ESM1_ARATH
ID ESM1_ARATH Reviewed; 392 AA.
AC Q9LJG3; A0MAV7; Q941A3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=GDSL esterase/lipase ESM1;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase ESM1;
DE AltName: Full=Protein EPITHIOSPECIFIER MODIFIER 1;
DE Short=AtESM1;
DE Flags: Precursor;
GN Name=ESM1; OrderedLocusNames=At3g14210; ORFNames=MAG2.6;
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 [GENOMIC DNA], FUNCTION, VARIANTS 8-ALA-GLY-9 AND
RP SER-389, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=16679459; DOI=10.1105/tpc.105.039602;
RA Zhang Z.-Y., Ober J.A., Kliebenstein D.J.;
RT "The gene controlling the quantitative trait locus EPITHIOSPECIFIER
RT MODIFIER1 alters glucosinolate hydrolysis and insect resistance in
RT Arabidopsis.";
RL Plant Cell 18:1524-1536(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [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].
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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [7]
RP REVIEW.
RX PubMed=15522763; DOI=10.1016/j.plipres.2004.09.002;
RA Akoh C.C., Lee G.-C., Liaw Y.-C., Huang T.-H., Shaw J.-F.;
RT "GDSL family of serine esterases/lipases.";
RL Prog. Lipid Res. 43:534-552(2004).
RN [8]
RP GENE FAMILY.
RX PubMed=18819574; DOI=10.3923/pjbs.2008.763.767;
RA Ling H.;
RT "Sequence analysis of GDSL lipase gene family in Arabidopsis thaliana.";
RL Pak. J. Biol. Sci. 11:763-767(2008).
RN [9]
RP FUNCTION.
RX PubMed=17920088; DOI=10.1016/j.phytochem.2007.08.027;
RA Burow M., Zhang Z.-Y., Ober J.A., Lambrix V.M., Wittstock U.,
RA Gershenzon J., Kliebenstein D.J.;
RT "ESP and ESM1 mediate indol-3-acetonitrile production from indol-3-ylmethyl
RT glucosinolate in Arabidopsis.";
RL Phytochemistry 69:663-671(2008).
CC -!- FUNCTION: Represses or inhibits nitriles production from methionine-
CC derived and from indol-3-ylmethyl glucosinolates. Favors isothiocyanate
CC production. {ECO:0000269|PubMed:16679459, ECO:0000269|PubMed:17920088}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: In cv. Columbia, altered ratio of endogenous
CC nitrile to isothiocyanate hydrolysis products.
CC {ECO:0000269|PubMed:16679459}.
CC -!- MISCELLANEOUS: ESM1 is highly expressed in cv. Columbia while lowly
CC expressed in cv. Landsberg erecta.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; DQ288725; ABB90255.1; -; Genomic_DNA.
DR EMBL; AP000600; BAB02989.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75487.1; -; Genomic_DNA.
DR EMBL; AY052318; AAK96511.1; -; mRNA.
DR EMBL; AY054230; AAL06890.1; -; mRNA.
DR EMBL; AY062690; AAL32768.1; -; mRNA.
DR EMBL; AY113066; AAM47374.1; -; mRNA.
DR EMBL; BT002522; AAO00882.1; -; mRNA.
DR EMBL; BT008484; AAP37843.1; -; mRNA.
DR EMBL; AK221834; BAD94063.1; -; mRNA.
DR PIR; PA0034; PA0034.
DR RefSeq; NP_188037.1; NM_112278.3.
DR AlphaFoldDB; Q9LJG3; -.
DR SMR; Q9LJG3; -.
DR BioGRID; 5973; 5.
DR IntAct; Q9LJG3; 1.
DR STRING; 3702.AT3G14210.1; -.
DR iPTMnet; Q9LJG3; -.
DR MetOSite; Q9LJG3; -.
DR PaxDb; Q9LJG3; -.
DR PRIDE; Q9LJG3; -.
DR ProteomicsDB; 222291; -.
DR EnsemblPlants; AT3G14210.1; AT3G14210.1; AT3G14210.
DR GeneID; 820639; -.
DR Gramene; AT3G14210.1; AT3G14210.1; AT3G14210.
DR KEGG; ath:AT3G14210; -.
DR Araport; AT3G14210; -.
DR TAIR; locus:2087502; AT3G14210.
DR eggNOG; ENOG502S4IX; Eukaryota.
DR HOGENOM; CLU_015101_7_0_1; -.
DR InParanoid; Q9LJG3; -.
DR OMA; YDAGNKV; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q9LJG3; -.
DR PRO; PR:Q9LJG3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJG3; baseline and differential.
DR Genevisible; Q9LJG3; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0019762; P:glucosinolate catabolic process; IDA:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009625; P:response to insect; IMP:TAIR.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR Pfam; PF00657; Lipase_GDSL; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..392
FT /note="GDSL esterase/lipase ESM1"
FT /id="PRO_0000367327"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 324
FT /evidence="ECO:0000250"
FT ACT_SITE 327
FT /evidence="ECO:0000250"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 8..9
FT /note="VS -> AG (in strain: cv. Landsberg erecta)"
FT VARIANT 389
FT /note="A -> S (in strain: cv. Landsberg erecta)"
FT /evidence="ECO:0000269|PubMed:16679459"
FT CONFLICT 271
FT /note="A -> T (in Ref. 4; AAM47374/AAK96511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 44060 MW; E49F3AF0EC586E72 CRC64;
MADNLNLVSV LGVLLVLTIF HNPIIVYAGE GVPNVALFTF GDSYYDAGNK VFLSQRKDLP
QTYWPYGKSR DYPNGKFSDG HIVPDFIADF ISIPNGVLPP VLKPGVDISR GVSFAVADAS
ILGAPVESMT LNQQVVKFKN MKSNWNDSYI EKSLFMIYIG TEDYLNFTKA NPNADASAQQ
AFVTNVINRL KNDIKLLYSL GASKFVVQLL APLGCLPIVR QEYKTGNECY ELLNDLAKQH
NGKIGPMLNE FAKISTSPYG FQFTVFDFYN AVLRRIATGR SLNYRFFVTN TSCCGVGTHN
AYGCGKGNVH SKLCEYQRSY FFFDGRHNTE KAQEEMAHLL YGADPDVVQP MTVRELIVYP
TGETMREYWE PNNLAIRRRP SRDFYLGLAA YY
