STAD7_ARATH
ID STAD7_ARATH Reviewed; 401 AA.
AC O22832; Q0WKW6; Q42591; Q94AE9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 7, chloroplastic;
DE Short=Stearoyl-ACP desaturase 7;
DE EC=1.14.19.2 {ECO:0000250|UniProtKB:P22337};
DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase 7;
DE AltName: Full=Protein FATTY ACID BIOSYNTHESIS 2;
DE AltName: Full=Protein SUPPRESSOR OF SA INSENSITIVITY 2;
DE Short=AtSSI2;
DE Flags: Precursor;
GN Name=FAB2; Synonyms=SSI2; OrderedLocusNames=At2g43710; ORFNames=F18O19.18;
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], MUTAGENESIS OF LEU-146, FUNCTION, AND INDUCTION
RP BY JA.
RC STRAIN=cv. Columbia;
RX PubMed=11481500; DOI=10.1073/pnas.151258398;
RA Kachroo P., Shanklin J., Shah J., Whittle E.J., Klessig D.F.;
RT "A fatty acid desaturase modulates the activation of defense signaling
RT pathways in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9448-9453(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RA Piffanelli P., Murphy D.J.;
RT "Cloning of a stearoyl-ACP desaturase from Arabidopis thaliana.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-401.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DISRUPTION PHENOTYPE, AND FAB2 MUTANT.
RX PubMed=12232421; DOI=10.1104/pp.106.4.1443;
RA Lightner J., Wu J., Browse J.;
RT "A mutant of Arabidopsis with increased levels of stearic acid.";
RL Plant Physiol. 106:1443-1451(1994).
RN [8]
RP SSI2 MUTANT, AND FUNCTION.
RX PubMed=11309146; DOI=10.1046/j.1365-313x.2001.00992.x;
RA Shah J., Kachroo P., Nandi A., Klessig D.F.;
RT "A recessive mutation in the Arabidopsis SSI2 gene confers SA- and NPR1-
RT independent expression of PR genes and resistance against bacterial and
RT oomycete pathogens.";
RL Plant J. 25:563-574(2001).
RN [9]
RP FUNCTION.
RX PubMed=14601670; DOI=10.1094/mpmi.2003.16.11.1022;
RA Kachroo P., Kachroo A., Lapchyk L., Hildebrand D., Klessig D.F.;
RT "Restoration of defective cross talk in ssi2 mutants: role of salicylic
RT acid, jasmonic acid, and fatty acids in SSI2-mediated signaling.";
RL Mol. Plant Microbe Interact. 16:1022-1029(2003).
RN [10]
RP FUNCTION.
RX PubMed=14615603; DOI=10.1105/tpc.017301;
RA Kachroo A., Lapchyk L., Fukushige H., Hildebrand D., Klessig D.,
RA Kachroo P.;
RT "Plastidial fatty acid signaling modulates salicylic acid- and jasmonic
RT acid-mediated defense pathways in the Arabidopsis ssi2 mutant.";
RL Plant Cell 15:2952-2965(2003).
RN [11]
RP FUNCTION.
RX PubMed=15195945; DOI=10.1094/mpmi.2004.17.6.623;
RA Sekine K.T., Nandi A., Ishihara T., Hase S., Ikegami M., Shah J.,
RA Takahashi H.;
RT "Enhanced resistance to Cucumber mosaic virus in the Arabidopsis thaliana
RT ssi2 mutant is mediated via an SA-independent mechanism.";
RL Mol. Plant Microbe Interact. 17:623-632(2004).
RN [12]
RP FUNCTION.
RX PubMed=15828688; DOI=10.1094/mpmi-18-0363;
RA Nandi A., Moeder W., Kachroo P., Klessig D.F., Shah J.;
RT "Arabidopsis ssi2-conferred susceptibility to Botrytis cinerea is dependent
RT on EDS5 and PAD4.";
RL Mol. Plant Microbe Interact. 18:363-370(2005).
RN [13]
RP GENE FAMILY, AND TISSUE SPECIFICITY.
RX PubMed=17072561; DOI=10.1007/s11103-006-9086-y;
RA Kachroo A., Shanklin J., Whittle E., Lapchyk L., Hildebrand D., Kachroo P.;
RT "The Arabidopsis stearoyl-acyl carrier protein-desaturase family and the
RT contribution of leaf isoforms to oleic acid synthesis.";
RL Plant Mol. Biol. 63:257-271(2007).
RN [14]
RP INDUCTION.
RX PubMed=18689444; DOI=10.1104/pp.108.126342;
RA Mu J., Tan H., Zheng Q., Fu F., Liang Y., Zhang J., Yang X., Wang T.,
RA Chong K., Wang X.J., Zuo J.;
RT "LEAFY COTYLEDON1 is a key regulator of fatty acid biosynthesis in
RT Arabidopsis.";
RL Plant Physiol. 148:1042-1054(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-36, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LEU-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP MUTAGENESIS OF THR-219.
RC STRAIN=cv. Columbia;
RX PubMed=27681170; DOI=10.1105/tpc.16.00612;
RA Troncoso-Ponce M.A., Barthole G., Tremblais G., To A., Miquel M.,
RA Lepiniec L., Baud S.;
RT "Transcriptional activation of two palmitoyl-ACP delta9 desaturase genes by
RT MYB115 and MYB118 is critical for biosynthesis of omega-7 monounsaturated
RT fatty acid in the endosperm of Arabidopsis seeds.";
RL Plant Cell 28:2666-2682(2016).
