WSD6_ARATH
ID WSD6_ARATH Reviewed; 518 AA.
AC Q9M3B1; Q0WP61;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 6 {ECO:0000303|PubMed:18621978, ECO:0000303|PubMed:30729606};
DE Short=WS/DGAT 6 {ECO:0000303|PubMed:18621978, ECO:0000303|PubMed:30729606};
DE AltName: Full=Diacylglycerol O-acyltransferase WSD6 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q93ZR6};
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase WSD6 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.75 {ECO:0000269|PubMed:30729606};
GN Name=WSD6 {ECO:0000303|PubMed:18621978, ECO:0000303|PubMed:30729606};
GN OrderedLocusNames=At3g49210 {ECO:0000312|Araport:AT3G49210};
GN ORFNames=F2K15.70 {ECO:0000312|EMBL:CAB66400.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 GENE FAMILY.
RX PubMed=12502715; DOI=10.1074/jbc.m210533200;
RA Kalscheuer R., Steinbuchel A.;
RT "A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
RT acyltransferase mediates wax ester and triacylglycerol biosynthesis in
RT Acinetobacter calcoaceticus ADP1.";
RL J. Biol. Chem. 278:8075-8082(2003).
RN [6]
RP INDUCTION.
RX PubMed=16299169; DOI=10.1104/pp.105.070805;
RA Suh M.C., Samuels A.L., Jetter R., Kunst L., Pollard M., Ohlrogge J.,
RA Beisson F.;
RT "Cuticular lipid composition, surface structure, and gene expression in
RT Arabidopsis stem epidermis.";
RL Plant Physiol. 139:1649-1665(2005).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18621978; DOI=10.1104/pp.108.123471;
RA Li F., Wu X., Lam P., Bird D., Zheng H., Samuels A.L., Jetter R., Kunst L.;
RT "Identification of the wax ester synthase/acyl-coenzyme A: diacylglycerol
RT acyltransferase WSD1 required for stem wax ester biosynthesis in
RT Arabidopsis.";
RL Plant Physiol. 148:97-107(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP REVIEW ON ACYL-LIPID METABOLISM.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INDUCTION BY DROUGHT;
RP SALT AND ABSCISIC ACID, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=30729606; DOI=10.1111/tpj.14269;
RA Patwari P., Salewski V., Gutbrod K., Kreszies T., Dresen-Scholz B.,
RA Peisker H., Steiner U., Meyer A.J., Schreiber L., Doermann P.;
RT "Surface wax esters contribute to drought tolerance in Arabidopsis.";
RL Plant J. 98:727-744(2019).
CC -!- FUNCTION: Bifunctional wax ester synthase/diacylglycerol
CC acyltransferase that uses acyl-CoAs with 16, 18 and 20 carbons as
CC substrates, preferably in combination with 16:0ol alcohol
CC (PubMed:30729606). Involved in cuticular wax biosynthesis (By
CC similarity). {ECO:0000250|UniProtKB:Q93ZR6,
CC ECO:0000269|PubMed:30729606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC Evidence={ECO:0000250|UniProtKB:Q93ZR6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester +
CC CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75;
CC Evidence={ECO:0000269|PubMed:30729606};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000250|UniProtKB:Q93ZR6}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000250|UniProtKB:Q93ZR6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5KS41};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:30729606}; Single-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:30729606};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M3B1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M3B1-2; Sequence=VSP_061028;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:30729606}.
CC -!- INDUCTION: Induced in roots and leaves during drought and salt
CC stresses, and upon abscisic acid (ABA) treatment (PubMed:30729606). Up-
CC regulated in the stem epidermis during active wax synthesis
CC (PubMed:16299169). {ECO:0000269|PubMed:16299169,
CC ECO:0000269|PubMed:30729606}.
CC -!- DISRUPTION PHENOTYPE: Normal wax ester loads on leaves.
CC {ECO:0000269|PubMed:30729606}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the long-chain O-
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AL132956; CAB66400.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78511.1; -; Genomic_DNA.
DR EMBL; BX824670; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK229221; BAF01088.1; -; mRNA.
DR PIR; T45826; T45826.
DR RefSeq; NP_190490.1; NM_114780.5. [Q9M3B1-1]
DR AlphaFoldDB; Q9M3B1; -.
DR SMR; Q9M3B1; -.
DR STRING; 3702.AT3G49210.1; -.
DR iPTMnet; Q0WP61; -.
DR PaxDb; Q9M3B1; -.
DR PRIDE; Q9M3B1; -.
DR ProteomicsDB; 187263; -.
DR EnsemblPlants; AT3G49210.1; AT3G49210.1; AT3G49210. [Q9M3B1-1]
DR GeneID; 824082; -.
DR Gramene; AT3G49210.1; AT3G49210.1; AT3G49210. [Q9M3B1-1]
DR KEGG; ath:AT3G49210; -.
DR Araport; AT3G49210; -.
DR TAIR; locus:2082936; AT3G49210.
DR eggNOG; ENOG502QTZ2; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR InParanoid; Q9M3B1; -.
DR OMA; NNGAKWG; -.
DR OrthoDB; 828506at2759; -.
DR PhylomeDB; Q9M3B1; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M3B1; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0102966; F:arachidoyl-CoA:1-dodecanol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; IDA:TAIR.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR PANTHER; PTHR31650; PTHR31650; 1.
DR Pfam; PF03007; WES_acyltransf; 1.
DR Pfam; PF06974; WS_DGAT_C; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cell membrane;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Stress response; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..518
FT /note="Wax ester synthase/diacylglycerol acyltransferase 6"
FT /id="PRO_0000452616"
FT TOPO_DOM 1..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..518
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..168
FT /note="Missing (in isoform 2)"
FT /id="VSP_061028"
FT CONFLICT 77
FT /note="M -> V (in Ref. 3; BX824670)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="N -> K (in Ref. 3; BX824670)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="T -> R (in Ref. 3; BX824670)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="S -> N (in Ref. 3; BX824670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 58529 MW; 3496A0D2399D1240 CRC64;
MEIKTRRDTS ETSVRKDDEE EVEEEQPLSP AARVFHAPEF NCYVISVIGI KKKIDPDVII
EGLKQTLIRH PRFSSKMVST SVGNKKRQTQ SWVRTNVVVT DHVIVSDIQT QNIENGNADA
FLETYVSNLT TVPLDISKPL WQLHLLDLKT SDAENVAVLK FHHSLGDGMS LMALVLACMR
KTSNPDELPS LPNQNRSSSR SSRLMAGSRG DSRFLWLVMV IWSAIMLVLN TVCDALEFIA
TTMFLKDTET PIKGDFRFSK SKRMCLVHRT VSLDDIKLIK NTMKMTVNDV VLGVSQAGLS
QYLDRRYGEK KKKVGEDQDS KRKATDMPKR IRLRSALLVN LRPNTGIQDL ADMMAKGSTC
RWGNWIGYIV FPFSIGLRDD PLQHLRRAKR IIDRKKNSLE AALTFVAGKF ILKTFGVQVA
AKIINRALSN TTMSFSNLIG PIEEISFYGH PITYMAPSVY GHPHALTMHF QSYMNQMTIS
LTVDPTVISD PHRLLDDWEK SLQSIKAAVQ ERDSRSLD
