ID   FAD3E_VIGRR             Reviewed;         380 AA.
AC   P32291;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Omega-3 fatty acid desaturase, endoplasmic reticulum;
DE            EC=1.14.19.-;
DE   AltName: Full=Indole-3-acetic acid-induced protein ARG1;
GN   Name=ARG1;
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypocotyl;
RA   Yamamoto K.T., Mori H., Imaseki H.;
RT   "Novel mRNA sequences induced by indole-3-acetic acid in sections of
RT   elongating hypocotyls of mung bean (Vigna radiata).";
RL   Plant Cell Physiol. 33:13-20(1992).
CC   -!- FUNCTION: Microsomal (ER) omega-3 fatty acid desaturase introduces the
CC       third 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.
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- INDUCTION: By auxin, ethylene and wounding.
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; D14410; BAA03306.1; -; mRNA.
DR   PIR; T10898; T10898.
DR   RefSeq; NP_001304084.1; NM_001317155.1.
DR   AlphaFoldDB; P32291; -.
DR   STRING; 3916.P32291; -.
DR   GeneID; 106775023; -.
DR   KEGG; vra:106775023; -.
DR   UniPathway; UPA00658; -.
DR   Proteomes; UP000087766; Chromosome 10.
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: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   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..380
FT                   /note="Omega-3 fatty acid desaturase, endoplasmic
FT                   reticulum"
FT                   /id="PRO_0000185413"
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           97..101
FT                   /note="Histidine box-1"
FT   MOTIF           133..137
FT                   /note="Histidine box-2"
FT   MOTIF           300..304
FT                   /note="Histidine box-3"
SQ   SEQUENCE   380 AA;  43996 MW;  1C005117A8DAE16B CRC64;
     MIQAQTLQHF GNGAREGDQS YFDPGAPPPF KIADIRAAIP KHCWEKSTLR SLSYVLRDVL
     VVTALAASAI SFNSWFFWPL YWPAQGTMFW ALFVLGHDCG HGSFSNSSKL NSFVGHILHS
     LILVPYNGWR ISHRTHHQNH GHVEKDESWV PLTEKVYKNL DDMTRMLRYS FPFPIFAYPF
     YLWNRSPGKE GSHFNPYSNL FSPGERKGVV TSTLCWGIVL SVLLYLSLTI GPIFMLKLYG
     VPYLIFVMWL DFVTYLHHHG YTHKLPWYRG QEWSYLRGGL TTVDRDYGWI NNVHHDIGTH
     VIHHLFPQIP HYHLVEATKS AKSVLGKYYR EPQKSGPLPF HLLKYLLQSI SQDHFVSDTG
     DIVYYQTDPK LHQDSWTKSK