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WSD10_ARATH
ID   WSD10_ARATH             Reviewed;         483 AA.
AC   Q9FK04; F4KJ46;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 10 {ECO:0000303|PubMed:18621978};
DE            Short=WS/DGAT 10 {ECO:0000303|PubMed:18621978};
DE   AltName: Full=Diacylglycerol O-acyltransferase WSD10 {ECO:0000303|PubMed:18621978};
DE            EC=2.3.1.20 {ECO:0000250|UniProtKB:Q93ZR6};
DE   AltName: Full=Long-chain-alcohol O-fatty-acyltransferase WSD10 {ECO:0000303|PubMed:18621978};
DE            EC=2.3.1.75 {ECO:0000250|UniProtKB:Q93ZR6};
GN   Name=WSD10 {ECO:0000303|PubMed:18621978};
GN   OrderedLocusNames=At5g53380 {ECO:0000312|Araport:AT5G53380};
GN   ORFNames=K19E1.18 {ECO:0000312|EMBL:BAB09800.1};
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}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots.
CC       {ECO:0000269|PubMed:30729606}.
CC   -!- INDUCTION: Induced in roots during drought and salt stresses.
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=AED96346.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB013388; BAB09800.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96346.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_001318794.1; NM_001345053.1.
DR   AlphaFoldDB; Q9FK04; -.
DR   SMR; Q9FK04; -.
DR   STRING; 3702.AT5G53380.1; -.
DR   PaxDb; Q9FK04; -.
DR   PRIDE; Q9FK04; -.
DR   EnsemblPlants; AT5G53380.1; AT5G53380.1; AT5G53380.
DR   GeneID; 835419; -.
DR   Gramene; AT5G53380.1; AT5G53380.1; AT5G53380.
DR   KEGG; ath:AT5G53380; -.
DR   Araport; AT5G53380; -.
DR   TAIR; locus:2154282; AT5G53380.
DR   eggNOG; ENOG502QU8B; Eukaryota.
DR   HOGENOM; CLU_027831_0_0_1; -.
DR   InParanoid; Q9FK04; -.
DR   OrthoDB; 828506at2759; -.
DR   PhylomeDB; Q9FK04; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FK04; 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0102966; F:arachidoyl-CoA:1-dodecanol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
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; Stress response; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..483
FT                   /note="Wax ester synthase/diacylglycerol acyltransferase
FT                   10"
FT                   /id="PRO_0000452620"
FT   TOPO_DOM        1..203
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..483
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        399
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   483 AA;  54280 MW;  ABF87FCD42C9CB59 CRC64;
     MTKEEVEEEP LSPMARLFQS PGIENCIITM IGFKAKINPD IILDDLKHNV SKHPRFCSKL
     VIATHTNYDG ERWMKTKVNV EDHVFVPDID LQEINKDGDG FVDDYVSRLT LSPLDKSKPL
     WDIHILNVKT SDAEAVGVMR CHHSLADGMS LMSLLVACTR KTSNLESFPT IPAIKRREQM
     MSHRFGNKGW YSRSINAVYY AVRLIWNTIV DLLLLWATSL FFKDTETPIS EGIGSGNNAR
     RFYHRTVSLD DIKLIKNAMK MTINDVLLGV TQDALSRYLN QRYGDKNGEG VTTTSNLNNL
     PGKIRIRAGV AVNLRQDIGI QPLEDMLAKD SKCRWGNYDS LVFVPFSISL ETDPLVPLLK
     AKSIMDRKKH SLVAPMHYSI IEFIINTFGT KVFNRTCSNT TTILSNIVGP VEEVSLHGNC
     ITYIALTGYG HSQALMIHFI SYANKMIITI AVDPAVIPDP HNICDEMEKS LKAMKDTLSG
     KSD
 
 
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