KCS6_ARATH
ID KCS6_ARATH Reviewed; 497 AA.
AC Q9XF43; Q3ECG1; Q56ZC4; Q8VYJ5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=3-ketoacyl-CoA synthase 6 {ECO:0000303|PubMed:18465198};
DE Short=KCS-6 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000269|PubMed:10330468};
DE AltName: Full=Cuticular protein 1 {ECO:0000303|PubMed:10330468};
DE AltName: Full=Eceriferum 6 {ECO:0000303|PubMed:11041893};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 6 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 6 {ECO:0000303|PubMed:18465198};
GN Name=CUT1 {ECO:0000303|PubMed:10330468};
GN Synonyms=CER6 {ECO:0000303|PubMed:11041893}, EL6,
GN KCS6 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At1g68530 {ECO:0000312|Araport:AT1G68530};
GN ORFNames=T26J14.10 {ECO:0000312|EMBL:AAG52390.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=10330468; DOI=10.2307/3870817;
RA Millar A.A., Clemens S., Zachgo S., Giblin E.M., Taylor D.C., Kunst L.;
RT "CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and
RT pollen fertility, encodes a very-long-chain fatty acid condensing enzyme.";
RL Plant Cell 11:825-838(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11041893; DOI=10.2307/3871209;
RA Fiebig A., Mayfield J.A., Miley N.L., Chau S., Fischer R.L., Preuss D.;
RT "Alterations in CER6, a gene identical to CUT1, differentially affect long-
RT chain lipid content on the surface of pollen and stems.";
RL Plant Cell 12:2001-2008(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 408-497.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12177469; DOI=10.1104/pp.003707;
RA Hooker T.S., Millar A.A., Kunst L.;
RT "Significance of the expression of the CER6 condensing enzyme for cuticular
RT wax production in Arabidopsis.";
RL Plant Physiol. 129:1568-1580(2002).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12467640; DOI=10.1016/s0163-7827(02)00045-0;
RA Kunst L., Samuels A.L.;
RT "Biosynthesis and secretion of plant cuticular wax.";
RL Prog. Lipid Res. 42:51-80(2003).
RN [10]
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).
RN [11]
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: Contributes to cuticular wax and suberin biosynthesis.
CC Involved in both decarbonylation and acyl-reduction wax synthesis
CC pathways. Required for elongation of C24 fatty acids, an essential step
CC of the cuticular wax production (PubMed:10330468, PubMed:11041893).
CC Major condensing enzyme for stem wax and pollen coat lipid biosynthesis
CC (PubMed:12467640). {ECO:0000269|PubMed:10330468,
CC ECO:0000269|PubMed:11041893, ECO:0000269|PubMed:12467640}.
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:0000269|PubMed:10330468};
CC -!- ACTIVITY REGULATION: Strongly inhibited by metazachlor and mefluidide.
CC {ECO:0000269|PubMed:22284369}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12467640, ECO:0000269|PubMed:18465198}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XF43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XF43-2; Sequence=VSP_022340, VSP_022341;
CC -!- TISSUE SPECIFICITY: In epidermal cells of aerial tissues and in the
CC tapetum of anthers near maturity (PubMed:10330468, PubMed:12177469).
CC Expressed in siliques, flowers and leaves (PubMed:18465198).
CC {ECO:0000269|PubMed:10330468, ECO:0000269|PubMed:12177469,
CC ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Up-regulated by osmotic stress and abscisic acid and
CC down-regulated by darkness (PubMed:12177469, PubMed:18465198). Down-
CC regulated by low temperature and up-regulated by salt and drought
CC (PubMed:18465198). {ECO:0000269|PubMed:12177469,
CC ECO:0000269|PubMed:12916765, ECO:0000269|PubMed:18465198}.
CC -!- DISRUPTION PHENOTYPE: Plants have no wax crystals and are male sterile.
CC {ECO:0000269|PubMed:10330468}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94789.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF129511; AAD37122.1; -; mRNA.
