FAD6E_ARATH
ID FAD6E_ARATH Reviewed; 383 AA.
AC P46313; Q19MZ0; Q8LFZ8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Delta(12)-fatty-acid desaturase {ECO:0000303|PubMed:7907506};
DE Short=Fatty acid desaturase 2 {ECO:0000303|PubMed:7907506};
DE EC=1.14.19.22 {ECO:0000269|PubMed:1730697};
DE EC=1.14.19.6 {ECO:0000269|PubMed:8685264};
DE AltName: Full=Omega-6 fatty acid desaturase, endoplasmic reticulum {ECO:0000303|PubMed:7907506};
GN Name=FAD2 {ECO:0000303|PubMed:7907506};
GN OrderedLocusNames=At3g12120 {ECO:0000312|Araport:AT3G12120};
GN ORFNames=T21B14.6 {ECO:0000312|EMBL:AAG51042.1}, T21B14_107,
GN T23B7.6 {ECO:0000312|EMBL:BAB01960.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY COLD, AND TISSUE
RP SPECIFICITY.
RX PubMed=7907506; DOI=10.2307/3869682;
RA Okuley J., Lightner J., Feldmann K.A., Yadav N., Lark E., Browse J.;
RT "Arabidopsis FAD2 gene encodes the enzyme that is essential for
RT polyunsaturated lipid synthesis.";
RL Plant Cell 6:147-158(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-267.
RA Zhang J., Yang Y., Xie Y., Huang B.;
RT "Phylogenetic relationships in Brassicas and related species based on
RT genomic sequences of delta-12 desaturase.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=1730697; DOI=10.1016/s0021-9258(18)45974-1;
RA Miquel M., Browse J.;
RT "Arabidopsis mutants deficient in polyunsaturated fatty acid synthesis.
RT Biochemical and genetic characterization of a plant oleoyl-
RT phosphatidylcholine desaturase.";
RL J. Biol. Chem. 267:1502-1509(1992).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8685264; DOI=10.1104/pp.111.1.223;
RA Covello P.S., Reed D.W.;
RT "Functional expression of the extraplastidial Arabidopsis thaliana oleate
RT desaturase gene (FAD2) in Saccharomyces cerevisiae.";
RL Plant Physiol. 111:223-226(1996).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ALA-63; ALA-104; THR-148; TYR-217; ALA-295;
RP SER-322 AND MET-324.
RX PubMed=9812895; DOI=10.1126/science.282.5392.1315;
RA Broun P., Shanklin J., Whittle E., Somerville C.;
RT "Catalytic plasticity of fatty acid modification enzymes underlying
RT chemical diversity of plant lipids.";
RL Science 282:1315-1317(1998).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11104757; DOI=10.1074/jbc.m006231200;
RA Caiveau O., Fortune D., Cantrel C., Zachowski A., Moreau F.;
RT "Consequences of omega -6-oleate desaturase deficiency on lipid dynamics
RT and functional properties of mitochondrial membranes of Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 276:5788-5794(2001).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF ALA-104; THR-148; SER-322 AND MET-324.
RX PubMed=11864983; DOI=10.1074/jbc.m200231200;
RA Broadwater J.A., Whittle E., Shanklin J.;
RT "Desaturation and hydroxylation. Residues 148 and 324 of Arabidopsis FAD2,
RT in addition to substrate chain length, exert a major influence in
RT partitioning of catalytic specificity.";
RL J. Biol. Chem. 277:15613-15620(2002).
RN [13]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=14690501; DOI=10.1111/j.1365-313x.2004.01949.x;
RA McCartney A.W., Dyer J.M., Dhanoa P.K., Kim P.K., Andrews D.W., McNew J.A.,
RA Mullen R.T.;
RT "Membrane-bound fatty acid desaturases are inserted co-translationally into
RT the ER and contain different ER retrieval motifs at their carboxy
RT termini.";
RL Plant J. 37:156-173(2004).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17507388; DOI=10.1093/pcp/pcm061;
RA Matos A.R., Hourton-Cabassa C., Cicek D., Reze N., Arrabaca J.D.,
RA Zachowski A., Moreau F.;
RT "Alternative oxidase involvement in cold stress response of Arabidopsis
RT thaliana fad2 and FAD3+ cell suspensions altered in membrane lipid
RT composition.";
RL Plant Cell Physiol. 48:856-865(2007).
