KCS9_ARATH
ID KCS9_ARATH Reviewed; 512 AA.
AC Q9SIX1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=3-ketoacyl-CoA synthase 9 {ECO:0000303|PubMed:18465198};
DE Short=KCS-9 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 9 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 9 {ECO:0000303|PubMed:18465198};
GN Name=KCS9 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At2g16280 {ECO:0000312|Araport:AT2G16280};
GN ORFNames=F16F14.22 {ECO:0000312|EMBL:AAD22309.1};
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=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 [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 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 [4]
RP INDUCTION, AND GENE FAMILY.
RX PubMed=12916765; DOI=10.1002/ps.714;
RA Lechelt-Kunze C., Meissner R.C., Drewes M., Tietjen K.;
RT "Flufenacet herbicide treatment phenocopies the fiddlehead mutant in
RT Arabidopsis thaliana.";
RL Pest Manag. Sci. 59:847-856(2003).
RN [5]
RP GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=18465198; DOI=10.1007/s11103-008-9339-z;
RA Joubes J., Raffaele S., Bourdenx B., Garcia C., Laroche-Traineau J.,
RA Moreau P., Domergue F., Lessire R.;
RT "The VLCFA elongase gene family in Arabidopsis thaliana: phylogenetic
RT analysis, 3D modelling and expression profiling.";
RL Plant Mol. Biol. 67:547-566(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23585652; DOI=10.1104/pp.112.210450;
RA Kim J., Jung J.H., Lee S.B., Go Y.S., Kim H.J., Cahoon R., Markham J.E.,
RA Cahoon E.B., Suh M.C.;
RT "Arabidopsis 3-ketoacyl-coenzyme a synthase9 is involved in the synthesis
RT of tetracosanoic acids as precursors of cuticular waxes, suberins,
RT sphingolipids, and phospholipids.";
RL Plant Physiol. 162:567-580(2013).
CC -!- FUNCTION: Involved in the elongation of C22 to C24 fatty acids, which
CC are precursors for the biosynthesis of cuticular waxes, aliphatic
CC suberins, and membrane lipids, including sphingolipids and
CC phospholipids. {ECO:0000269|PubMed:23585652}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000305};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23585652}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, stems, leaves, flowers and
CC siliques (PubMed:18465198). Expressed in roots, leaves, and stems,
CC including epidermis, silique walls, sepals, the upper portion of the
CC styles, and seed coats, but not in developing embryos
CC (PubMed:23585652). {ECO:0000269|PubMed:18465198,
CC ECO:0000269|PubMed:23585652}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Down-regulated by darkness and low temperature, and
CC up-regulated by drought and osmotic stress (PubMed:18465198).
CC {ECO:0000269|PubMed:12916765, ECO:0000269|PubMed:18465198}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but significant reduction
CC in C24 VLCFAs and accumulation of C20 and C22 VLCFAs.
CC {ECO:0000269|PubMed:23585652}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK226284; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007047; AAD22309.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06480.1; -; Genomic_DNA.
DR EMBL; AK226284; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; F84538; F84538.
DR RefSeq; NP_179223.1; NM_127184.3.
DR AlphaFoldDB; Q9SIX1; -.
DR SMR; Q9SIX1; -.
DR BioGRID; 1483; 10.
DR STRING; 3702.AT2G16280.1; -.
DR iPTMnet; Q9SIX1; -.
DR PaxDb; Q9SIX1; -.
DR PRIDE; Q9SIX1; -.
DR ProteomicsDB; 230118; -.
DR EnsemblPlants; AT2G16280.1; AT2G16280.1; AT2G16280.
DR GeneID; 816124; -.
DR Gramene; AT2G16280.1; AT2G16280.1; AT2G16280.
DR KEGG; ath:AT2G16280; -.
DR Araport; AT2G16280; -.
DR TAIR; locus:2042684; AT2G16280.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_0_1; -.
DR InParanoid; Q9SIX1; -.
DR OMA; YQIWLHL; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9SIX1; -.
DR BioCyc; ARA:AT2G16280-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9SIX1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIX1; baseline and differential.
DR Genevisible; Q9SIX1; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR012392; 3-ktacl-CoA_syn.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR013601; FAE1_typ3_polyketide_synth.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR31561; PTHR31561; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR Pfam; PF08392; FAE1_CUT1_RppA; 1.
DR PIRSF; PIRSF036417; 3-ktacl-CoA_syn; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="3-ketoacyl-CoA synthase 9"
FT /id="PRO_0000249101"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 100..389
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 244
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 323
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 407
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 411
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 440
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 444
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 512 AA; 57973 MW; B4A92FA95F67F8EF CRC64;
MEAANEPVNG GSVQIRTENN ERRKLPNFLQ SVNMKYVKLG YHYLITHLFK LCLVPLMAVL
VTEISRLTTD DLYQIWLHLQ YNLVAFIFLS ALAIFGSTVY IMSRPRSVYL VDYSCYLPPE
SLQVKYQKFM DHSKLIEDFN ESSLEFQRKI LERSGLGEET YLPEALHCIP PRPTMMAARE
ESEQVMFGAL DKLFENTKIN PRDIGVLVVN CSLFNPTPSL SAMIVNKYKL RGNVKSFNLG
GMGCSAGVIS IDLAKDMLQV HRNTYAVVVS TENITQNWYF GNKKAMLIPN CLFRVGGSAI
LLSNKGKDRR RSKYKLVHTV RTHKGAVEKA FNCVYQEQDD NGKTGVSLSK DLMAIAGEAL
KANITTLGPL VLPISEQILF FMTLVTKKLF NSKLKPYIPD FKLAFDHFCI HAGGRAVIDE
LEKNLQLSQT HVEASRMTLH RFGNTSSSSI WYELAYIEAK GRMKKGNRVW QIAFGSGFKC
NSAVWVALNN VKPSVSSPWE HCIDRYPVKL DF
