WSD2_ARATH
ID WSD2_ARATH Reviewed; 479 AA.
AC Q9C7H4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 2 {ECO:0000303|PubMed:18621978};
DE Short=WS/DGAT 2 {ECO:0000303|PubMed:18621978};
DE AltName: Full=Diacylglycerol O-acyltransferase WSD2 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q93ZR6};
DE AltName: Full=Long-chain-alcohol O-fatty-acyltransferase WSD2 {ECO:0000303|PubMed:18621978};
DE EC=2.3.1.75 {ECO:0000250|UniProtKB:Q93ZR6};
GN Name=WSD2 {ECO:0000303|PubMed:18621978};
GN OrderedLocusNames=At1g72110 {ECO:0000312|Araport:AT1G72110};
GN ORFNames=F28P5.3 {ECO:0000312|EMBL:AAG51135.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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 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 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 -!- TISSUE SPECIFICITY: Mostly expressed in flowers and siliques and barely
CC in roots and stems. {ECO:0000269|PubMed:30729606}.
CC -!- INDUCTION: Up-regulated in the stem epidermis during active wax
CC synthesis. {ECO:0000269|PubMed:16299169}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the long-chain O-
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AC069273; AAG51135.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35274.1; -; Genomic_DNA.
DR EMBL; BT003906; AAO41954.1; -; mRNA.
DR EMBL; BT005032; AAO50565.1; -; mRNA.
DR PIR; D96744; D96744.
DR RefSeq; NP_177356.1; NM_105869.4.
DR AlphaFoldDB; Q9C7H4; -.
DR SMR; Q9C7H4; -.
DR STRING; 3702.AT1G72110.1; -.
DR PaxDb; Q9C7H4; -.
DR PRIDE; Q9C7H4; -.
DR ProteomicsDB; 177686; -.
DR EnsemblPlants; AT1G72110.1; AT1G72110.1; AT1G72110.
DR GeneID; 843542; -.
DR Gramene; AT1G72110.1; AT1G72110.1; AT1G72110.
DR KEGG; ath:AT1G72110; -.
DR Araport; AT1G72110; -.
DR TAIR; locus:2030332; AT1G72110.
DR eggNOG; ENOG502QTZ2; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR InParanoid; Q9C7H4; -.
DR OMA; KARHICW; -.
DR OrthoDB; 828506at2759; -.
DR PhylomeDB; Q9C7H4; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7H4; 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..479
FT /note="Wax ester synthase/diacylglycerol acyltransferase 2"
FT /id="PRO_0000452612"
FT TOPO_DOM 1..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..479
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 479 AA; 53545 MW; 573270CF2D58AF0E CRC64;
MAIERQVTEA EEPVSPFARL FSLPGLDVFN IVTIGCKTEG NASTIVEGIK NTLINHPRFS
SILVTGHGEH KGKARWIPTK INVEEHVIVP DIDPNIENPD EFLEDYTSNM ALSPMDMSKP
LWEFHLLKLK TSHAEAVTVA RFHHSLGDGM SLMSLLLACT RKTCDPEAFP TFVAPKKNKA
KNVCFSLVAW LWFIVRLMFH TCVEVIKSIV FICRASDTSA HIMGKPGATL SANKFIHRII
SLDDVKMVKN AMNMTVNDVL FGMVQAGLSR YLNQRYDLET SSKSRKNLHN IGLHGVVFFN
LRPNRNIEDL AKMMAKGSKC RWGNSIGYVL IPLGMKPQDD VFEYVRQAKT IMDGKKHSLE
PLFSYGLLKV TMEVFGLRGL KTLVKRIFGS TTMIFSNVVG PDEEISFFGH RIAYIAASTF
GVPQALNICI QSYVDKLIIN IGVDVDVIPD PHHLCDLIIE ALRMMNSAAP KKVFHASKV
