KCS2_ARATH
ID KCS2_ARATH Reviewed; 528 AA.
AC Q5XEP9; O64485; Q56WE1; Q8VXW2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=3-ketoacyl-CoA synthase 2 {ECO:0000303|PubMed:18465198};
DE Short=KCS-2 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Docosanoic acid synthase {ECO:0000303|PubMed:18786002};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 2 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 2 {ECO:0000303|PubMed:18465198};
GN Name=KCS2 {ECO:0000303|PubMed:18465198};
GN Synonyms=DAISY {ECO:0000303|PubMed:18786002},
GN KCS17 {ECO:0000305|PubMed:12916765};
GN OrderedLocusNames=At1g04220 {ECO:0000312|Araport:AT1G04220};
GN ORFNames=F20D22.1 {ECO:0000312|EMBL:AAC16740.1};
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=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 [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] OF 6-528.
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] OF 11-528.
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 332-528.
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 [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 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 [8]
RP GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, AND TISSUE SPECIFICITY.
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP WOUNDING; DROUGHT AND SALT.
RX PubMed=18786002; DOI=10.1111/j.1365-313x.2008.03674.x;
RA Franke R., Hoefer R., Briesen I., Emsermann M., Efremova N., Yephremov A.,
RA Schreiber L.;
RT "The DAISY gene from Arabidopsis encodes a fatty acid elongase condensing
RT enzyme involved in the biosynthesis of aliphatic suberin in roots and the
RT chalaza-micropyle region of seeds.";
RL Plant J. 57:80-95(2009).
RN [10]
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 [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).
RN [12]
RP INDUCTION BY MYB94.
RX PubMed=25305760; DOI=10.1093/pcp/pcu142;
RA Lee S.B., Suh M.C.;
RT "Cuticular wax biosynthesis is up-regulated by the MYB94 transcription
RT factor in Arabidopsis.";
RL Plant Cell Physiol. 56:48-60(2015).
CC -!- FUNCTION: Mediates the synthesis of VLCFAs from 22 to 26 carbons in
CC length (e.g. C22, C24, C26) (PubMed:15277688). Involved in the
CC elongation of C20 fatty acid suberin precursors (PubMed:18786002).
CC Functionally redundant with KCS20 in the two-carbon elongation of C22
CC fatty acids that is required for cuticular wax and root suberin
CC biosynthesis (PubMed:19619160). {ECO:0000269|PubMed:15277688,
CC ECO:0000269|PubMed:18786002, 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 allidochlor,
CC anilofos, cafenstrole and flufenacet (PubMed:15277688). Strongly
CC inhibited by metazachlor (PubMed:22284369).
CC {ECO:0000269|PubMed:15277688, 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 siliques, flowers and stems
CC (PubMed:18465198). In young seedlings, expressed in the central
CC cylinder of primary roots, in emerging lateral roots and in their root
CC cap, but not in aboveground tissues such as hypocotyls, cotyledons and
CC leaves. Expressed in sepals in mature flowers and in the chalaza and
CC micropyle region of developing seeds shortly prior to or just after the
CC detachment from the funiculus (PubMed:18786002). Expressed in roots,
CC flowers, cauline leaves and siliques (PubMed:19619160).
CC {ECO:0000269|PubMed:18465198, ECO:0000269|PubMed:18786002,
CC ECO:0000269|PubMed:19619160}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Up-regulated by wounding, drought and salt
CC (PubMed:18786002). Strongly up-regulated by abscisic acid and drought,
CC and to a lower level, by salt and osmotic stress (PubMed:19619160). Up-
CC regulated by the MYB94 transcription factor (PubMed:25305760).
CC {ECO:0000269|PubMed:12916765, ECO:0000269|PubMed:18786002,
CC ECO:0000269|PubMed:19619160, ECO:0000269|PubMed:25305760}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in flowers or siliques, but
CC reduced root growth. Suberin with a significant decrease in VLCFA
CC derivatives longer than C20 (PubMed:18786002). No visible phenotype,
CC but reduced root growth. Kcs2 and kcs20 double mutants have a glossy
CC green appearance due to a significant reduction of the amount of
CC epicuticular wax crystals on the stems and siliques, a significant
CC reduction of C22 and C24 VLCFA derivatives in aliphatic suberin and a
CC roots growth retardation and abnormal lamellation of the suberin layer
CC in the endodermis (PubMed:19619160). {ECO:0000269|PubMed:18786002,
CC ECO:0000269|PubMed:19619160}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95022.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002411; AAC16740.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27671.1; -; Genomic_DNA.
DR EMBL; AY074518; AAL67132.1; -; mRNA.
DR EMBL; BT015917; AAU95453.1; -; mRNA.
DR EMBL; AK222101; BAD95022.1; ALT_INIT; mRNA.
DR PIR; T00951; T00951.
DR RefSeq; NP_171918.1; NM_100303.4.
DR AlphaFoldDB; Q5XEP9; -.
DR SMR; Q5XEP9; -.
DR BioGRID; 24813; 9.
DR STRING; 3702.AT1G04220.1; -.
DR ChEMBL; CHEMBL2242736; -.
DR PaxDb; Q5XEP9; -.
DR PRIDE; Q5XEP9; -.
DR ProteomicsDB; 247243; -.
DR EnsemblPlants; AT1G04220.1; AT1G04220.1; AT1G04220.
DR GeneID; 839578; -.
DR Gramene; AT1G04220.1; AT1G04220.1; AT1G04220.
DR KEGG; ath:AT1G04220; -.
DR Araport; AT1G04220; -.
DR TAIR; locus:2020215; AT1G04220.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q5XEP9; -.
DR OMA; VMCPKEL; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q5XEP9; -.
DR BioCyc; ARA:AT1G04220-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q5XEP9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5XEP9; baseline and differential.
DR Genevisible; Q5XEP9; 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:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0010345; P:suberin 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 2: Evidence at transcript level;
KW Acyltransferase; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..528
FT /note="3-ketoacyl-CoA synthase 2"
FT /id="PRO_0000249109"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 97..388
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 241
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 320
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 444
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT CONFLICT 453
FT /note="E -> G (in Ref. 3; AAL67132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59528 MW; FC47749CBBB26B3E CRC64;
MNENHIQSDH MNNTIHVTNK KLPNFLLSVR LKYVKLGYHY LISNAVYILI LPVGLLAATS
SSFSLTDLTL LYNHLLKFHF LSSTLFAALL IFLTTLYFTT RPRRIFLLDF ACYKPDSSLI
CTRETFMDRS QRVGIFTEDN LAFQQKILER SGLGQKTYFP EALLRVPPNP CMSEARKEAE
TVMFGAIDAV LEKTGVNPKD IGILVVNCSL FNPTPSLSAM IVNKYKLRGN VLSYNLGGMG
CSAGLISIDL AKQLLQVQPN SYALVVSTEN ITLNWYLGND RSMLLSNCIF RMGGAAVLLS
NRSSDRCRSK YQLIHTVRTH KGSDDNAFNC VYQREDNDDN KQIGVSLSKN LMAIAGEALK
TNITTLGPLV LPMSEQLLFF ATLVARKVFN VKKIKPYIPD FKLAFEHFCI HAGGRAVLDE
IEKNLDLSEW HMEPSRMTLN RFGNTSSSSL WYELAYSEAK GRIKRGDRTW QIAFGSGFKC
NSAVWRALRT IDPSKEKKKK TNPWIDEIHE FPVPVPRTSP VTSSSESR
