FAD6C_ARATH
ID FAD6C_ARATH Reviewed; 448 AA.
AC P46312; Q9M094;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Omega-6 fatty acid desaturase, chloroplastic {ECO:0000303|PubMed:7846158};
DE EC=1.14.19.23 {ECO:0000269|PubMed:7846158};
DE Flags: Precursor;
GN Name=FAD6 {ECO:0000303|PubMed:7846158};
GN Synonyms=FADC {ECO:0000303|PubMed:7846158};
GN OrderedLocusNames=At4g30950 {ECO:0000312|Araport:AT4G30950};
GN ORFNames=F6I18.140 {ECO:0000312|EMBL:CAA18198.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-418, FUNCTION, CATALYTIC ACTIVITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=7846158; DOI=10.1104/pp.106.4.1453;
RA Falcone D.L., Gibson S., Lemieux B., Somerville C.R.;
RT "Identification of a gene that complements an Arabidopsis mutant deficient
RT in chloroplast omega 6 desaturase activity.";
RL Plant Physiol. 106:1453-1459(1994).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [7]
RP MUTAGENESIS OF PRO-225.
RX PubMed=20410050; DOI=10.1093/pcp/pcq053;
RA Xu C., Moellering E.R., Muthan B., Fan J., Benning C.;
RT "Lipid transport mediated by Arabidopsis TGD proteins is unidirectional
RT from the endoplasmic reticulum to the plastid.";
RL Plant Cell Physiol. 51:1019-1028(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-70, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-69, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Chloroplast omega-6 fatty acid desaturase introduces the
CC second double bond in the biosynthesis of 16:3 and 18:3 fatty acids,
CC important constituents of plant membranes. It is thought to use
CC ferredoxin as an electron donor and to act on fatty acids esterified to
CC galactolipids, sulfolipids and phosphatidylglycerol.
CC {ECO:0000269|PubMed:7846158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z)-octadecenoyl-containing glycerolipid + 2 H(+) + O2 + 2
CC reduced [2Fe-2S]-[ferredoxin] = a (9Z,12Z)-octadecadienoyl-containing
CC glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:46376, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:88240,
CC ChEBI:CHEBI:88351; EC=1.14.19.23;
CC Evidence={ECO:0000269|PubMed:7846158};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:12766230}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Highest levels found in expanding leaves.
CC {ECO:0000269|PubMed:7846158}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AL022198; CAA18198.1; -; Genomic_DNA.
DR EMBL; AL161578; CAB79813.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85834.1; -; Genomic_DNA.
DR EMBL; AY045621; AAK73979.1; -; mRNA.
DR EMBL; AY058078; AAL24186.1; -; mRNA.
DR EMBL; AY079039; AAL79589.1; -; mRNA.
DR EMBL; AY058852; AAL24240.1; -; mRNA.
DR EMBL; AY088002; AAM65548.1; -; mRNA.
DR EMBL; U09503; AAA92800.1; -; mRNA.
DR PIR; D85362; D85362.
DR RefSeq; NP_194824.1; NM_119243.4.
DR AlphaFoldDB; P46312; -.
DR BioGRID; 14507; 4.
DR IntAct; P46312; 1.
DR STRING; 3702.AT4G30950.1; -.
DR iPTMnet; P46312; -.
DR PaxDb; P46312; -.
DR PRIDE; P46312; -.
DR ProteomicsDB; 222374; -.
DR EnsemblPlants; AT4G30950.1; AT4G30950.1; AT4G30950.
DR GeneID; 829220; -.
DR Gramene; AT4G30950.1; AT4G30950.1; AT4G30950.
DR KEGG; ath:AT4G30950; -.
DR Araport; AT4G30950; -.
DR TAIR; locus:2126734; AT4G30950.
DR eggNOG; ENOG502QQPI; Eukaryota.
DR HOGENOM; CLU_033094_3_0_1; -.
DR InParanoid; P46312; -.
DR OMA; CGHRSFA; -.
DR OrthoDB; 577374at2759; -.
DR PhylomeDB; P46312; -.
DR BioCyc; MetaCyc:AT4G30950-MON; -.
DR BRENDA; 1.14.19.23; 399.
DR UniPathway; UPA00658; -.
DR PRO; PR:P46312; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P46312; baseline and differential.
DR Genevisible; P46312; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0102873; F:1-18:1-2-16:0-digalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102834; F:1-18:1-2-16:0-monogalactosyldiacylglycerol acyl-lipid omega-6 desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102850; F:1-18:1-2-16:0-phosphatidylglycerol omega-6 desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102836; F:1-18:1-2-16:1-monogalactosyldiacylglyceroldesaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102838; F:1-18:1-2-16:2-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102841; F:1-18:1-2-16:2-monogalactosyldiacylglycerol synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102655; F:1-18:1-2-trans-16:1-phosphatidylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102844; F:1-18:2-2-16:1-monogalactosyldiacylglycerol desaturase activity (SN2-16:2 forming); IEA:UniProtKB-EC.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; TAS:TAIR.
DR GO; GO:0010205; P:photoinhibition; IMP:TAIR.
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 1: Evidence at protein level;
KW Acetylation; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase; Plastid;
KW Plastid inner membrane; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 70..448
FT /note="Omega-6 fatty acid desaturase, chloroplastic"
FT /id="PRO_0000007123"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 171..175
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 207..211
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 367..371
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT MOD_RES 70
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 225
FT /note="P->S: In fad6-2; loss of function, but no visible
FT phenotype under normal growth conditions."
FT /evidence="ECO:0000269|PubMed:20410050"
SQ SEQUENCE 448 AA; 51226 MW; C3AC72FB28FBF287 CRC64;
MASRIADSLF AFTGPQQCLP RVPKLAASSA RVSPGVYAVK PIDLLLKGRT HRSRRCVAPV
KRRIGCIKAV AAPVAPPSAD SAEDREQLAE SYGFRQIGED LPENVTLKDI MDTLPKEVFE
IDDLKALKSV LISVTSYTLG LFMIAKSPWY LLPLAWAWTG TAITGFFVIG HDCAHKSFSK
NKLVEDIVGT LAFLPLVYPY EPWRFKHDRH HAKTNMLVHD TAWQPVPPEE FESSPVMRKA
IIFGYGPIRP WLSIAHWVNW HFNLKKFRAS EVNRVKISLA CVFAFMAVGW PLIVYKVGIL
GWVKFWLMPW LGYHFWMSTF TMVHHTAPHI PFKPADEWNA AQAQLNGTVH CDYPSWIEIL
CHDINVHIPH HISPRIPSYN LRAAHESIQE NWGKYTNLAT WNWRLMKTIM TVCHVYDKEE
NYIPFDRLAP EESQPITFLK KAMPNYTA
