ADS2_ARATH
ID ADS2_ARATH Reviewed; 307 AA.
AC Q9SID2; O65798; Q8LD80;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Delta-9 acyl-lipid desaturase 2 {ECO:0000303|PubMed:9559566};
DE EC=1.14.19.75 {ECO:0000269|PubMed:23175755};
GN Name=ADS2 {ECO:0000303|PubMed:9559566};
GN OrderedLocusNames=At2g31360 {ECO:0000312|Araport:AT2G31360};
GN ORFNames=T28P16.15 {ECO:0000312|EMBL:AAD26482.2};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=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 [5]
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 [6]
RP FUNCTION, 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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, 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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23585650; DOI=10.1105/tpc.113.111179;
RA Chen M., Thelen J.J.;
RT "ACYL-LIPID DESATURASE2 is required for chilling and freezing tolerance in
RT Arabidopsis.";
RL Plant Cell 25:1430-1444(2013).
CC -!- FUNCTION: Involved in delta-9 desaturation of fatty acids (Probable)
CC (PubMed:15240892). Plays a role in the production of very-long-chain
CC monounsaturated fatty acids (VLCMUFAs) in seed lipids and in membrane
CC phospholipids and sphingolipids (PubMed:23175755). Acts as C-16:0
CC desaturase for monogalactosyl diacylglycerol (MGDG) and
CC phosphatidylglycerol (PG) (PubMed:23585650). Is an essential component
CC for cold adaptation (PubMed:23585650). Is essential to adjust the acyl
CC composition of organelle membrane lipid composition in response to cold
CC stress (PubMed:23585650). {ECO:0000269|PubMed:15240892,
CC ECO:0000269|PubMed:23175755, ECO:0000269|PubMed:23585650,
CC ECO:0000305|PubMed:9559566}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-hexacosanoyl-2-acyl-phosphoglycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a 1-[(17Z)-hexacos-17-enoyl]-2-acyl-
CC phosphoglycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:57600, 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:142019,
CC ChEBI:CHEBI:142020; EC=1.14.19.75;
CC Evidence={ECO:0000269|PubMed:23175755};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-tetracosanoyl-2-acyl-phosphoglycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a 1-[(15Z)-tetracos-15-enoyl]-2-acyl-
CC phosphoglycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:57604, 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:142021,
CC ChEBI:CHEBI:142022; EC=1.14.19.75;
CC Evidence={ECO:0000269|PubMed:23175755};
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}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in flowers, roots, leaves,
CC seedpods, and inflorescence meristems. {ECO:0000269|PubMed:9559566}.
CC -!- INDUCTION: Up-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 plant display a dwarf and sterile phenotype when
CC grown at 6 degrees Celsius and also show increased sensitivity to
CC freezing temperature. {ECO:0000269|PubMed:23585650}.
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; D88537; BAA25181.1; -; mRNA.
DR EMBL; AC007169; AAD26482.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08533.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61591.1; -; Genomic_DNA.
DR EMBL; AY045918; AAK76592.1; -; mRNA.
DR EMBL; AY079388; AAL85119.1; -; mRNA.
DR EMBL; AY086154; AAM63359.1; -; mRNA.
DR PIR; G84719; G84719.
DR PIR; T52109; T52109.
DR RefSeq; NP_001323798.1; NM_001336328.1.
DR RefSeq; NP_565721.1; NM_128693.5.
DR AlphaFoldDB; Q9SID2; -.
DR SMR; Q9SID2; -.
DR BioGRID; 3041; 35.
DR IntAct; Q9SID2; 34.
DR STRING; 3702.AT2G31360.1; -.
DR iPTMnet; Q9SID2; -.
DR PaxDb; Q9SID2; -.
DR PRIDE; Q9SID2; -.
DR ProteomicsDB; 244738; -.
DR EnsemblPlants; AT2G31360.1; AT2G31360.1; AT2G31360.
DR EnsemblPlants; AT2G31360.2; AT2G31360.2; AT2G31360.
DR GeneID; 817694; -.
DR Gramene; AT2G31360.1; AT2G31360.1; AT2G31360.
DR Gramene; AT2G31360.2; AT2G31360.2; AT2G31360.
DR KEGG; ath:AT2G31360; -.
DR Araport; AT2G31360; -.
DR TAIR; locus:2061260; AT2G31360.
DR eggNOG; KOG1600; Eukaryota.
DR HOGENOM; CLU_027359_1_0_1; -.
DR InParanoid; Q9SID2; -.
DR OMA; FWVTTHR; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; Q9SID2; -.
DR BioCyc; ARA:AT2G31360-MON; -.
DR BioCyc; MetaCyc:AT2G31360-MON; -.
DR BRENDA; 1.14.19.75; 399.
DR UniPathway; UPA00658; -.
DR PRO; PR:Q9SID2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SID2; baseline and differential.
DR Genevisible; Q9SID2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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:0010114; P:response to red light; IEP:UniProtKB.
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 Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..307
FT /note="Delta-9 acyl-lipid desaturase 2"
FT /id="PRO_0000185426"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 85..90
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 122..126
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 254..258
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT CONFLICT 23
FT /note="E -> EE (in Ref. 5; AAM63359)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="V -> L (in Ref. 5; AAM63359)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="E -> K (in Ref. 5; AAM63359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 36376 MW; 8E26FA0F2E9EEAEB CRC64;
MSVTSTVEEN HQKNPSTPAA VEEKKKRRWV FWDRRWRRLD YVKFSASFTV HSLALLAPFY
FTWSALWVTF LFYTIGGLGI TVSYHRNLAH RSFKVPKWLE YLLAYCALLA IQGDPIDWVS
THRYHHQFTD SERDPHSPKE GFWFSHLLWI YDSAYLVSKC GRRANVEDLK RQWFYRFLQK
TVLFHILGLG FFLFYLGGMS FVTWGMGVGA ALEVHVTCLI NSLCHIWGTR TWKTNDTSRN
VWWLSVFSFG ESWHNNHHAF ESSARQGLEW WQIDISWYIV RFFEIIGLAT DVKVPTEAQR
RRMAIVR
