KCS8_ARATH
ID KCS8_ARATH Reviewed; 481 AA.
AC Q4V3C9; Q9ZUK2;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=3-ketoacyl-CoA synthase 8 {ECO:0000303|PubMed:18465198};
DE Short=KCS-8 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 8 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 8 {ECO:0000303|PubMed:18465198};
GN Name=KCS8 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At2g15090 {ECO:0000312|Araport:AT2G15090};
GN ORFNames=T15J14.13 {ECO:0000312|EMBL:AAD03366.1};
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 Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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 membrane
CC {ECO:0000269|PubMed:18465198}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and seedlings.
CC {ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Down-regulated by darkness, low temperature, drought
CC and osmotic stress (PubMed:18465198). {ECO:0000269|PubMed:12916765,
CC ECO:0000269|PubMed:18465198}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD03366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005957; AAD03366.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC06369.1; -; Genomic_DNA.
DR EMBL; BT023427; AAY56418.1; -; mRNA.
DR EMBL; AK229027; BAF00913.1; -; mRNA.
DR PIR; H84524; H84524.
DR RefSeq; NP_179113.2; NM_127071.3.
DR AlphaFoldDB; Q4V3C9; -.
DR SMR; Q4V3C9; -.
DR STRING; 3702.AT2G15090.1; -.
DR PaxDb; Q4V3C9; -.
DR PRIDE; Q4V3C9; -.
DR ProteomicsDB; 247150; -.
DR EnsemblPlants; AT2G15090.1; AT2G15090.1; AT2G15090.
DR GeneID; 815998; -.
DR Gramene; AT2G15090.1; AT2G15090.1; AT2G15090.
DR KEGG; ath:AT2G15090; -.
DR Araport; AT2G15090; -.
DR TAIR; locus:2055782; AT2G15090.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q4V3C9; -.
DR OMA; FECATQE; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q4V3C9; -.
DR BioCyc; ARA:AT2G15090-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q4V3C9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q4V3C9; baseline and differential.
DR Genevisible; Q4V3C9; 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: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; 2.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..481
FT /note="3-ketoacyl-CoA synthase 8"
FT /id="PRO_0000249100"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 61..358
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 213
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 292
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 376
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 380
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 409
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 413
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 481 AA; 54191 MW; 577065209EFF1B7C CRC64;
MKNLKMVFFK ILFISLMAGL AMKGSKINVE DLQKFSLHHT QNNLQTISLL LFLVVFVWIL
YMLTRPKPVY LVDFSCYLPP SHLKVSIQTL MGHARRAREA GMCWKNKESD HLVDFQEKIL
ERSGLGQETY IPEGLQCFPL QQGMGASRKE TEEVIFGALD NLFRNTGVKP DDIGILVVNS
STFNPTPSLA SMIVNKYKLR DNIKSLNLGG MGCSAGVIAV DVAKGLLQVH RNTYAIVVST
ENITQNLYLG KNKSMLVTNC LFRVGGAAVL LSNRSRDRNR AKYELVHTVR IHTGSDDRSF
ECATQEEDED GIIGVTLTKN LPMVAARTLK INIATLGPLV LPLKEKLAFF ITFVKKKYFK
PELRNYTPDF KLAFEHFCIH AGGRALIDEL EKNLKLSPLH VEASRMTLHR FGNTSSSSIW
YELAYTEAKG RMKEGDRIWQ IALGSGFKCN SSVWVALRDV KPSANSPWED CMDRYPVEID
I