RN [15]
RP MUTAGENESIS OF ALA-335.
RX PubMed=20345604; DOI=10.1111/j.1365-313x.2010.04212.x;
RA Song W., Maeda H., DellaPenna D.;
RT "Mutations of the ER to plastid lipid transporters TGD1, 2, 3 and 4 and the
RT ER oleate desaturase FAD2 suppress the low temperature-induced phenotype of
RT Arabidopsis tocopherol-deficient mutant vte2.";
RL Plant J. 62:1004-1018(2010).
RN [16]
RP CATALYTIC ACTIVITY.
RX PubMed=22041902; DOI=10.1074/jbc.m111.266114;
RA Zhou X.-R., Green A.G., Singh S.P.;
RT "Caenorhabditis elegans Delta12-desaturase FAT-2 is a bifunctional
RT desaturase able to desaturate a diverse range of fatty acid substrates at
RT the Delta12 and Delta15 positions.";
RL J. Biol. Chem. 286:43644-43650(2011).
RN [17]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY OSMOTIC
RP STRESS, AND MUTAGENESIS OF ALA-104.
RX PubMed=22279586; DOI=10.1371/journal.pone.0030355;
RA Zhang J., Liu H., Sun J., Li B., Zhu Q., Chen S., Zhang H.;
RT "Arabidopsis fatty acid desaturase FAD2 is required for salt tolerance
RT during seed germination and early seedling growth.";
RL PLoS ONE 7:E30355-E30355(2012).
RN [18]
RP SUBUNIT, AND INTERACTION WITH FAD3.
RX PubMed=24811169; DOI=10.1074/jbc.m114.572883;
RA Lou Y., Schwender J., Shanklin J.;
RT "FAD2 and FAD3 desaturases form heterodimers that facilitate metabolic
RT channeling in vivo.";
RL J. Biol. Chem. 289:17996-18007(2014).
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 (PubMed:14593172, PubMed:7907506).
CC Delta(12)-desaturase with regioselectivity determined by the double
CC bond (delta(9) position) and carboxyl group of the substrate. Can use
CC both 16:1 and 18:1 fatty acids as substrates (PubMed:8685264). It is
CC thought to use cytochrome b5 as an electron donor and to act on fatty
CC acids esterified to phosphatidylcholine (PC) and, possibly, other
CC phospholipids (PubMed:14593172, PubMed:7907506, PubMed:1730697). Very
CC low constitutive hydroxylation activity (PubMed:11864983). Required for
CC desaturation of fatty acids present in extraplastidial membranes,
CC including mitochondria (PubMed:11104757, PubMed:17507388). Required for
CC salt tolerance during seed germination and early seedling growth
CC (PubMed:22279586). {ECO:0000269|PubMed:11104757,
CC ECO:0000269|PubMed:11864983, ECO:0000269|PubMed:14593172,
CC ECO:0000269|PubMed:1730697, ECO:0000269|PubMed:17507388,
CC ECO:0000269|PubMed:22279586, ECO:0000269|PubMed:7907506,
CC ECO:0000269|PubMed:8685264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:25856, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57387; EC=1.14.19.6;
CC Evidence={ECO:0000269|PubMed:8685264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:45096, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:61540,
CC ChEBI:CHEBI:76552; EC=1.14.19.6;
CC Evidence={ECO:0000269|PubMed:8685264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z)-octadecenoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a (9Z,12Z)-octadecadienoyl-containing
CC glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46332, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88240,
CC ChEBI:CHEBI:88351; EC=1.14.19.22;
CC Evidence={ECO:0000269|PubMed:1730697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + AH2 + O2 = (9Z,12Z)-octadecadienoyl-
CC CoA + A + 2 H2O; Xref=Rhea:RHEA:36863, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36864;
CC Evidence={ECO:0000269|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + AH2 + O2 = (9Z,12Z)-hexadecadienoyl-
CC CoA + A + 2 H2O; Xref=Rhea:RHEA:39671, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:76552;
CC Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39672;
