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Database: UniProt
Entry: ADSL2_ARATH
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Original site: ADSL2_ARATH 
ID   ADSL2_ARATH             Reviewed;         299 AA.
AC   Q9LND8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Delta-9 desaturase-like 2 protein;
DE            EC=1.14.19.-;
GN   OrderedLocusNames=At1g06100; ORFNames=T21E18.15, T21E18_12;
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;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AC024174; AAF80133.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27939.1; -; Genomic_DNA.
DR   EMBL; BT014933; AAT47784.1; -; mRNA.
DR   EMBL; BT015835; AAU94398.1; -; mRNA.
DR   PIR; C86196; C86196.
DR   RefSeq; NP_172100.1; NM_100491.2.
DR   AlphaFoldDB; Q9LND8; -.
DR   SMR; Q9LND8; -.
DR   STRING; 3702.Q9LND8; -.
DR   PaxDb; 3702-AT1G06100-1; -.
DR   ProteomicsDB; 244840; -.
DR   EnsemblPlants; AT1G06100.1; AT1G06100.1; AT1G06100.
DR   GeneID; 837119; -.
DR   Gramene; AT1G06100.1; AT1G06100.1; AT1G06100.
DR   KEGG; ath:AT1G06100; -.
DR   Araport; AT1G06100; -.
DR   TAIR; AT1G06100; -.
DR   eggNOG; KOG1600; Eukaryota.
DR   HOGENOM; CLU_027359_1_0_1; -.
DR   InParanoid; Q9LND8; -.
DR   OMA; IREKCGR; -.
DR   OrthoDB; 5487114at2759; -.
DR   PhylomeDB; Q9LND8; -.
DR   BioCyc; ARA:AT1G06100-MONOMER; -.
DR   UniPathway; UPA00658; -.
DR   PRO; PR:Q9LND8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LND8; baseline and differential.
DR   Genevisible; Q9LND8; AT.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; ACYL-COA DESATURASE; 1.
DR   PANTHER; PTHR11351:SF71; DELTA-9 DESATURASE-LIKE 1 PROTEIN-RELATED; 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 2 protein"
FT                   /id="PRO_0000185428"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
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;  35356 MW;  9FCDBA8CF21D6507 CRC64;
     MSETTKDDGS SQKKSVRKEK RAYVLRKWTQ FDVGRASTVG TVHLLCLLAP FNYKWEAFRF
     GIILAILTNL CITFSYHRNL THRSFKLPKW LEYPFAYSAL LALQGDPLDW VSIHRFHHQF
     TDSDRDPHSP IEGFWFSHVL WIFDTDYIRE KCGRRNNVMD LKQQWFYRFL KKTLVLHILA
     FWTLIYLWGG LPYLTWTVGF GGVIGYHGTW LVNSACHICG SQAWQTNDTS RNVWWLALLT
     MGESWHNNHH AFETSARHGL EWYQLDITWY LIWFFQALGL ATNVKLPTDA QKRKMAIRR
//
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