ADSL3_ARATH
ID ADSL3_ARATH Reviewed; 299 AA.
AC Q9FPD5; Q9LND6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Delta-9 desaturase-like 3 protein;
DE EC=1.14.19.-;
GN OrderedLocusNames=At1g06120; ORFNames=T21E18.17, T21E18_14;
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=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 [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].
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).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF80135.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC024174; AAF80135.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27941.1; -; Genomic_DNA.
DR EMBL; AF332434; AAG48797.1; -; mRNA.
DR EMBL; AK117555; BAC42216.1; -; mRNA.
DR PIR; E86196; E86196.
DR RefSeq; NP_172102.1; NM_100493.3.
DR AlphaFoldDB; Q9FPD5; -.
DR SMR; Q9FPD5; -.
DR STRING; 3702.AT1G06120.1; -.
DR PaxDb; Q9FPD5; -.
DR PRIDE; Q9FPD5; -.
DR EnsemblPlants; AT1G06120.1; AT1G06120.1; AT1G06120.
DR GeneID; 837121; -.
DR Gramene; AT1G06120.1; AT1G06120.1; AT1G06120.
DR KEGG; ath:AT1G06120; -.
DR Araport; AT1G06120; -.
DR TAIR; locus:2198836; AT1G06120.
DR eggNOG; KOG1600; Eukaryota.
DR HOGENOM; CLU_027359_1_0_1; -.
DR InParanoid; Q9FPD5; -.
DR OMA; WHISFAR; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; Q9FPD5; -.
DR BioCyc; ARA:AT1G06120-MON; -.
DR UniPathway; UPA00658; -.
DR PRO; PR:Q9FPD5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FPD5; baseline and differential.
DR Genevisible; Q9FPD5; AT.
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 Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..299
FT /note="Delta-9 desaturase-like 3 protein"
FT /id="PRO_0000185429"
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 77..82
FT /note="Histidine box-1"
FT MOTIF 114..118
FT /note="Histidine box-2"
FT MOTIF 246..250
FT /note="Histidine box-3"
SQ SEQUENCE 299 AA; 35178 MW; 8A516A666CB164FB CRC64;
MGDKNKDDSS SQSKAVRKEK RAFLFRKWTR VDVMRVSAVG AVHLLCLLAP FNYTWEAFRF
AAMVGISTNL SITFSYHRNL THRSFKLPKW LEYPFAYSAL FALQGHPIDW VSTHRFHHQF
TDSDRDPHSP IEGFWFSHVF WIFDTSYIRE KCGGRDNVMD LKQQWFYRFL QNTIGLHILT
FWILVYLWGG LPYLTWSVGV GGAIGYHATW LINSACHIWG SRAWNTKDTS RNIWWLGPFT
MGESWHNNHH AFEASARHGL EWYQVDLTWY LIWFFQVLGL ATDVKLPTDA QKRKMSLAR
