WSD9_ARATH
ID WSD9_ARATH Reviewed; 482 AA.
AC Q9FK89;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 9 {ECO:0000303|PubMed:18621978};
DE Short=WS/DGAT 2 {ECO:0000303|PubMed:18621978};
DE AltName: Full=Diacylglycerol O-acyltransferase WSD9 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q93ZR6};
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase WSD9 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.75 {ECO:0000250|UniProtKB:Q93ZR6};
GN Name=WSD9 {ECO:0000303|PubMed:18621978};
GN OrderedLocusNames=At5g22490 {ECO:0000312|Araport:AT5G22490};
GN ORFNames=MQJ16.3 {ECO:0000312|EMBL:AED93033.1};
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 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 [4]
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 [5]
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 [6]
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}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems 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; AB012244; BAB09121.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93033.1; -; Genomic_DNA.
DR RefSeq; NP_197641.1; NM_122154.2.
DR AlphaFoldDB; Q9FK89; -.
DR SMR; Q9FK89; -.
DR STRING; 3702.AT5G22490.1; -.
DR PaxDb; Q9FK89; -.
DR PRIDE; Q9FK89; -.
DR EnsemblPlants; AT5G22490.1; AT5G22490.1; AT5G22490.
DR GeneID; 832310; -.
DR Gramene; AT5G22490.1; AT5G22490.1; AT5G22490.
DR KEGG; ath:AT5G22490; -.
DR Araport; AT5G22490; -.
DR TAIR; locus:2171152; AT5G22490.
DR eggNOG; ENOG502QU8B; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR InParanoid; Q9FK89; -.
DR OMA; NGAHDKT; -.
DR OrthoDB; 828506at2759; -.
DR PhylomeDB; Q9FK89; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK89; 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; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..482
FT /note="Wax ester synthase/diacylglycerol acyltransferase 9"
FT /id="PRO_0000452619"
FT TOPO_DOM 1..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..328
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..482
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 482 AA; 54478 MW; E8C6C3CF780486E8 CRC64;
MEKKMKEEEE EPLSPMARAF QEPSIDCGIV IKFGCKTKIN PDVIVDSLKL NVFKHPRFCS
LLDDDGTKWL RTDVVNVEEH VFVPDIDPKL TEEDVEWFVE DYISSITMIP LDRTKPLWEV
HILNAKTSDA EAICVIRCHH ALGDGVSILS LILASTRKTS EPEAFSTLPV PKCRESYNHR
RGFSFFRLVL VVCSTVRLIW NTLVDSFLCM ATIFFLKDTD TPLKGKPGAI KKFSHRIVSL
DDIKLIKNAM EMTINDVLLG VTEAALTRYL HQSYDKTNEE AGTSLTPNRQ DLLDRIRLRS
LIVVNLRPTG SQSIADMMAK GSKCRWGNYI SVILFPFTIA LQSDPLVYLS NVKSMIDRKK
NSLITYIIYT FSEFVIKAFG INVAVAFQRK IMLNTTMCIS NLPGPTEEVS FHGHPIAYFA
PSIYGLPQAL TIHYLSYANK MIISVAVDPM IIDAHKLCDE LEESLKNMKL AILEKGLPNH
VN
