FAD6E_BRAJU
ID FAD6E_BRAJU Reviewed; 384 AA.
AC Q39287;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Omega-6 fatty acid desaturase, endoplasmic reticulum;
DE EC=1.14.19.-;
DE AltName: Full=Delta(12) desaturase;
OS Brassica juncea (Indian mustard) (Sinapis juncea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. 651-2-5-7-4;
RA Singh S.P., van der Heide T., McKinney S., Green A.;
RT "Nucleotide sequence of a cDNA from Brassica juncea encoding a microsomal
RT omega-6 desaturase.";
RL (er) Plant Gene Register PGR95-107(1995).
CC -!- FUNCTION: ER (microsomal) omega-6 fatty acid desaturase introduces the
CC second double bond in the biosynthesis of 18:3 fatty acids, important
CC constituents of plant membranes. It is thought to use cytochrome b5 as
CC an electron donor and to act on fatty acids esterified to
CC phosphatidylcholine and, possibly, other phospholipids (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X91139; CAA62578.1; -; mRNA.
DR AlphaFoldDB; Q39287; -.
DR UniPathway; UPA00658; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005804; FA_desaturase_dom.
DR Pfam; PF00487; FA_desaturase; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..384
FT /note="Omega-6 fatty acid desaturase, endoplasmic
FT reticulum"
FT /id="PRO_0000185419"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 105..109
FT /note="Histidine box-1"
FT MOTIF 141..145
FT /note="Histidine box-2"
FT MOTIF 316..320
FT /note="Histidine box-3"
SQ SEQUENCE 384 AA; 44315 MW; 43AF77CE9861A492 CRC64;
MGAGGRMQVS PSPKKSETDT LKRVPCETPP FTVGELKKAI PPHCFKRSIP RSFSYLIWDI
IVASCFYYVA TTYFPLLPHP LSYVAWPLYW ACQGVVLTGV WVIAHECGHH AFSDYQWLDD
TVGLIFHSFL LVPYFSWKYS HRRHHSNTGS LERDEVFVPK KKSDIKWYGK YLNNPLGRTV
MLTVQFTLGW PLYWAFNVSG RPYPEGFACH FHPNAPIYND RERLQIYVSD AGILAVCYGL
YRYAAAQGVA SMVCLYGVPL LIVNAFLVLI TYLQHTHPSL PHYDSSEWDW LRGALATVDR
DYGILNKVFH NITDTHVAHH LFSTMPHYHA MEVTKAIKPI LGDYYQFDGT PWVKAMWREA
KECIYVEPDR QGEKKGVFWY NNKL
