ADS1_ARATH
ID ADS1_ARATH Reviewed; 305 AA.
AC O65797; Q8GW15;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Delta-9 acyl-lipid desaturase 1 {ECO:0000303|PubMed:9559566};
DE EC=1.14.19.- {ECO:0000269|PubMed:15240892};
GN Name=ADS1 {ECO:0000303|PubMed:9559566};
GN OrderedLocusNames=At1g06080 {ECO:0000312|Araport:AT1G06080};
GN ORFNames=T21E18.13 {ECO:0000312|EMBL:AAF80131.1};
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, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9559566; DOI=10.1093/oxfordjournals.pcp.a029364;
RA Fukuchi-Mizutani M., Tasaka Y., Tanaka Y., Ashikari T., Kusumi T.,
RA Murata N.;
RT "Characterization of delta 9 acyl-lipid desaturase homologues from
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 39:247-253(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 FUNCTION.
RX PubMed=17156034; DOI=10.1046/j.1467-7652.2003.00021.x;
RA Yao K., Bacchetto R.G., Lockhart K.M., Friesen L.J., Potts D.A.,
RA Covello P.S., Taylor D.C.;
RT "Expression of the Arabidopsis ADS1 gene in Brassica juncea results in a
RT decreased level of total saturated fatty acids.";
RL Plant Biotechnol. J. 1:221-229(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SPECIFICITY.
RX PubMed=15240892; DOI=10.1073/pnas.0402200101;
RA Heilmann I., Pidkowich M.S., Girke T., Shanklin J.;
RT "Switching desaturase enzyme specificity by alternate subcellular
RT targeting.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10266-10271(2004).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23175755; DOI=10.1104/pp.112.202325;
RA Smith M.A., Dauk M., Ramadan H., Yang H., Seamons L.E., Haslam R.P.,
RA Beaudoin F., Ramirez-Erosa I., Forseille L.;
RT "Involvement of Arabidopsis ACYL-COENZYME A DESATURASE-LIKE2 (At2g31360) in
RT the biosynthesis of the very-long-chain monounsaturated fatty acid
RT components of membrane lipids.";
RL Plant Physiol. 161:81-96(2013).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27062193; DOI=10.1111/ppl.12448;
RA Chen M., Thelen J.J.;
RT "Acyl-lipid desaturase 1 primes cold acclimation response in Arabidopsis.";
RL Physiol. Plantarum 158:11-22(2016).
CC -!- FUNCTION: Involved in delta-9 desaturation of fatty acids (Probable)
CC (PubMed:17156034, PubMed:15240892). Involved in the production of very-
CC long-chain fatty acids (VLCFAs) (PubMed:23175755). May desaturate
CC chloroplastic monogalactosyl diacylglycerol (MGDG) and alter
CC chloroplast membrane fluidity, which is required to prime a cold
CC acclimation response (PubMed:27062193). {ECO:0000269|PubMed:15240892,
CC ECO:0000269|PubMed:17156034, ECO:0000269|PubMed:23175755,
CC ECO:0000269|PubMed:27062193, ECO:0000305|PubMed:9559566}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23175755}; Multi-pass membrane protein
CC {ECO:0000255}. Plastid, chloroplast membrane
CC {ECO:0000305|PubMed:27062193}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in inflorescence meristems,
CC leaves, and flowers, and weakly in roots and seedpods.
CC {ECO:0000269|PubMed:9559566}.
CC -!- INDUCTION: Down-regulated by cold. {ECO:0000269|PubMed:9559566}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250|UniProtKB:O00767}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants display enhanced freezing tolerance upon
CC cold acclimation. {ECO:0000269|PubMed:27062193}.
CC -!- MISCELLANEOUS: Substrate specificity shifts from delta-9 to delta-7
CC desaturation when the protein is retargeted to the chloroplast.
CC {ECO:0000269|PubMed:15240892}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; D88536; BAA25180.1; -; mRNA.
DR EMBL; AC024174; AAF80131.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27937.1; -; Genomic_DNA.
DR EMBL; AK119146; BAC43716.1; -; mRNA.
DR EMBL; AF332433; AAG48796.1; -; mRNA.
DR PIR; T52111; T52111.
DR RefSeq; NP_172098.1; NM_100489.4.
DR AlphaFoldDB; O65797; -.
DR SMR; O65797; -.
DR STRING; 3702.AT1G06080.1; -.
DR PaxDb; O65797; -.
DR PRIDE; O65797; -.
DR ProteomicsDB; 244737; -.
DR EnsemblPlants; AT1G06080.1; AT1G06080.1; AT1G06080.
DR GeneID; 837117; -.
DR Gramene; AT1G06080.1; AT1G06080.1; AT1G06080.
DR KEGG; ath:AT1G06080; -.
DR Araport; AT1G06080; -.
DR TAIR; locus:2198786; AT1G06080.
DR eggNOG; KOG1600; Eukaryota.
DR HOGENOM; CLU_027359_1_0_1; -.
DR InParanoid; O65797; -.
DR OMA; WVLHMTW; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; O65797; -.
DR BioCyc; ARA:AT1G06080-MON; -.
DR UniPathway; UPA00658; -.
DR PRO; PR:O65797; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O65797; baseline and differential.
DR Genevisible; O65797; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009979; F:16:0 monogalactosyldiacylglycerol desaturase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; 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 GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:TAIR.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
PE 1: Evidence at protein level;
KW Chloroplast; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="Delta-9 acyl-lipid desaturase 1"
FT /id="PRO_0000185425"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 83..88
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 120..124
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 252..256
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 252
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 255
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT CONFLICT 154
FT /note="L -> R (in Ref. 4; BAC43716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 36107 MW; 0BDABE2162AFC2D0 CRC64;
MSLSASEKEE NNKKMAADKA EMGRKKRAMW ERKWKRLDIV KAFASLFVHF LCLLAPFNFT
WPALRVALIV YTVGGLGITV SYHRNLAHRS FKVPKWLEYF FAYCGLLAIQ GDPIDWVSTH
RYHHQFTDSD RDPHSPNEGF WFSHLLWLFD TGYLVEKCGR RTNVEDLKRQ WYYKFLQRTV
LYHILTFGFL LYYFGGLSFL TWGMGIGVAM EHHVTCLINS LCHVWGSRTW KTNDTSRNVW
WLSVFSFGES WHNNHHAFES SARQGLEWWQ IDISWYIVRF LEIIGLATDV KLPSESQRRR
MAMVR
