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STAD3_ARATH
ID   STAD3_ARATH             Reviewed;         401 AA.
AC   Q9LF05;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 3.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase 3, chloroplastic;
DE            Short=Stearoyl-ACP desaturase 3;
DE            EC=1.14.19.2 {ECO:0000269|PubMed:17072561, ECO:0000269|PubMed:27681170};
DE   AltName: Full=Acyl-[acyl-carrier-protein] desaturase 3;
DE   Flags: Precursor;
GN   Name=S-ACP-DES3; Synonyms=AAD3, SAD3; OrderedLocusNames=At5g16230;
GN   ORFNames=T21H19_150;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY, FUNCTION, CATALYTIC ACTIVITY, 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   [5]
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. Also able to
CC       convert palmitoyl-ACP to palmitoleoyl-ACP at the C9 position. Exhibits
CC       delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD) activity.
CC       Involved in omega-7 monounsaturated fatty acid biosynthesis, especially
CC       in the endosperm oil (PubMed:27681170). {ECO:0000269|PubMed:17072561,
CC       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:17072561, 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: Ubiquitously expressed with a preference in leaves,
CC       flowers and stems. {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}.
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DR   EMBL; AL391148; CAC01864.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92263.1; -; Genomic_DNA.
DR   EMBL; BT029294; ABK32108.1; -; mRNA.
DR   PIR; T51493; T51493.
DR   RefSeq; NP_197127.1; NM_121628.4.
DR   AlphaFoldDB; Q9LF05; -.
DR   SMR; Q9LF05; -.
DR   STRING; 3702.AT5G16230.1; -.
DR   PaxDb; Q9LF05; -.
DR   PRIDE; Q9LF05; -.
DR   ProteomicsDB; 228342; -.
DR   EnsemblPlants; AT5G16230.1; AT5G16230.1; AT5G16230.
DR   GeneID; 831483; -.
DR   Gramene; AT5G16230.1; AT5G16230.1; AT5G16230.
DR   KEGG; ath:AT5G16230; -.
DR   Araport; AT5G16230; -.
DR   TAIR; locus:2181427; AT5G16230.
DR   eggNOG; ENOG502QRJK; Eukaryota.
DR   HOGENOM; CLU_034505_1_0_1; -.
DR   InParanoid; Q9LF05; -.
DR   OrthoDB; 608188at2759; -.
DR   BRENDA; 1.14.19.2; 399.
DR   UniPathway; UPA00199; -.
DR   PRO; PR:Q9LF05; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LF05; baseline and differential.
DR   Genevisible; Q9LF05; 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:0009960; P:endosperm development; IMP:TAIR.
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..35
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..401
FT                   /note="Stearoyl-[acyl-carrier-protein] 9-desaturase 3,
FT                   chloroplastic"
FT                   /id="PRO_0000401421"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
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         231
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         264
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         264
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="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   SITE            216
FT                   /note="Confers substrate specificity"
FT                   /evidence="ECO:0000305|PubMed:27681170"
SQ   SEQUENCE   401 AA;  45860 MW;  8EE1D3EEF09BF65C CRC64;
     MSMALLLTSP AMKQKPAVIT SPRRGSSPSR RLRVSCVTTN PARKKNETCN HFRPIKEVNN
     QLTHTIPQEK LEIFKSMENW AEQKLLPYLK PVEDSWQPQD FLPAPENDDE FYDRVKEIRE
     RTKEIPDDYF VVLVGDMITE EALPTYQTTL NTLDGVKDET GGSLSPWAVW IRAWTAEENR
     HGDLLNKYLY LTGRVDMRHV EKTIQYLIGS GMDSKFENNP YNGFIYTSFQ ERATFISHGN
     TARLATTYGD VTLAKICGTI AADEKRHETA YTKIVEKLFE IDPDGSVQAL ASMMKKRITM
     PAHLMHDGRD NDLFDHYAAV AQRIGVYTAA DYAGILEFLL RRWKVESLGL GLSGEGRRAQ
     EYLCTLPQRI KRLEERANDR VKLVSKPSVS FSWVFGRDVK L
 
 
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