CC Evidence={ECO:0000269|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (9Z,12Z)-tetradecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:42176, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:65060,
CC ChEBI:CHEBI:78680; Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42177;
CC Evidence={ECO:0000269|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-pentadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (9Z,12Z)-pentadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:42192, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74310,
CC ChEBI:CHEBI:78684; Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42193;
CC Evidence={ECO:0000269|PubMed:22041902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-heptadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (9Z,12Z)-heptadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:42196, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74308,
CC ChEBI:CHEBI:78690; Evidence={ECO:0000269|PubMed:22041902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42197;
CC Evidence={ECO:0000269|PubMed:22041902};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBUNIT: Homo- and heterodimer (PubMed:24811169). Interacts with FAD3
CC but not with FAD6 (PubMed:24811169). FAD2-FAD3 heterodimers can form a
CC metabolic channel in which 18:1-PC is converted to 18:3-PC without
CC releasing a free 18:2-PC intermediate (PubMed:24811169).
CC {ECO:0000269|PubMed:24811169}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14690501, ECO:0000305|PubMed:7907506}; Multi-pass
CC membrane protein {ECO:0000255}. Microsome membrane
CC {ECO:0000269|PubMed:1730697}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots and roots (PubMed:7907506,
CC PubMed:22279586). Expressed in leaves, stems, flowers and siliques
CC (PubMed:22279586). {ECO:0000269|PubMed:22279586,
CC ECO:0000269|PubMed:7907506}.
CC -!- INDUCTION: Up-regulated by osmotic stress (PubMed:22279586). Not
CC regulated by cold stress (PubMed:7907506).
CC {ECO:0000269|PubMed:22279586, ECO:0000269|PubMed:7907506}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding (Probable). The C-terminal sequence (-
CC YNNKL) is necessary and sufficient for maintaining localization in the
CC endoplasmic reticulum (PubMed:14690501). {ECO:0000269|PubMed:14690501,
CC ECO:0000305|PubMed:7907506}.
CC -!- DISRUPTION PHENOTYPE: Enhancement of both microviscosity and
CC lipid/protein ratio of mitochondrial membranes, which in turn were
CC responsible for the change in lateral mobility of lipids and for
CC bioenergetic parameter modifications (PubMed:11104757). Increased
CC membrane rigidity and cold sensitivity (PubMed:17507388).
CC Hypersensitivity to salt or osmotic stress (PubMed:22279586).
CC {ECO:0000269|PubMed:11104757, ECO:0000269|PubMed:17507388,
CC ECO:0000269|PubMed:22279586}.
CC -!- MISCELLANEOUS: Introduction of Ile at position 146 or 324 has a
CC dominant role in specifying hydroxylation activity.
CC {ECO:0000269|PubMed:11864983}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; L26296; AAA32782.1; -; mRNA.
DR EMBL; AP002063; BAB01960.1; -; Genomic_DNA.
DR EMBL; AC069473; AAG51042.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75152.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75153.1; -; Genomic_DNA.
DR EMBL; AY039572; AAK62627.1; -; mRNA.
DR EMBL; AY142057; AAM98321.1; -; mRNA.
DR EMBL; AY084545; AAM61113.1; -; mRNA.
DR EMBL; DQ518270; ABF70287.1; -; Genomic_DNA.
DR RefSeq; NP_001319529.1; NM_001337975.1.
DR RefSeq; NP_187819.1; NM_112047.4.
DR AlphaFoldDB; P46313; -.
DR BioGRID; 5721; 3.
DR STRING; 3702.AT3G12120.1; -.
