KCS4_ARATH
ID KCS4_ARATH Reviewed; 516 AA.
AC Q9LN49; B3LF56;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=3-ketoacyl-CoA synthase 4 {ECO:0000303|PubMed:18465198};
DE Short=KCS-4 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 4 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 4 {ECO:0000303|PubMed:18465198};
GN Name=KCS4 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At1g19440 {ECO:0000312|Araport:AT1G19440};
GN ORFNames=F18O14.21 {ECO:0000312|EMBL:AAF79428.1};
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].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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).
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: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in siliques, flowers,
CC leaves and stems. {ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate.
CC {ECO:0000269|PubMed:12916765}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AC025808; AAF79428.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29852.1; -; Genomic_DNA.
DR EMBL; BT033044; ACE79746.1; -; mRNA.
DR PIR; F86327; F86327.
DR RefSeq; NP_173376.1; NM_101800.3.
DR AlphaFoldDB; Q9LN49; -.
DR SMR; Q9LN49; -.
DR STRING; 3702.AT1G19440.1; -.
DR PaxDb; Q9LN49; -.
DR PRIDE; Q9LN49; -.
DR ProteomicsDB; 247272; -.
DR EnsemblPlants; AT1G19440.1; AT1G19440.1; AT1G19440.
DR GeneID; 838528; -.
DR Gramene; AT1G19440.1; AT1G19440.1; AT1G19440.
DR KEGG; ath:AT1G19440; -.
DR Araport; AT1G19440; -.
DR TAIR; locus:2016397; AT1G19440.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9LN49; -.
DR OMA; EAMHLIP; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9LN49; -.
DR BioCyc; ARA:AT1G19440-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9LN49; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LN49; baseline and differential.
DR Genevisible; Q9LN49; AT.
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; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..516
FT /note="3-ketoacyl-CoA synthase 4"
FT /id="PRO_0000249096"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 104..393
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 248
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 327
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 411
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 415
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 444
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 448
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 516 AA; 57842 MW; 3EDD488EE755C367 CRC64;
MDGAGESRLG GDGGGDGSVG VQIRQTRMLP DFLQSVNLKY VKLGYHYLIS NLLTLCLFPL
AVVISVEASQ MNPDDLKQLW IHLQYNLVSI IICSAILVFG LTVYVMTRPR PVYLVDFSCY
LPPDHLKAPY ARFMEHSRLT GDFDDSALEF QRKILERSGL GEDTYVPEAM HYVPPRISMA
AAREEAEQVM FGALDNLFAN TNVKPKDIGI LVVNCSLFNP TPSLSAMIVN KYKLRGNIRS
YNLGGMGCSA GVIAVDLAKD MLLVHRNTYA VVVSTENITQ NWYFGNKKSM LIPNCLFRVG
GSAVLLSNKS RDKRRSKYRL VHVVRTHRGA DDKAFRCVYQ EQDDTGRTGV SLSKDLMAIA
GETLKTNITT LGPLVLPISE QILFFMTLVV KKLFNGKVKP YIPDFKLAFE HFCIHAGGRA
VIDELEKNLQ LSPVHVEASR MTLHRFGNTS SSSIWYELAY IEAKGRMRRG NRVWQIAFGS
GFKCNSAIWE ALRHVKPSNN SPWEDCIDKY PVTLSY
