ADS32_ARATH
ID ADS32_ARATH Reviewed; 361 AA.
AC Q9LVZ3; Q5IGR4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable lipid desaturase ADS3.2, chloroplastic {ECO:0000303|PubMed:15579662};
DE EC=1.14.19.- {ECO:0000305};
DE Flags: Precursor;
GN Name=ADS3.2 {ECO:0000303|PubMed:15579662};
GN OrderedLocusNames=At3g15870 {ECO:0000312|Araport:AT3G15870};
GN ORFNames=MSJ11.26 {ECO:0000312|EMBL:BAB02317.1};
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 [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=15579662; DOI=10.1104/pp.104.052951;
RA Heilmann I., Mekhedov S., King B., Browse J., Shanklin J.;
RT "Identification of the Arabidopsis palmitoyl-monogalactosyldiacylglycerol
RT Delta7-desaturase gene FAD5, and effects of plastidial retargeting of
RT Arabidopsis desaturases on the fad5 mutant phenotype.";
RL Plant Physiol. 136:4237-4245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and wild-type levels of both
CC Hexadeca 7,10,13-trienoic acid (16:3(7Z,10Z,13Z)) and leaf chlorophyll
CC content. {ECO:0000269|PubMed:15579662}.
CC -!- MISCELLANEOUS: ADS3.2 does not contribute to the FAD5 phenotype.
CC {ECO:0000269|PubMed:15579662}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW51921.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB02317.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY734685; AAW51921.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB017071; BAB02317.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75739.1; -; Genomic_DNA.
DR RefSeq; NP_188208.4; NM_112457.6.
DR AlphaFoldDB; Q9LVZ3; -.
DR SMR; Q9LVZ3; -.
DR STRING; 3702.AT3G15870.1; -.
DR PaxDb; Q9LVZ3; -.
DR PRIDE; Q9LVZ3; -.
DR EnsemblPlants; AT3G15870.1; AT3G15870.1; AT3G15870.
DR GeneID; 820830; -.
DR Gramene; AT3G15870.1; AT3G15870.1; AT3G15870.
DR KEGG; ath:AT3G15870; -.
DR Araport; AT3G15870; -.
DR TAIR; locus:2093207; AT3G15870.
DR eggNOG; KOG1600; Eukaryota.
DR HOGENOM; CLU_027359_1_0_1; -.
DR InParanoid; Q9LVZ3; -.
DR OMA; IRVHRTH; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; Q9LVZ3; -.
DR BioCyc; ARA:AT3G15870-MON; -.
DR UniPathway; UPA00658; -.
DR PRO; PR:Q9LVZ3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVZ3; baseline and differential.
DR Genevisible; Q9LVZ3; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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: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 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 2: Evidence at transcript level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..361
FT /note="Probable lipid desaturase ADS3.2, chloroplastic"
FT /id="PRO_0000007145"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 140..145
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 177..181
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 309..313
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 42343 MW; 712139C6A2C9ADF3 CRC64;
MMSLSTTLKP LSHFSPFVKR HNPKTNNTLF TLDTHNFTNS FWSKRGGSVS HRKHTVVAVY
EAPDHVESSW RRLLSEVVVV RTKRSFWERS WTSWDVSKLV IFVGTHLLSL LAPFYFSWEA
FWVFPWLVFI NGICITLSYH RNLSHRSFDL PKWLEYLFAY GGVLAFQGDP IEWVSNHRYH
HKHCETQRDP HSPTQGFWFS HMAWIFDTSS ILENCGGEEN VDDLVRQPFY RFLQRTVLLH
MMAYSFLFYF CGGMPLLVWG IGITIAVRLH LTFLVNSVCH IWGTRAWNTS DFSKNNWWVA
ILTLGEGWHN NHHAFEFSAR HGLEWWQLDI TWCLIRFLEA IGLATNVKLP TETQMKGKAL
V