DR SwissLipids; SLP:000000808; -.
DR PaxDb; P46313; -.
DR PRIDE; P46313; -.
DR ProteomicsDB; 230847; -.
DR EnsemblPlants; AT3G12120.1; AT3G12120.1; AT3G12120.
DR EnsemblPlants; AT3G12120.2; AT3G12120.2; AT3G12120.
DR GeneID; 820387; -.
DR Gramene; AT3G12120.1; AT3G12120.1; AT3G12120.
DR Gramene; AT3G12120.2; AT3G12120.2; AT3G12120.
DR KEGG; ath:AT3G12120; -.
DR Araport; AT3G12120; -.
DR TAIR; locus:2099297; AT3G12120.
DR eggNOG; ENOG502QQNB; Eukaryota.
DR HOGENOM; CLU_033094_0_1_1; -.
DR InParanoid; P46313; -.
DR OMA; FYLFHNY; -.
DR OrthoDB; 577374at2759; -.
DR PhylomeDB; P46313; -.
DR BioCyc; MetaCyc:AT3G12120-MON; -.
DR BRENDA; 1.14.19.22; 399.
DR UniPathway; UPA00658; -.
DR PRO; PR:P46313; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P46313; baseline and differential.
DR Genevisible; P46313; AT.
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:0102871; F:1-16:0-2-18:1-phosphatidylcholine desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102855; F:1-18:1-2-18:2-phosphatidylcholine desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102860; F:1-18:1-2-18:2-phosphatidylcholine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102857; F:1-18:1-2-18:3-phosphatidylcholinedesaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102861; F:1-18:2-2-18:1-phosphatidylcholine desaturase activity (SN2-18:2 forming); IEA:UniProtKB-EC.
DR GO; GO:0102985; F:delta12-fatty-acid desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0045485; F:omega-6 fatty acid desaturase activity; IDA:TAIR.
DR GO; GO:0102987; F:palmitoleic acid delta 12 desaturase activity; IEA:RHEA.
DR GO; GO:0050184; F:phosphatidylcholine desaturase activity; IEA:UniProtKB-EC.
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 Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Microsome; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..383
FT /note="Delta(12)-fatty-acid desaturase"
FT /id="PRO_0000185418"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 105..109
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 141..145
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 315..319
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT MUTAGEN 63
FT /note="A->V: In m7FAD2/L7M; Converted from a desaturase to
FT a bifunctional desaturase/hydroxylase; when associated with
FT G-104; N-148; F-217; V-295; A-322 and I-324."
FT /evidence="ECO:0000269|PubMed:9812895"
FT MUTAGEN 104
FT /note="A->G: Produces less than 1% hydroxy fatty acid. In
FT m7FAD2/L7M; Converted from a desaturase to a bifunctional
FT desaturase/hydroxylase; when associated with V-63; N-148;
FT F-217; V-295; A-322 and I-324. In C4M; Converted from a
FT desaturase to a bifunctional desaturase/hydroxylase with a
FT high hydroxylase activity; when associated with I-148; A-
FT 322 and V-324."
FT /evidence="ECO:0000269|PubMed:11864983,
FT ECO:0000269|PubMed:9812895"
FT MUTAGEN 104
FT /note="A->T: Increased monounsaturated and decreased
FT polyunsaturated fatty acid levels."
FT /evidence="ECO:0000269|PubMed:22279586"
FT MUTAGEN 148
FT /note="T->I: Produces up to 4.2% hydroxy fatty acid. In
FT C4M; Converted from a desaturase to a bifunctional
FT desaturase/hydroxylase with a high hydroxylase activity;
FT when associated with G-104; A-322 and V-324."
FT /evidence="ECO:0000269|PubMed:11864983"
FT MUTAGEN 148
FT /note="T->N: Produces less than 1% hydroxy fatty acid. In
FT m7FAD2/L7M; Converted from a desaturase to a bifunctional
FT desaturase/hydroxylase; when associated with V-63; G-104;
FT F-217; V-295; A-322 and I-324. In m4FAD2/L4M; Converted
FT from a desaturase to a bifunctional desaturase/hydroxylase;
FT when associated with V-295; A-322 and I-324."
