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GDSL esterase/lipase ESM1 (EC 3.1.1.-) (Extracellular lipase ESM1) (Protein EPITHIOSPECIFIER MODIFIER 1) (AtESM1)

 ESM1_ARATH              Reviewed;         392 AA.
Q9LJG3; A0MAV7; Q941A3;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 99.
RecName: Full=GDSL esterase/lipase ESM1;
EC=3.1.1.-;
AltName: Full=Extracellular lipase ESM1;
AltName: Full=Protein EPITHIOSPECIFIER MODIFIER 1;
Short=AtESM1;
Flags: Precursor;
Name=ESM1; OrderedLocusNames=At3g14210; ORFNames=MAG2.6;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, VARIANTS 8-ALA-GLY-9 AND
SER-389, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=16679459; DOI=10.1105/tpc.105.039602;
Zhang Z.-Y., Ober J.A., Kliebenstein D.J.;
"The gene controlling the quantitative trait locus EPITHIOSPECIFIER
MODIFIER1 alters glucosinolate hydrolysis and insect resistance in
Arabidopsis.";
Plant Cell 18:1524-1536(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[7]
REVIEW.
PubMed=15522763; DOI=10.1016/j.plipres.2004.09.002;
Akoh C.C., Lee G.-C., Liaw Y.-C., Huang T.-H., Shaw J.-F.;
"GDSL family of serine esterases/lipases.";
Prog. Lipid Res. 43:534-552(2004).
[8]
GENE FAMILY.
PubMed=18819574; DOI=10.3923/pjbs.2008.763.767;
Ling H.;
"Sequence analysis of GDSL lipase gene family in Arabidopsis
thaliana.";
Pak. J. Biol. Sci. 11:763-767(2008).
[9]
FUNCTION.
PubMed=17920088; DOI=10.1016/j.phytochem.2007.08.027;
Burow M., Zhang Z.-Y., Ober J.A., Lambrix V.M., Wittstock U.,
Gershenzon J., Kliebenstein D.J.;
"ESP and ESM1 mediate indol-3-acetonitrile production from indol-3-
ylmethyl glucosinolate in Arabidopsis.";
Phytochemistry 69:663-671(2008).
-!- FUNCTION: Represses or inhibits nitriles production from
methionine-derived and from indol-3-ylmethyl glucosinolates.
Favors isothiocyanate production. {ECO:0000269|PubMed:16679459,
ECO:0000269|PubMed:17920088}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: In cv. Columbia, altered ratio of endogenous
nitrile to isothiocyanate hydrolysis products.
{ECO:0000269|PubMed:16679459}.
-!- MISCELLANEOUS: ESM1 is highly expressed in cv. Columbia while
lowly expressed in cv. Landsberg erecta.
-!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
{ECO:0000305}.
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EMBL; DQ288725; ABB90255.1; -; Genomic_DNA.
EMBL; AP000600; BAB02989.1; -; Genomic_DNA.
EMBL; CP002686; AEE75487.1; -; Genomic_DNA.
EMBL; AY052318; AAK96511.1; -; mRNA.
EMBL; AY054230; AAL06890.1; -; mRNA.
EMBL; AY062690; AAL32768.1; -; mRNA.
EMBL; AY113066; AAM47374.1; -; mRNA.
EMBL; BT002522; AAO00882.1; -; mRNA.
EMBL; BT008484; AAP37843.1; -; mRNA.
EMBL; AK221834; BAD94063.1; -; mRNA.
PIR; PA0034; PA0034.
RefSeq; NP_188037.1; NM_112278.3.
UniGene; At.23866; -.
ProteinModelPortal; Q9LJG3; -.
BioGrid; 5973; 5.
IntAct; Q9LJG3; 1.
STRING; 3702.AT3G14210.1; -.
iPTMnet; Q9LJG3; -.
PaxDb; Q9LJG3; -.
PRIDE; Q9LJG3; -.
EnsemblPlants; AT3G14210.1; AT3G14210.1; AT3G14210.
GeneID; 820639; -.
Gramene; AT3G14210.1; AT3G14210.1; AT3G14210.
KEGG; ath:AT3G14210; -.
Araport; AT3G14210; -.
TAIR; locus:2087502; AT3G14210.
eggNOG; ENOG410JUR5; Eukaryota.
eggNOG; ENOG41106MS; LUCA.
HOGENOM; HOG000237649; -.
InParanoid; Q9LJG3; -.
OMA; MREYWEP; -.
OrthoDB; EOG09360DI2; -.
PhylomeDB; Q9LJG3; -.
PRO; PR:Q9LJG3; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LJG3; baseline and differential.
Genevisible; Q9LJG3; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0019762; P:glucosinolate catabolic process; IDA:TAIR.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009625; P:response to insect; IMP:TAIR.
CDD; cd01837; SGNH_plant_lipase_like; 1.
Gene3D; 3.40.50.1110; -; 1.
InterPro; IPR001087; GDSL.
InterPro; IPR036514; SGNH_hydro_sf.
InterPro; IPR035669; SGNH_plant_lipase_like.
Pfam; PF00657; Lipase_GDSL; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Hydrolase; Lipid degradation;
Lipid metabolism; Reference proteome; Secreted; Signal.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 392 GDSL esterase/lipase ESM1.
/FTId=PRO_0000367327.
ACT_SITE 43 43 Nucleophile. {ECO:0000250}.
ACT_SITE 324 324 {ECO:0000250}.
ACT_SITE 327 327 {ECO:0000250}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 8 9 VS -> AG (in strain: cv. Landsberg
erecta).
VARIANT 389 389 A -> S (in strain: cv. Landsberg erecta).
{ECO:0000269|PubMed:16679459}.
CONFLICT 271 271 A -> T (in Ref. 4; AAM47374/AAK96511).
{ECO:0000305}.
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


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