WSD7_ARATH
ID WSD7_ARATH Reviewed; 480 AA.
AC Q94CK0; Q56XB1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 7 {ECO:0000303|PubMed:18621978};
DE Short=WS/DGAT 7 {ECO:0000303|PubMed:18621978};
DE AltName: Full=Diacylglycerol O-acyltransferase WSD7 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q93ZR6};
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase WSD7 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.75 {ECO:0000269|PubMed:30729606};
GN Name=WSD7 {ECO:0000303|PubMed:18621978};
GN OrderedLocusNames=At5g12420 {ECO:0000312|Araport:AT5G12420};
GN ORFNames=T2L20 {ECO:0000312|EMBL:CAC42903.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-480.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [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 14, 16 and 18 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}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:30729606};
CC Multi-pass membrane protein {ECO:0000255}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93847.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL592312; CAC42903.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91807.1; -; Genomic_DNA.
DR EMBL; AK117487; BAC42150.1; -; mRNA.
DR EMBL; AY080798; AAL87279.1; -; mRNA.
DR EMBL; AY114076; AAM45124.1; -; mRNA.
DR EMBL; AK221764; BAD93847.1; ALT_INIT; mRNA.
DR RefSeq; NP_568275.1; NM_121280.4.
DR AlphaFoldDB; Q94CK0; -.
DR SMR; Q94CK0; -.
DR IntAct; Q94CK0; 5.
DR STRING; 3702.AT5G12420.1; -.
DR PaxDb; Q94CK0; -.
DR PRIDE; Q94CK0; -.
DR ProteomicsDB; 183463; -.
DR EnsemblPlants; AT5G12420.1; AT5G12420.1; AT5G12420.
DR GeneID; 831117; -.
DR Gramene; AT5G12420.1; AT5G12420.1; AT5G12420.
DR KEGG; ath:AT5G12420; -.
DR Araport; AT5G12420; -.
DR TAIR; locus:505006610; AT5G12420.
DR eggNOG; ENOG502QU8B; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR InParanoid; Q94CK0; -.
DR OMA; RNPTRFY; -.
DR OrthoDB; 828506at2759; -.
DR PhylomeDB; Q94CK0; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94CK0; 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; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Stress response;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..480
FT /note="Wax ester synthase/diacylglycerol acyltransferase 7"
FT /id="PRO_0000452617"
FT TOPO_DOM 1..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..329
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..480
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 480 AA; 53996 MW; B97AF65D56462C51 CRC64;
MTYGEEEPVS PMARVFQSPG IDLCAVTIMG FKTKINPDVV LDALKQNVSK HPRFSSILSD
NGAKWIETEV NVEDHVIVPY IDAEEIGEGG QSFIDDYMSR LTMIPLDRSR PLWDIHILNV
KTSEAEAVGF IRSHHSLGDG MSLISLMLAC THKTSDPDMF SNAIPSMKRR ATMSHSLKTK
GWFLRSIFTI GSTMRLLWNT TIDMLLLLAT VLFLKDTKTP LKAGADVRSN PKRFYHRIIS
LDDIKLIKNA MNMTINDVLF GITQASLSHY LNRQYGTKKE EDGALTSYRN NLPDGIRFRV
ACTVNLRSDI GFKPLADMMV KDSKCRWGNY FSFIFLPFTI GLQTDPLVYL KMSKSMMARK
KHSYHAALVY FIIKIVLKVF GAKAAAELFD RPVRNTTTCV SNVIGPMEEI SFRGHPVSYI
APSSYGHSHA LLIHLMSYAD KMIISLAYDP TVISDPHKIC DDMEESLKAM KASLCERGLL
