KCS20_ARATH
ID KCS20_ARATH Reviewed; 529 AA.
AC Q9FG87; Q94CA1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=3-ketoacyl-CoA synthase 20 {ECO:0000303|PubMed:18465198};
DE Short=KCS-20 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 20 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 20 {ECO:0000303|PubMed:18465198};
GN Name=KCS20 {ECO:0000303|PubMed:18465198};
GN Synonyms=KCS19 {ECO:0000305|PubMed:12916765};
GN OrderedLocusNames=At5g43760 {ECO:0000312|Araport:AT5G43760};
GN ORFNames=MQD19.11 {ECO:0000312|EMBL:BAB11304.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 TISSUE SPECIFICITY.
RX PubMed=15914083; DOI=10.1016/j.bbalip.2005.04.002;
RA Costaglioli P., Joubes J., Garcia C., Stef M., Arveiler B., Lessire R.,
RA Garbay B.;
RT "Profiling candidate genes involved in wax biosynthesis in Arabidopsis
RT thaliana by microarray analysis.";
RL Biochim. Biophys. Acta 1734:247-258(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=15277688; DOI=10.1073/pnas.0404600101;
RA Trenkamp S., Martin W., Tietjen K.;
RT "Specific and differential inhibition of very-long-chain fatty acid
RT elongases from Arabidopsis thaliana by different herbicides.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11903-11908(2004).
RN [6]
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 [7]
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19619160; DOI=10.1111/j.1365-313x.2009.03973.x;
RA Lee S.B., Jung S.J., Go Y.S., Kim H.U., Kim J.K., Cho H.J., Park O.K.,
RA Suh M.C.;
RT "Two Arabidopsis 3-ketoacyl CoA synthase genes, KCS20 and KCS2/DAISY, are
RT functionally redundant in cuticular wax and root suberin biosynthesis, but
RT differentially controlled by osmotic stress.";
RL Plant J. 60:462-475(2009).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=22284369; DOI=10.1016/j.phytochem.2011.12.023;
RA Tresch S., Heilmann M., Christiansen N., Looser R., Grossmann K.;
RT "Inhibition of saturated very-long-chain fatty acid biosynthesis by
RT mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA
RT synthases.";
RL Phytochemistry 76:162-171(2012).
CC -!- FUNCTION: Mediates the synthesis of VLCFAs from 22 to 26 carbons in
CC length (e.g. C22, C24, C26) (PubMed:15277688). Functionally redundant
CC with KCS2 in the two-carbon elongation of C22 fatty acids that is
CC required for cuticular wax and root suberin biosynthesis
CC (PubMed:19619160). {ECO:0000269|PubMed:15277688,
CC ECO:0000269|PubMed:19619160}.
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 -!- ACTIVITY REGULATION: Inhibited by K3 herbicides such as alachlor,
CC allidochlor, anilofos, cafenstrole, fentrazamide and flufenacet
CC (PubMed:15277688). Strongly inhibited by metazachlor and only slightly
CC by mefluidide (PubMed:22284369). {ECO:0000269|PubMed:15277688,
CC ECO:0000269|PubMed:22284369}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15277688}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:15277688}.
CC -!- TISSUE SPECIFICITY: Expressed in aerial organs (PubMed:15914083).
CC Expressed in leaves, flowers, siliques and stems (PubMed:18465198).
CC Expressed in roots, young seedlings, leaves, flowers and siliques
CC (PubMed:19619160). {ECO:0000269|PubMed:15914083,
CC ECO:0000269|PubMed:18465198, ECO:0000269|PubMed:19619160}.
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). Up-
CC regulated twofold by drought, but no effect of other stress treatments
CC (PubMed:19619160). {ECO:0000269|PubMed:12916765,
CC ECO:0000269|PubMed:18465198, ECO:0000269|PubMed:19619160}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but reduced root growth.
CC Kcs2 and kcs20 double mutants have a glossy green appearance due to a
CC significant reduction of the amount of epicuticular wax crystals on the
CC stems and siliques, a significant reduction of C22 and C24 VLCFA
CC derivatives in aliphatic suberin and a roots growth retardation and
CC abnormal lamellation of the suberin layer in the endodermis.
CC {ECO:0000269|PubMed:19619160}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AB026651; BAB11304.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95007.1; -; Genomic_DNA.
DR EMBL; AF424620; AAL11613.1; -; mRNA.
DR EMBL; AY035030; AAK59535.1; -; mRNA.
DR EMBL; AY150469; AAN12994.1; -; mRNA.
DR RefSeq; NP_199189.1; NM_123743.4.
DR AlphaFoldDB; Q9FG87; -.
DR SMR; Q9FG87; -.
DR BioGRID; 19648; 3.
DR IntAct; Q9FG87; 3.
DR STRING; 3702.AT5G43760.1; -.
DR ChEMBL; CHEMBL2242734; -.
DR PaxDb; Q9FG87; -.
DR PRIDE; Q9FG87; -.
DR ProteomicsDB; 247242; -.
DR EnsemblPlants; AT5G43760.1; AT5G43760.1; AT5G43760.
DR GeneID; 834398; -.
DR Gramene; AT5G43760.1; AT5G43760.1; AT5G43760.
DR KEGG; ath:AT5G43760; -.
DR Araport; AT5G43760; -.
DR TAIR; locus:2170837; AT5G43760.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9FG87; -.
DR OMA; HYLISHF; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9FG87; -.
DR BioCyc; ARA:AT5G43760-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9FG87; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG87; baseline and differential.
DR Genevisible; Q9FG87; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009922; F:fatty acid elongase activity; IDA:TAIR.
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; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..529
FT /note="3-ketoacyl-CoA synthase 20"
FT /id="PRO_0000249111"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 103..396
FT /note="FAE"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 326
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 415
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 419
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 452
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT CONFLICT 348
FT /note="T -> A (in Ref. 3; AAK59535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 59307 MW; 5687F64CA91FEAA7 CRC64;
MSHNQNQPHR PVPVHVTNAE PNPNPNNLPN FLLSVRLKYV KLGYHYLISN ALYILLLPLL
AATIANLSSF TINDLSLLYN TLRFHFLSAT LATALLISLS TAYFTTRPRR VFLLDFSCYK
PDPSLICTRE TFMDRSQRVG IFTEDNLAFQ QKILERSGLG QKTYFPEALL RVPPNPCMEE
ARKEAETVMF GAIDAVLEKT GVKPKDIGIL VVNCSLFNPT PSLSAMIVNK YKLRGNILSY
NLGGMGCSAG LISIDLAKQM LQVQPNSYAL VVSTENITLN WYLGNDRSML LSNCIFRMGG
AAVLLSNRSS DRSRSKYQLI HTVRTHKGAD DNAFGCVYQR EDNNAEETGK IGVSLSKNLM
AIAGEALKTN ITTLGPLVLP MSEQLLFFAT LVARKVFKVK KIKPYIPDFK LAFEHFCIHA
GGRAVLDEIE KNLDLSEWHM EPSRMTLNRF GNTSSSSLWY ELAYSEAKGR IKRGDRTWQI
AFGSGFKCNS AVWKALRTID PMDEKTNPWI DEIDDFPVQV PRITPITSS
