WSD3_ARATH
ID WSD3_ARATH Reviewed; 487 AA.
AC F4IU14; Q0WVI1; Q84RJ9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 3 {ECO:0000303|PubMed:18621978};
DE Short=WS/DGAT 3 {ECO:0000303|PubMed:18621978};
DE AltName: Full=Diacylglycerol O-acyltransferase WSD3 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q93ZR6};
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase WSD3 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.75 {ECO:0000250|UniProtKB:Q93ZR6};
GN Name=WSD3 {ECO:0000303|PubMed:18621978};
GN OrderedLocusNames=At2g38995 {ECO:0000312|Araport:AT2G38995}; ORFNames=T7F6;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IU14-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IU14-2; Sequence=VSP_061025, VSP_061026, VSP_061027;
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers and siliques.
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; AC005770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC09622.1; -; Genomic_DNA.
DR EMBL; AY231419; AAO86847.1; -; mRNA.
DR EMBL; AY649239; AAT69156.1; -; Genomic_DNA.
DR EMBL; AK226769; BAE98867.1; -; mRNA.
DR RefSeq; NP_001189709.1; NM_001202780.2. [F4IU14-1]
DR AlphaFoldDB; F4IU14; -.
DR SMR; F4IU14; -.
DR STRING; 3702.AT2G38995.1; -.
DR PRIDE; F4IU14; -.
DR ProteomicsDB; 211899; -.
DR EnsemblPlants; AT2G38995.2; AT2G38995.2; AT2G38995. [F4IU14-1]
DR GeneID; 818485; -.
DR Gramene; AT2G38995.2; AT2G38995.2; AT2G38995. [F4IU14-1]
DR KEGG; ath:AT2G38995; -.
DR Araport; AT2G38995; -.
DR eggNOG; ENOG502QTZ2; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR OrthoDB; 828506at2759; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IU14; 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 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 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Cell membrane;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..487
FT /note="Wax ester synthase/diacylglycerol acyltransferase 3"
FT /id="PRO_0000452613"
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..487
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT VAR_SEQ 2..72
FT /note="YTMKKGKDMAKEEQETAAIEPLSPVSQLFVSPSLYCFIIFTLGFQTRCNPST
FT IVEGVKNTWIKLPRFSSKV -> FQ (in isoform 2)"
FT /id="VSP_061025"
FT VAR_SEQ 263..275
FT /note="KVNDVLLGMTQAG -> VRIFNIHIGIFFL (in isoform 2)"
FT /id="VSP_061026"
FT VAR_SEQ 276..487
FT /note="Missing (in isoform 2)"
FT /id="VSP_061027"
FT CONFLICT F4IU14-2:3
FT /note="Q -> R (in Ref. 3; AAO86847 and 4; AAT69156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 55226 MW; A3F1EAA1C96402F6 CRC64;
MYTMKKGKDM AKEEQETAAI EPLSPVSQLF VSPSLYCFII FTLGFQTRCN PSTIVEGVKN
TWIKLPRFSS KVEIKKNGKA SWVPVSVRVE DHVVVPDLDY SNIENPDQFI EDYTSKLANT
PMDMSRPLWE LHLLNIKTSN AESLAIGKFH HSLGDGMSLI SLLLASSRKT SDPDALPTTA
ATRKHASSNK KSWWLVGRFW FMIRIIFTTV VELFKYLLTL CFMRDTKTPL MGKTGDAIRS
RKVIHRIVSF DDVKLVKNNM DMKVNDVLLG MTQAGLSRYL SRKYDEDMVV EKKKNLEKIR
LRGTVFVNLR ADTKLEDLAN MMAKGSKCRW GNFVGVIIFP LWVRSEDDPL EYVRRAKSTM
DIKKLSIESL ICYGLIKLTR KILGGKVVET LVRRLFDHTT LTFSNVMGPD EDISFFDHPM
SYVAASALGG PQALIIHYVT YVNKIVINLA VDTSVIRDPH LLCDDLVESL DIIKLAAMEK
GVHKMEV
