [3]
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 [4]
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 [5]
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(15) fatty acid desaturase capable of converting
CC hexadecadienoic acid into hexadecatrienoic acid (16:3(9Z,12Z,15Z))
CC (PubMed:17178719). The double bond introduced occurred between carbons
CC 15 and 16 resulting in a terminal double bond aliphatic chain
CC (PubMed:17178719). Can also convert linoleic acid (18:2(9Z,12Z)) into
CC alpha-linolenic acid (18:3(9Z,12Z,15Z)) (PubMed:17178719). Involved in
CC the biosynthesis of the aliphatic side chain of sorgoleone, a
CC phytotoxic secondary metabolite playing a direct role in allelopathic
CC interactions (PubMed:15361534, PubMed:17178719).
CC {ECO:0000269|PubMed:15361534, ECO:0000269|PubMed:17178719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-hexadecadienoyl-CoA + AH2 + O2 = (9Z,12Z,15Z)-
CC hexadecatrienoyl-CoA + A + 2 H2O; Xref=Rhea:RHEA:37599,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:76552, ChEBI:CHEBI:85914;
CC EC=1.14.19.13; Evidence={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:15361534, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY566285; AAT72937.1; -; mRNA.
DR EMBL; EF206348; ABN49521.1; -; mRNA.
DR EMBL; CM000764; EES09078.1; -; Genomic_DNA.
DR RefSeq; XP_002450090.1; XM_002450045.1.
DR AlphaFoldDB; Q594P3; -.
DR STRING; 4558.Sb05g000390.1; -.
DR EnsemblPlants; EES09078; EES09078; SORBI_3005G002700.
DR GeneID; 8079957; -.
DR Gramene; EES09078; EES09078; SORBI_3005G002700.
DR KEGG; sbi:8079957; -.
DR eggNOG; ENOG502QTIC; Eukaryota.
DR HOGENOM; CLU_033094_1_0_1; -.
DR InParanoid; Q594P3; -.
DR OMA; NKCQFVE; -.
DR OrthoDB; 577374at2759; -.
DR BioCyc; MetaCyc:MON-14103; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000000768; Chromosome 5.
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 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..389
FT /note="Fatty acid desaturase DES3"
FT /id="PRO_0000434403"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..107
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 139..143
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 306..310
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 44775 MW; BC11658129BFA335 CRC64;
MAATDHEVEE AVAKAREDDK SRRQVDGFDA GKAPPFRIGD VRAAVPEHCW RKSPWRSLWY
VVRDVAVVVA LGAAAAAMDS WAVWPLYWAV QGTMFWAFFV LGHDCGHGSF SDNATLNSVV
GHLLHSFILI PYHGWRISHR THHQNHGHVD RDESWHPLTE RRYRRLPPRA KKLRFTPPFP
LLLFPLYLFY RSPGKRGSHF LPSSPLFSPK DKGDVILSTT CWCIMLAFLL AMSCAFGPLQ
VLKMYGVPYL VSVMWLDLVT YLHHHGHQER LPWYRGEEWS YLRGGLTTVD RDYGWINSIH
HDIGTHVIHH LFPQIPHYHL VEATKAAKPV LGRYYREPHK SGPLPLHLLG VLLRSLRVDH
FVSDHGDVVY YQTDHHLNDT TTDDAHKQK
