KCS12_ARATH
ID KCS12_ARATH Reviewed; 476 AA.
AC Q9SIB2; Q8LFQ0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=3-ketoacyl-CoA synthase 12 {ECO:0000303|PubMed:18465198};
DE Short=KCS-12 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 12 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 12 {ECO:0000303|PubMed:18465198};
DE Flags: Precursor;
GN Name=KCS12 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At2g28630 {ECO:0000312|Araport:AT2G28630};
GN ORFNames=T8O18.8 {ECO:0000312|EMBL:AAD24372.1};
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;
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND 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).
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
CC {ECO:0000269|PubMed:18465198}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, flowers and leaves.
CC {ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Up-regulated by osmotic stress and down-regulated by
CC low temperature, salt and drought (PubMed:18465198).
CC {ECO:0000269|PubMed:12916765, ECO:0000269|PubMed:18465198}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AC007171; AAD24372.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08152.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62747.1; -; Genomic_DNA.
DR EMBL; AY056170; AAL07019.1; -; mRNA.
DR EMBL; AY091195; AAM14134.1; -; mRNA.
DR EMBL; AY084716; AAM61290.1; -; mRNA.
DR PIR; C84687; C84687.
DR RefSeq; NP_001318305.1; NM_001336183.1.
DR RefSeq; NP_180431.1; NM_128424.3.
DR AlphaFoldDB; Q9SIB2; -.
DR SMR; Q9SIB2; -.
DR STRING; 3702.AT2G28630.1; -.
DR PaxDb; Q9SIB2; -.
DR PRIDE; Q9SIB2; -.
DR ProteomicsDB; 247147; -.
DR EnsemblPlants; AT2G28630.1; AT2G28630.1; AT2G28630.
DR EnsemblPlants; AT2G28630.2; AT2G28630.2; AT2G28630.
DR GeneID; 817412; -.
DR Gramene; AT2G28630.1; AT2G28630.1; AT2G28630.
DR Gramene; AT2G28630.2; AT2G28630.2; AT2G28630.
DR KEGG; ath:AT2G28630; -.
DR Araport; AT2G28630; -.
DR TAIR; locus:2065499; AT2G28630.
DR eggNOG; ENOG502QPV6; Eukaryota.
DR HOGENOM; CLU_013238_3_1_1; -.
DR InParanoid; Q9SIB2; -.
DR OMA; TYGWINE; -.
DR OrthoDB; 663765at2759; -.
DR PhylomeDB; Q9SIB2; -.
DR BioCyc; ARA:AT2G28630-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9SIB2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIB2; baseline and differential.
DR Genevisible; Q9SIB2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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 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; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..476
FT /note="3-ketoacyl-CoA synthase 12"
FT /id="PRO_0000249104"
FT DOMAIN 26..313
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 168
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 247
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 344
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 348
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 377
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 381
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT CONFLICT 286
FT /note="E -> D (in Ref. 4; AAM61290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53974 MW; 04C9124611E75D87 CRC64;
MDLLFLFFSL LLSYLFFKIW KLIDSKQDKD CYILDYQCHK PTDDRMVSTQ FSGEIIYRNQ
NLGLTEYKFL LKAIVSSGIG EQTYAPRLVF EGREERPSLQ DGISEMEEFY VDSIGKLLER
NQISPKDIDI LVVNVSMLSS TPSLASRIIN HYKMRDDVKV FNLTGMGCSA SLISVDIVKN
IFKSYANKLA LVATSESLSP NWYSGNNRSM ILANCLFRSG GCAILLTNKR SLRKKAMFKL
KCMVRTHHGA REESYNCCIQ AEDEQGRVGF YLGKNLPKAA TRAFVENLKV ITPKILPVTE
LIRFMLKLLI KKIKIRQNPS KGSTNLPPGT PLKAGINFKT GIEHFCIHTG GKAVIDGIGH
SLDLNEYDIE PARMTLHRFG NTSASSLWYV LAYMEAKKRL KRGDRVFMIS FGAGFKCNSC
VWEVVRDLTG GESKGNVWNH CIDDYPPKSI LNPYLEKFGW IQDEDPDTFK VPDAFM