DR EMBL; AC011915; AAG52390.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34804.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34805.1; -; Genomic_DNA.
DR EMBL; AY070727; AAL50069.1; -; mRNA.
DR EMBL; AY093969; AAM16230.1; -; mRNA.
DR EMBL; AK221042; BAD94789.1; ALT_INIT; mRNA.
DR PIR; T52308; T52308.
DR RefSeq; NP_177020.1; NM_105524.3. [Q9XF43-1]
DR RefSeq; NP_849861.1; NM_179530.1. [Q9XF43-2]
DR AlphaFoldDB; Q9XF43; -.
DR SMR; Q9XF43; -.
DR BioGRID; 28403; 9.
DR STRING; 3702.AT1G68530.1; -.
DR PaxDb; Q9XF43; -.
DR PRIDE; Q9XF43; -.
DR ProteomicsDB; 230117; -. [Q9XF43-1]
DR EnsemblPlants; AT1G68530.1; AT1G68530.1; AT1G68530. [Q9XF43-1]
DR EnsemblPlants; AT1G68530.2; AT1G68530.2; AT1G68530. [Q9XF43-2]
DR GeneID; 843182; -.
DR Gramene; AT1G68530.1; AT1G68530.1; AT1G68530. [Q9XF43-1]
DR Gramene; AT1G68530.2; AT1G68530.2; AT1G68530. [Q9XF43-2]
DR KEGG; ath:AT1G68530; -.
DR Araport; AT1G68530; -.
DR TAIR; locus:2201262; AT1G68530.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9XF43; -.
DR OMA; PWSEQIK; -.
DR PhylomeDB; Q9XF43; -.
DR BioCyc; ARA:AT1G68530-MON; -.
DR BioCyc; MetaCyc:AT1G68530-MON; -.
DR BRENDA; 2.3.1.199; 399.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9XF43; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XF43; baseline and differential.
DR Genevisible; Q9XF43; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0005739; C:mitochondrion; HDA: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 GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR GO; GO:0010025; P:wax biosynthetic process; IMP: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 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..497
FT /note="3-ketoacyl-CoA synthase 6"
FT /id="PRO_0000249098"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 81..370
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 225
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 304
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 388
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 392
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 421
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 425
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT VAR_SEQ 350..377
FT /note="PLVLPASEQLLFLTSLIGRKIFNPKWKP -> NKHTSFYFTYIYTLTMIYTV
FT KTISRGGH (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_022340"
FT VAR_SEQ 378..497
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_022341"
FT CONFLICT 73
FT /note="F -> L (in Ref. 5; AAL50069/AAM16230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 56396 MW; B371C7948B33D6EB CRC64;
MPQAPMPEFS SSVKLKYVKL GYQYLVNHFL SFLLIPIMAI VAVELLRMGP EEILNVWNSL
QFDLVQVLCS SFFVIFISTV YFMSKPRTIY LVDYSCYKPP VTCRVPFATF MEHSRLILKD
KPKSVEFQMR ILERSGLGEE TCLPPAIHYI PPTPTMDAAR SEAQMVIFEA MDDLFKKTGL
KPKDVDILIV NCSLFSPTPS LSAMVINKYK LRSNIKSFNL SGMGCSAGLI SVDLARDLLQ
VHPNSNAIIV STEIITPNYY QGNERAMLLP NCLFRMGAAA IHMSNRRSDR WRAKYKLSHL
VRTHRGADDK SFYCVYEQED KEGHVGINLS KDLMAIAGEA LKANITTIGP LVLPASEQLL
FLTSLIGRKI FNPKWKPYIP DFKLAFEHFC IHAGGRAVID ELQKNLQLSG EHVEASRMTL
HRFGNTSSSS LWYELSYIES KGRMRRGDRV WQIAFGSGFK CNSAVWKCNR TIKTPKDGPW
SDCIDRYPVF IPEVVKL
