WSD8_ARATH
ID WSD8_ARATH Reviewed; 488 AA.
AC Q9FFE8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 8 {ECO:0000303|PubMed:18621978};
DE Short=WS/DGAT 8 {ECO:0000303|PubMed:18621978};
DE AltName: Full=Diacylglycerol O-acyltransferase WSD8 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q93ZR6};
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase WSD8 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.75 {ECO:0000250|UniProtKB:Q93ZR6};
GN Name=WSD8 {ECO:0000303|PubMed:18621978};
GN OrderedLocusNames=At5g16350 {ECO:0000312|Araport:AT5G16350};
GN ORFNames=MQK4.7 {ECO:0000312|EMBL:BAB09602.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 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 [5]
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 [6]
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 [7]
RP 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 (By similarity). Involved in cuticular wax biosynthesis
CC (By similarity). {ECO:0000250|UniProtKB:Q93ZR6}.
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:0000250|UniProtKB:Q93ZR6};
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:0000250|UniProtKB:Q93ZR6}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers and siliques and at low
CC levels in stems. {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; AB005242; BAB09602.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92282.1; -; Genomic_DNA.
DR EMBL; BT004100; AAO42125.1; -; mRNA.
DR EMBL; BT006151; AAP04136.1; -; mRNA.
DR RefSeq; NP_197139.1; NM_121640.5.
DR AlphaFoldDB; Q9FFE8; -.
DR SMR; Q9FFE8; -.
DR STRING; 3702.AT5G16350.1; -.
DR PaxDb; Q9FFE8; -.
DR PRIDE; Q9FFE8; -.
DR DNASU; 831496; -.
DR EnsemblPlants; AT5G16350.1; AT5G16350.1; AT5G16350.
DR GeneID; 831496; -.
DR Gramene; AT5G16350.1; AT5G16350.1; AT5G16350.
DR KEGG; ath:AT5G16350; -.
DR Araport; AT5G16350; -.
DR TAIR; locus:2171372; AT5G16350.
DR eggNOG; ENOG502QU8B; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR InParanoid; Q9FFE8; -.
DR OrthoDB; 828506at2759; -.
DR PhylomeDB; Q9FFE8; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFE8; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acyltransferase; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..488
FT /note="Wax ester synthase/diacylglycerol acyltransferase 8"
FT /id="PRO_0000452618"
FT TOPO_DOM 1..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..488
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 488 AA; 55105 MW; 96328FCD26263BEB CRC64;
MKNEEEEPLS PMARVFQSPD IDLCAIINIG FKTKINPDVV LDALKQNVYK HPRFSSKLSE
NGEKWIETEV NVEDHVIVPY IDPEDICEGG QSFVDDYISR LTLIPLDRSR PLWDIHILNV
KTSYAEAVGV IRFNHALADG MSFISLVLAC THKTSNPDML STAIPSVKRR STVSHSLKKT
GWFLTAIFTI GSTMRLIWNT LVDMFLLFAT MLFLKDTKTP LKGGANVRSN PKTFYHRNIS
LDDIKLIKNA MNMTINDVLL GITQAALSSY LNRRYEHENN NEEDGVLTSY TNNLPDRIRF
RAGCTVNLRS DIGFKPLAEM MVKDSKCRWG NYFSFIILPL SISLETDPLV YLNKSKAMMA
RTKHSYQAAL TYFLIKISLK VLGAKATTSL FNQHLMNITT CVSNVMGPME EISFNGHPVA
YISPSSYGHS HALLIHYTSY AGEMTITITV DPTVIPDPHK ICDDMEESLK TMKAVLWERG
LLKEAYKV
