{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P46313","secondaryAccessions":["Q19MZ0","Q8LFZ8"],"uniProtkbId":"FAD6E_ARATH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":181,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Arabidopsis thaliana","commonName":"Mouse-ear cress","taxonId":3702,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7907506"}],"value":"Delta(12)-fatty-acid desaturase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7907506"}],"value":"Fatty acid desaturase 2"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1730697"}],"value":"1.14.19.22"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8685264"}],"value":"1.14.19.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7907506"}],"value":"Omega-6 fatty acid desaturase, endoplasmic reticulum"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7907506"}],"value":"FAD2"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"Araport","id":"AT3G12120"}],"value":"At3g12120"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAG51042.1"}],"value":"T21B14.6"},{"value":"T21B14_107"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"BAB01960.1"}],"value":"T23B7.6"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11104757"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11864983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14593172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1730697"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17507388"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22279586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7907506"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8685264"}],"value":"ER (microsomal) omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes (PubMed:14593172, PubMed:7907506). Delta(12)-desaturase with regioselectivity determined by the double bond (delta(9) position) and carboxyl group of the substrate. Can use both 16:1 and 18:1 fatty acids as substrates (PubMed:8685264). It is thought to use cytochrome b5 as an electron donor and to act on fatty acids esterified to phosphatidylcholine (PC) and, possibly, other phospholipids (PubMed:14593172, PubMed:1730697, PubMed:7907506). Very low constitutive hydroxylation activity (PubMed:11864983). Required for desaturation of fatty acids present in extraplastidial membranes, including mitochondria (PubMed:11104757, PubMed:17507388). Required for salt tolerance during seed germination and early seedling growth (PubMed:22279586)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25856"},{"database":"Rhea","id":"RHEA-COMP:10438"},{"database":"Rhea","id":"RHEA-COMP:10439"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"},{"database":"ChEBI","id":"CHEBI:57383"},{"database":"ChEBI","id":"CHEBI:57387"}],"ecNumber":"1.14.19.6","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8685264"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (9Z,12Z)-hexadecadienoyl-CoA + 2 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H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46332"},{"database":"Rhea","id":"RHEA-COMP:10438"},{"database":"Rhea","id":"RHEA-COMP:10439"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"},{"database":"ChEBI","id":"CHEBI:88240"},{"database":"ChEBI","id":"CHEBI:88351"}],"ecNumber":"1.14.19.22","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1730697"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-octadecenoyl-CoA + AH2 + O2 = (9Z,12Z)-octadecadienoyl-CoA + A + 2 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H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42176"},{"database":"Rhea","id":"RHEA-COMP:10438"},{"database":"Rhea","id":"RHEA-COMP:10439"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"},{"database":"ChEBI","id":"CHEBI:65060"},{"database":"ChEBI","id":"CHEBI:78680"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22041902"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:42177"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22041902"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-pentadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (9Z,12Z)-pentadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42192"},{"database":"Rhea","id":"RHEA-COMP:10438"},{"database":"Rhea","id":"RHEA-COMP:10439"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"},{"database":"ChEBI","id":"CHEBI:74310"},{"database":"ChEBI","id":"CHEBI:78684"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22041902"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:42193"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22041902"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-heptadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (9Z,12Z)-heptadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42196"},{"database":"Rhea","id":"RHEA-COMP:10438"},{"database":"Rhea","id":"RHEA-COMP:10439"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"},{"database":"ChEBI","id":"CHEBI:74308"},{"database":"ChEBI","id":"CHEBI:78690"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22041902"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:42197"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22041902"}]}]},{"texts":[{"value":"Lipid metabolism; polyunsaturated fatty acid biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24811169"}],"value":"Homo- and heterodimer (PubMed:24811169). Interacts with FAD3 but not with FAD6 (PubMed:24811169). FAD2-FAD3 heterodimers can form a metabolic channel in which 18:1-PC is converted to 18:3-PC without releasing a free 18:2-PC intermediate (PubMed:24811169)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14690501"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7907506"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1730697"}],"value":"Microsome membrane","id":"SL-0165"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22279586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7907506"}],"value":"Expressed in shoots and roots (PubMed:22279586, PubMed:7907506). Expressed in leaves, stems, flowers and siliques (PubMed:22279586)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22279586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7907506"}],"value":"Up-regulated by osmotic stress (PubMed:22279586). Not regulated by cold stress (PubMed:7907506)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14690501"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7907506"}],"value":"The histidine box domains may contain the active site and/or be involved in metal ion binding (Probable). The C-terminal sequence (-YNNKL) is necessary and sufficient for maintaining localization in the endoplasmic reticulum (PubMed:14690501)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11104757"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17507388"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22279586"}],"value":"Enhancement of both microviscosity and lipid/protein ratio of mitochondrial membranes, which in turn were responsible for the change in lateral mobility of lipids and for bioenergetic parameter modifications (PubMed:11104757). Increased membrane rigidity and cold sensitivity (PubMed:17507388). Hypersensitivity to salt or osmotic stress (PubMed:22279586)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11864983"}],"value":"Introduction of Ile at position 146 or 324 has a dominant role in specifying hydroxylation activity"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the fatty acid desaturase type 1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Delta(12)-fatty-acid desaturase","featureId":"PRO_0000185418"},{"type":"Transmembrane","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"Histidine box-1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Motif","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Histidine box-2","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Motif","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"Histidine box-3","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Compositional bias","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Mutagenesis","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"In m7FAD2/L7M; Converted from a desaturase to a bifunctional desaturase/hydroxylase; when associated with G-104; N-148; F-217; V-295; A-322 and I-324.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9812895"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["V"]}},{"type":"Mutagenesis","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Produces less than 1% hydroxy fatty acid. In m7FAD2/L7M; Converted from a desaturase to a bifunctional desaturase/hydroxylase; when associated with V-63; N-148; F-217; V-295; A-322 and I-324. In C4M; Converted from a desaturase to a bifunctional desaturase/hydroxylase with a high hydroxylase activity; when associated with I-148; A-322 and V-324.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11864983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9812895"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["G"]}},{"type":"Mutagenesis","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Increased monounsaturated and decreased polyunsaturated fatty acid levels.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22279586"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["T"]}},{"type":"Mutagenesis","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Produces up to 4.2% hydroxy fatty acid. 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In C4M; Converted from a desaturase to a bifunctional desaturase/hydroxylase with a high hydroxylase activity; when associated with G-104; I-148 and V-324.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11864983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9812895"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"Produces up to 5.4% hydroxy fatty acid. In m7FAD2/L7M; Converted from a desaturase to a bifunctional desaturase/hydroxylase; when associated with V-63; G-104; N-148; F-217; V-295 and A-322. 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