ID   DES1_SORBI              Reviewed;         388 AA.
AC   A3F5L2;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Probable fatty acid desaturase DES1 {ECO:0000303|PubMed:17178719};
DE            Short=SbDES1 {ECO:0000303|PubMed:17178719};
GN   Name=DES1 {ECO:0000303|PubMed:17178719};
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:ABN49519.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], 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).
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   -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC       involved in metal ion binding. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Exhibits no detectable activity in the heterologous
CC       expression system tested. {ECO:0000269|PubMed:17178719}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; EF206346; ABN49519.1; -; mRNA.
DR   AlphaFoldDB; A3F5L2; -.
DR   STRING; 4558.Sb08g000430.1; -.
DR   EnsemblPlants; KXG22757; KXG22757; SORBI_3008G002800.
DR   Gramene; KXG22757; KXG22757; SORBI_3008G002800.
DR   eggNOG; ENOG502QTIC; Eukaryota.
DR   OrthoDB; 577374at2759; -.
DR   BioCyc; MetaCyc:MON-19092; -.
DR   UniPathway; UPA00658; -.
DR   ExpressionAtlas; A3F5L2; baseline and differential.
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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..388
FT                   /note="Probable fatty acid desaturase DES1"
FT                   /id="PRO_0000434401"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           107..111
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           143..147
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           310..314
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        12..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  44662 MW;  CF0491895D12BA8F CRC64;
     MATTPMTVVD HEAEEAVAKA REDDKSRQVD AFDAGKPPPF RIGDVRAAVP EHCWHKSPWR
     SLWYVVRDVA AVVALGTAAA AMDSWAVWPV YWAVQGTMFW AFFVLGHDCG HGSFSDSRTL
     NSVVGHLLHS FILIPYHGWR ISHRTHHQNH GHVDRDESWH PITEGRYRRL PPRAKKIRFT
     APYPLLLFPL YLFYRGPDKP GTHFLPSSEL FSPKEKGDVM LSTTCWCIML ASLLAMSCAF
     GPLQVLKMYG LPYLVFVMWL DLVTYLHHHG HHERLPWYRG EEWSYLRGGL TTVDRDYGWI
     NKIHHDIGTH VIHHLFPQIP HYHLVEATKA AKPVLGRYYR EPQKSGPLPL PLLGVFLRSI
     RVNHFVSDHG DVVYYQTDHH LNDTTKQK