CC -!- FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis
CC double bond between carbons 9 and 10 of the acyl chain. Required for
CC the activation of certain jasmonic acid (JA)-mediated responses and the
CC repression of the salicylic acid (SA) signaling pathway.
CC {ECO:0000269|PubMed:11309146, ECO:0000269|PubMed:11481500,
CC ECO:0000269|PubMed:14601670, ECO:0000269|PubMed:14615603,
CC ECO:0000269|PubMed:15195945, ECO:0000269|PubMed:15828688}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:11776, Rhea:RHEA-COMP:9656, Rhea:RHEA-
CC COMP:9924, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78495,
CC ChEBI:CHEBI:78783; EC=1.14.19.2;
CC Evidence={ECO:0000250|UniProtKB:P22337};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P22337};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P22337}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O22832-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:17072561}.
CC -!- INDUCTION: Positively regulated by LEC1. Up-regulated by jasmomic acid
CC (JA). {ECO:0000269|PubMed:11481500, ECO:0000269|PubMed:18689444}.
CC -!- DISRUPTION PHENOTYPE: Increased level of stearate (18:0) and reduced
CC level of oleic acid (18:1) in leaves. Spontaneous cell death,
CC constitutive PR genes expression, accumulation of high levels of
CC salicylic acid (SA), enhanced resistance to Pseudomonas syringae,
CC Peronospora parasitica and Cucumber mosaic virus, and enhanced
CC susceptibility to Botrytis cinerea. {ECO:0000269|PubMed:12232421}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63746.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF395441; AAK85232.1; -; mRNA.
DR EMBL; X93461; CAA63746.1; ALT_SEQ; mRNA.
DR EMBL; AC002333; AAB64035.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10311.1; -; Genomic_DNA.
DR EMBL; AY048233; AAK82496.1; -; mRNA.
DR EMBL; AY094014; AAM16170.1; -; mRNA.
DR EMBL; AK230443; BAF02241.1; -; mRNA.
DR PIR; E84869; E84869.
DR PIR; S71264; S71264.
DR RefSeq; NP_181899.1; NM_129933.4. [O22832-1]
DR AlphaFoldDB; O22832; -.
DR SMR; O22832; -.
DR BioGRID; 4309; 14.
DR IntAct; O22832; 6.
DR STRING; 3702.AT2G43710.1; -.
DR iPTMnet; O22832; -.
DR PaxDb; O22832; -.
DR PRIDE; O22832; -.
DR ProteomicsDB; 228392; -. [O22832-1]
DR EnsemblPlants; AT2G43710.1; AT2G43710.1; AT2G43710. [O22832-1]
DR GeneID; 818973; -.
DR Gramene; AT2G43710.1; AT2G43710.1; AT2G43710. [O22832-1]
DR KEGG; ath:AT2G43710; -.
DR Araport; AT2G43710; -.
DR eggNOG; ENOG502QRJK; Eukaryota.
DR HOGENOM; CLU_034505_1_0_1; -.
DR InParanoid; O22832; -.
DR OMA; NRHSMLH; -.
DR PhylomeDB; O22832; -.
DR BRENDA; 1.14.19.2; 399.
DR UniPathway; UPA00199; -.
DR PRO; PR:O22832; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22832; baseline and differential.
DR Genevisible; O22832; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102786; F:stearoyl-[acp] desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR CDD; cd01050; Acyl_ACP_Desat; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR005803; FADS-2_CS.
DR InterPro; IPR005067; Fatty_acid_desaturase-2.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR PANTHER; PTHR31155; PTHR31155; 1.
DR Pfam; PF03405; FA_desaturase_2; 1.
DR PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00574; FATTY_ACID_DESATUR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Fatty acid biosynthesis;
KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Plant defense; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 36..401
FT /note="Stearoyl-[acyl-carrier-protein] 9-desaturase 7,
FT chloroplastic"
FT /id="PRO_0000401425"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT MOD_RES 36
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 146
FT /note="L->F: In ssi2; reduced activity."
FT /evidence="ECO:0000269|PubMed:11481500"
FT MUTAGEN 219
FT /note="T->F: Sufficient to trigger a significant
FT accumulation of omega-7 fatty acids."
FT /evidence="ECO:0000269|PubMed:27681170"
FT CONFLICT 271
FT /note="E -> K (in Ref. 5; AAK82496/AAM16170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 45693 MW; 0C46984578D4E1D1 CRC64;
MALKFNPLVA SQPYKFPSST RPPTPSFRSP KFLCLASSSP ALSSGPKEVE SLKKPFTPPR
EVHVQVLHSM PPQKIEIFKS MENWAEENLL IHLKDVEKSW QPQDFLPDPA SDGFEDQVRE
LRERARELPD DYFVVLVGDM ITEEALPTYQ TMLNTLDGVR DETGASPTSW AIWTRAWTAE
ENRHGDLLNK YLYLSGRVDM RQIEKTIQYL IGSGMDPRTE NNPYLGFIYT SFQERATFIS
HGNTARQAKE HGDIKLAQIC GTIAADEKRH ETAYTKIVEK LFEIDPDGTV MAFADMMRKK
ISMPAHLMYD GRNDNLFDNF SSVAQRLGVY TAKDYADILE FLVGRWKIQD LTGLSGEGNK
AQDYLCGLAP RIKRLDERAQ ARAKKGPKIP FSWIHDREVQ L
