WSD1_ARATH
ID WSD1_ARATH Reviewed; 481 AA.
AC Q93ZR6; Q9FHT5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 1 {ECO:0000303|PubMed:18621978};
DE Short=WS/DGAT 1 {ECO:0000303|PubMed:18621978};
DE AltName: Full=Diacylglycerol O-acyltransferase {ECO:0000303|PubMed:18621978};
DE Short=DGAT {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.20 {ECO:0000269|PubMed:18621978};
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.75 {ECO:0000269|PubMed:18621978};
DE AltName: Full=O-acyltransferase WSD1 {ECO:0000303|PubMed:18621978};
DE AltName: Full=Wax synthase {ECO:0000303|PubMed:18621978};
DE Short=WS {ECO:0000303|PubMed:18621978};
GN Name=WSD1 {ECO:0000303|PubMed:18621978};
GN OrderedLocusNames=At5g37300 {ECO:0000312|Araport:AT5G37300};
GN ORFNames=MNJ8.9 {ECO:0000312|EMBL:BAB09102.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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;
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].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, PATHWAY, 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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY DROUGHT; SALT AND ABSCISIC
RP ACID, 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 (PubMed:18621978). Involved in cuticular wax
CC biosynthesis (PubMed:18621978, PubMed:30729606). Required to reduce
CC leaf water loss, especially during drought (PubMed:30729606).
CC {ECO:0000269|PubMed:18621978, ECO:0000269|PubMed:30729606}.
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:18621978};
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:0000269|PubMed:18621978};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000269|PubMed:18621978}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000269|PubMed:18621978}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5KS41};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:18621978}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, top parts of stems,
CC and leaves (PubMed:18621978, PubMed:30729606). Not found in roots,
CC seeds and young seedlings (PubMed:18621978).
CC {ECO:0000269|PubMed:18621978, ECO:0000269|PubMed:30729606}.
CC -!- INDUCTION: Up-regulated in the stem epidermis during active wax
CC synthesis (PubMed:16299169). Induced in roots during drought and salt
CC stresses, and upon abscisic acid (ABA) treatment (PubMed:30729606).
CC {ECO:0000269|PubMed:16299169, ECO:0000269|PubMed:30729606}.
CC -!- DISRUPTION PHENOTYPE: Severe reduction in wax alkyl esters
CC (PubMed:18621978). Reduced wax ester coverage on leaves and stems
CC during normal and drought conditions leading to compromised growth and
CC relative water content due to an increased leaf water loss, especially
CC during drought (PubMed:30729606). {ECO:0000269|PubMed:18621978,
CC ECO:0000269|PubMed:30729606}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the long-chain O-
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09102.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB017069; BAB09102.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED94163.1; -; Genomic_DNA.
DR EMBL; AY056316; AAL07165.1; -; mRNA.
DR EMBL; BT015776; AAU90066.1; -; mRNA.
DR RefSeq; NP_001331809.1; NM_001344180.1.
DR RefSeq; NP_568547.1; NM_123089.3.
DR AlphaFoldDB; Q93ZR6; -.
DR SMR; Q93ZR6; -.
DR STRING; 3702.AT5G37300.1; -.
DR iPTMnet; Q93ZR6; -.
DR PaxDb; Q93ZR6; -.
DR ProteomicsDB; 242660; -.
DR EnsemblPlants; AT5G37300.1; AT5G37300.1; AT5G37300.
DR GeneID; 833704; -.
DR Gramene; AT5G37300.1; AT5G37300.1; AT5G37300.
DR KEGG; ath:AT5G37300; -.
DR Araport; AT5G37300; -.
DR TAIR; locus:2169175; AT5G37300.
DR eggNOG; ENOG502QTZ2; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR InParanoid; Q93ZR6; -.
DR OrthoDB; 828506at2759; -.
DR PhylomeDB; Q93ZR6; -.
DR BioCyc; ARA:AT5G37300-MON; -.
DR BRENDA; 2.3.1.20; 399.
DR UniPathway; UPA00282; -.
DR PRO; PR:Q93ZR6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93ZR6; baseline and differential.
DR Genevisible; Q93ZR6; 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: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; IDA:TAIR.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:UniProtKB.
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; Cell membrane; Endoplasmic reticulum; Membrane;
KW Reference proteome; Stress response; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..481
FT /note="Wax ester synthase/diacylglycerol acyltransferase 1"
FT /id="PRO_0000378331"
FT TOPO_DOM 1..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..481
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 481 AA; 54417 MW; F871EAE6F316E5D6 CRC64;
MKAEKVMERE IETTPIEPLS PMSHMLSSPN FFIVITFGFK TRCNRSAFVD GINNTLINAP
RFSSKMEINY KKKGEPVWIP VKLRVDDHII VPDLEYSNIQ NPDQFVEDYT SNIANIPMDM
SKPLWEFHLL NMKTSKAESL AIVKIHHSIG DGMSLMSLLL ACSRKISDPD ALVSNTTATK
KPADSMAWWL FVGFWFMIRV TFTTIVEFSK LMLTVCFLED TKNPLMGNPS DGFQSWKVVH
RIISFEDVKL IKDTMNMKVN DVLLGMTQAG LSRYLSSKYD GSTAEKKKIL EKLRVRGAVA
INLRPATKIE DLADMMAKGS KCRWGNFIGT VIFPLWVKSE KDPLEYIRRA KATMDRKKIS
LEAFFFYGII KFTLKFFGGK AVEAFGKRIF GHTSLAFSNV KGPDEEISFF HHPISYIAGS
ALVGAQALNI HFISYVDKIV INLAVDTTTI QDPNRLCDDM VEALEIIKSA TQGEIFHKTE
V
