STAD2_ARATH
ID STAD2_ARATH Reviewed; 411 AA.
AC Q9M881; F4IX66; Q67ZF5; Q6NQK5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 2, chloroplastic;
DE Short=Stearoyl-ACP desaturase 2;
DE EC=1.14.19.2 {ECO:0000269|PubMed:27681170};
DE AltName: Full=Acyl-[acyl-carrier-protein] desaturase 2;
DE Flags: Precursor;
GN Name=S-ACP-DES2; Synonyms=AAD2, SAD2; OrderedLocusNames=At3g02610;
GN ORFNames=F16B3.24;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY MYB115 AND MYB118,
RP DEVELOPMENTAL STAGE, SITE FOR SUBSTRATE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
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 (By similarity).
CC Exhibits delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD)
CC activity. Involved in omega-7 monounsaturated fatty acid biosynthesis,
CC especially in the endosperm oil (PubMed:27681170).
CC {ECO:0000250|UniProtKB:P22337, ECO:0000269|PubMed:27681170}.
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:0000269|PubMed:27681170};
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 {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in roots and flowers.
CC {ECO:0000269|PubMed:17072561}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in maturing endosperm.
CC {ECO:0000269|PubMed:27681170}.
CC -!- INDUCTION: Activated by MYB115 and MYB118 in the endosperm.
CC {ECO:0000269|PubMed:27681170}.
CC -!- DISRUPTION PHENOTYPE: Reduced omega-7 fatty acids accumulation in the
CC endosperm. The endosperm oil of double mutant aad2-3 aad3-3 lacks
CC omega-7 fatty acids. {ECO:0000269|PubMed:27681170}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD43925.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC021640; AAF32468.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73839.2; -; Genomic_DNA.
DR EMBL; BT010447; AAQ62867.1; -; mRNA.
DR EMBL; AK176162; BAD43925.1; ALT_INIT; mRNA.
DR RefSeq; NP_001319454.1; NM_001337426.1.
DR AlphaFoldDB; Q9M881; -.
DR SMR; Q9M881; -.
DR STRING; 3702.AT3G02610.1; -.
DR PaxDb; Q9M881; -.
DR PRIDE; Q9M881; -.
DR EnsemblPlants; AT3G02610.1; AT3G02610.1; AT3G02610.
DR GeneID; 820709; -.
DR Gramene; AT3G02610.1; AT3G02610.1; AT3G02610.
DR KEGG; ath:AT3G02610; -.
DR Araport; AT3G02610; -.
DR eggNOG; ENOG502QRJK; Eukaryota.
DR HOGENOM; CLU_034505_1_0_1; -.
DR InParanoid; Q9M881; -.
DR PhylomeDB; Q9M881; -.
DR BRENDA; 1.14.19.2; 399.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9M881; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M881; baseline and differential.
DR Genevisible; Q9M881; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IDA:UniProtKB.
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:0055089; P:fatty acid homeostasis; IMP:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:2000014; P:regulation of endosperm development; IMP:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:UniProtKB.
DR CDD; cd01050; Acyl_ACP_Desat; 1.
DR Gene3D; 1.10.620.20; -; 1.
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.
PE 1: Evidence at protein level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..411
FT /note="Stearoyl-[acyl-carrier-protein] 9-desaturase 2,
FT chloroplastic"
FT /id="PRO_0000401420"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT SITE 224
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000305|PubMed:27681170"
FT CONFLICT 6
FT /note="N -> S (in Ref. 4; BAD43925)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="P -> S (in Ref. 4; BAD43925 and 3; AAQ62867)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="S -> F (in Ref. 3; AAQ62867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46950 MW; 8C206A6CDB39DA00 CRC64;
MALLLNSTIT VAMKQNPLVA VSFPRTTCLG SSFSPPRLLR VSCVATNPSK TSEETDKKKF
RPIKEVPNQV THTITQEKLE IFKSMENWAQ ENLLSYLKPV EASWQPQDFL PETNDEDRFY
EQVKELRDRT KEIPDDYFVV LVGDMITEEA LPTYQTTLNT LDGVKDETGG SLTPWAVWVR
AWTAEENRHG DLLNKYLYLS GRVDMRHVEK TIQYLIGSGM DSKFENNPYN GFIYTSFQER
ATFISHGNTA KLATTYGDTT LAKICGTIAA DEKRHETAYT RIVEKLFEID PDGTVQALAS
MMRKRITMPA HLMHDGRDDD LFDHYAAVAQ RIGVYTATDY AGILEFLLRR WEVEKLGMGL
SGEGRRAQDY LCTLPQRIRR LEERANDRVK LASKSKPSVS FSWIYGREVE L
