FAD3C_ARATH
ID FAD3C_ARATH Reviewed; 446 AA.
AC P46310;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=sn-2 acyl-lipid omega-3 desaturase (ferredoxin), chloroplastic {ECO:0000303|PubMed:8226956};
DE EC=1.14.19.35 {ECO:0000269|PubMed:8226956};
DE AltName: Full=Omega-3 fatty acid desaturase 7, chloroplastic {ECO:0000303|PubMed:8226956};
DE Flags: Precursor;
GN Name=FAD7 {ECO:0000303|PubMed:8226956};
GN Synonyms=FADD {ECO:0000303|PubMed:8029334};
GN OrderedLocusNames=At3g11170 {ECO:0000312|Araport:AT3G11170};
GN ORFNames=F11B9.10 {ECO:0000312|EMBL:AAG50977.1},
GN F9F8.4 {ECO:0000312|EMBL:AAF01508.1};
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].
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RX PubMed=8029334; DOI=10.1104/pp.103.2.467;
RA Yadav N.S., Wierzbicki A., Aegerter M., Caster C.S., Perez-Grau L.,
RA Kinney A.J., Hitz W.D., Booth J.R. Jr., Schweiger B., Stecca K.L.,
RA Allen S.M., Blackwell M., Reiter R.S., Carlson T.J., Russell S.H.,
RA Feldmann K.A., Pierce J., Browse J.;
RT "Cloning of higher plant omega-3 fatty acid desaturases.";
RL Plant Physiol. 103:467-476(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Aerial part;
RX PubMed=8226956; DOI=10.1016/s0021-9258(20)80498-0;
RA Iba K., Gibson S., Nishiuchi T., Fuse T., Nishimura M., Arondel V.,
RA Hugly S., Somerville C.R.;
RT "A gene encoding a chloroplast omega-3 fatty acid desaturase complements
RT alterations in fatty acid desaturation and chloroplast copy number of the
RT fad7 mutant of Arabidopsis thaliana.";
RL J. Biol. Chem. 268:24099-24105(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RA Watahiki M., Yamamoto K.;
RT "cDNA cloning of fatty acid desaturase from Arabidopsis thaliana.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [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).
CC -!- FUNCTION: Chloroplast omega-3 fatty acid desaturase introduces the
CC third 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:8226956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (7Z,10Z)-hexadecadienoyl-containing glycerolipid + 2 H(+) +
CC O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a (7Z,10Z,13Z)-
CC hexadecatrienoyl-containing glycerolipid + 2 H2O + 2 oxidized [2Fe-
CC 2S]-[ferredoxin]; Xref=Rhea:RHEA:46412, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:88268, ChEBI:CHEBI:88269; EC=1.14.19.35;
CC Evidence={ECO:0000269|PubMed:8226956};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 H(+) +
CC O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z,12Z,15Z)-octadecatrienoyl-
CC containing glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:46408, 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:88351,
CC ChEBI:CHEBI:90078; EC=1.14.19.35;
CC Evidence={ECO:0000269|PubMed:8226956};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:8226956}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:12766230}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12766230}.
CC -!- TISSUE SPECIFICITY: Most abundant in leaves and seedlings.
CC {ECO:0000269|PubMed:8226956}.
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; L22961; AAA61773.1; -; mRNA.
DR EMBL; D14007; BAA03106.1; -; Genomic_DNA.
DR EMBL; D26019; BAA05040.1; -; mRNA.
DR EMBL; AC009991; AAF01508.1; -; Genomic_DNA.
DR EMBL; AC073395; AAG50977.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75009.1; -; Genomic_DNA.
DR PIR; JQ2336; JQ2336.
DR RefSeq; NP_187727.1; NM_111953.3.
DR AlphaFoldDB; P46310; -.
DR BioGRID; 5622; 2.
DR STRING; 3702.AT3G11170.1; -.
DR PaxDb; P46310; -.
DR PRIDE; P46310; -.
DR ProteomicsDB; 230845; -.
DR EnsemblPlants; AT3G11170.1; AT3G11170.1; AT3G11170.
DR GeneID; 820288; -.
DR Gramene; AT3G11170.1; AT3G11170.1; AT3G11170.
DR KEGG; ath:AT3G11170; -.
DR Araport; AT3G11170; -.
DR TAIR; locus:2074628; AT3G11170.
DR eggNOG; ENOG502QQQ2; Eukaryota.
DR HOGENOM; CLU_033094_1_0_1; -.
DR InParanoid; P46310; -.
DR OMA; KNDHYVS; -.
DR OrthoDB; 577374at2759; -.
DR PhylomeDB; P46310; -.
DR BioCyc; ARA:AT3G11170-MON; -.
DR BioCyc; MetaCyc:AT3G11170-MON; -.
DR BRENDA; 1.14.19.35; 399.
DR UniPathway; UPA00658; -.
DR PRO; PR:P46310; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P46310; baseline and differential.
DR Genevisible; P46310; 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:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042170; C:plastid membrane; TAS:TAIR.
DR GO; GO:0102874; F:1-16:0-2-18:2-digalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102842; F:1-18:1-2-16:2-monogalactosyldiacylglycerol desaturase activity (SN2-16:3 forming); IEA:UniProtKB-EC.
DR GO; GO:0102835; F:1-18:2-2-16:0-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102837; F:1-18:2-2-16:1-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102839; F:1-18:2-2-16:2-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102840; F:1-18:2-2-16:3-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102848; F:1-18:2-2-18:2-digalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102875; F:1-18:2-2-18:2-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102849; F:1-18:2-2-18:3-digalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102993; F:linolenate delta15 desaturase activity; IEA:RHEA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
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 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..65
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 66..446
FT /note="sn-2 acyl-lipid omega-3 desaturase (ferredoxin),
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007117"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 163..167
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 199..203
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 366..370
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 51174 MW; 121125F634553D35 CRC64;
MANLVLSECG IRPLPRIYTT PRSNFLSNNN KFRPSLSSSS YKTSSSPLSF GLNSRDGFTR
NWALNVSTPL TTPIFEESPL EEDNKQRFDP GAPPPFNLAD IRAAIPKHCW VKNPWKSLSY
VVRDVAIVFA LAAGAAYLNN WIVWPLYWLA QGTMFWALFV LGHDCGHGSF SNDPKLNSVV
GHLLHSSILV PYHGWRISHR THHQNHGHVE NDESWHPMSE KIYNTLDKPT RFFRFTLPLV
MLAYPFYLWA RSPGKKGSHY HPDSDLFLPK ERKDVLTSTA CWTAMAALLV CLNFTIGPIQ
MLKLYGIPYW INVMWLDFVT YLHHHGHEDK LPWYRGKEWS YLRGGLTTLD RDYGLINNIH
HDIGTHVIHH LFPQIPHYHL VEATEAAKPV LGKYYREPDK SGPLPLHLLE ILAKSIKEDH
YVSDEGEVVY YKADPNLYGE VKVRAD