FT /evidence="ECO:0000269|PubMed:11864983,
FT ECO:0000269|PubMed:9812895"
FT MUTAGEN 217
FT /note="Y->F: In m7FAD2/L7M; Converted from a desaturase to
FT a bifunctional desaturase/hydroxylase; when associated with
FT V-63; G-104; N-148; V-295; A-322 and I-324."
FT /evidence="ECO:0000269|PubMed:9812895"
FT MUTAGEN 295
FT /note="A->V: In m7FAD2/L7M; Converted from a desaturase to
FT a bifunctional desaturase/hydroxylase; when associated with
FT V-63; G-104; N-148; F-217; A-322 and I-324. In m4FAD2/L4M;
FT Converted from a desaturase to a bifunctional
FT desaturase/hydroxylase; when associated with N-148; A-322
FT and I-324."
FT /evidence="ECO:0000269|PubMed:9812895"
FT MUTAGEN 322
FT /note="S->A: Produces less than 1% hydroxy fatty acid. In
FT m7FAD2/L7M; Converted from a desaturase to a bifunctional
FT desaturase/hydroxylase; when associated with V-63; G-104;
FT N-148; F-217; V-295 and I-324. In m4FAD2/L4M; Converted
FT from a desaturase to a bifunctional desaturase/hydroxylase;
FT when associated with N-148; V-295 and I-324. In C4M;
FT Converted from a desaturase to a bifunctional
FT desaturase/hydroxylase with a high hydroxylase activity;
FT when associated with G-104; I-148 and V-324."
FT /evidence="ECO:0000269|PubMed:11864983,
FT ECO:0000269|PubMed:9812895"
FT MUTAGEN 324
FT /note="M->I: Produces up to 5.4% hydroxy fatty acid. In
FT m7FAD2/L7M; Converted from a desaturase to a bifunctional
FT desaturase/hydroxylase; when associated with V-63; G-104;
FT N-148; F-217; V-295 and A-322. In m4FAD2/L4M; Converted
FT from a desaturase to a bifunctional desaturase/hydroxylase;
FT when associated with N-148; V-295 and A-322."
FT /evidence="ECO:0000269|PubMed:11864983,
FT ECO:0000269|PubMed:9812895"
FT MUTAGEN 324
FT /note="M->V: In C4M; Converted from a desaturase to a
FT bifunctional desaturase/hydroxylase with a high hydroxylase
FT activity; when associated with G-104; I-148 and A-322."
FT /evidence="ECO:0000269|PubMed:11864983"
FT MUTAGEN 335
FT /note="A->T: In sve1; Altered fatty acid composition and
FT suppresses the low temperature-induced phenotype of
FT tocopherol-deficient mutant."
FT /evidence="ECO:0000269|PubMed:20345604"
SQ SEQUENCE 383 AA; 44048 MW; 8815ADD2D3BBC982 CRC64;
MGAGGRMPVP TSSKKSETDT TKRVPCEKPP FSVGDLKKAI PPHCFKRSIP RSFSYLISDI
IIASCFYYVA TNYFSLLPQP LSYLAWPLYW ACQGCVLTGI WVIAHECGHH AFSDYQWLDD
TVGLIFHSFL LVPYFSWKYS HRRHHSNTGS LERDEVFVPK QKSAIKWYGK YLNNPLGRIM
MLTVQFVLGW PLYLAFNVSG RPYDGFACHF FPNAPIYNDR ERLQIYLSDA GILAVCFGLY
RYAAAQGMAS MICLYGVPLL IVNAFLVLIT YLQHTHPSLP HYDSSEWDWL RGALATVDRD
YGILNKVFHN ITDTHVAHHL FSTMPHYNAM EATKAIKPIL GDYYQFDGTP WYVAMYREAK
ECIYVEPDRE GDKKGVYWYN NKL
