ID   LTL1_ARATH              Reviewed;         366 AA.
AC   Q9M8Y5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=GDSL esterase/lipase LTL1;
DE            EC=3.1.1.-;
DE   AltName: Full=Extracellular lipase LTL1;
DE   AltName: Full=Lithium-tolerant lipase 1;
DE            Short=AtLTL1;
DE            Short=Li-tolerant lipase 1;
DE   Flags: Precursor;
GN   Name=LTL1; OrderedLocusNames=At3g04290; ORFNames=T6K12.9;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY HIGH SALINITY AND SA.
RX   PubMed=16930315; DOI=10.1111/j.1365-3040.2006.01565.x;
RA   Naranjo M.A., Forment J., Roldan M., Serrano R., Vicente O.;
RT   "Overexpression of Arabidopsis thaliana LTL1, a salt-induced gene encoding
RT   a GDSL-motif lipase, increases salt tolerance in yeast and transgenic
RT   plants.";
RL   Plant Cell Environ. 29:1890-1900(2006).
RN   [6]
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).
CC   -!- FUNCTION: Involved in the mechanisms of salt tolerance. Mediates
CC       resistance to LiCl and NaCl. {ECO:0000269|PubMed:16930315}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in flowers, reproductive stems and
CC       rosette leaves, and, to a lower extent, in roots.
CC       {ECO:0000269|PubMed:16930315}.
CC   -!- INDUCTION: By high salinity (LiCl and NaCl). Also induced transiently
CC       by salicylic acid (SA). {ECO:0000269|PubMed:16930315}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC016829; AAF26785.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74063.1; -; Genomic_DNA.
DR   EMBL; AY085128; AAM61681.1; -; mRNA.
DR   RefSeq; NP_187079.1; NM_111300.4.
DR   AlphaFoldDB; Q9M8Y5; -.
DR   SMR; Q9M8Y5; -.
DR   STRING; 3702.AT3G04290.1; -.
DR   PaxDb; Q9M8Y5; -.
DR   PRIDE; Q9M8Y5; -.
DR   ProteomicsDB; 238505; -.
DR   EnsemblPlants; AT3G04290.1; AT3G04290.1; AT3G04290.
DR   GeneID; 819584; -.
DR   Gramene; AT3G04290.1; AT3G04290.1; AT3G04290.
DR   KEGG; ath:AT3G04290; -.
DR   Araport; AT3G04290; -.
DR   TAIR; locus:2103005; AT3G04290.
DR   eggNOG; ENOG502QQP0; Eukaryota.
DR   HOGENOM; CLU_015101_0_0_1; -.
DR   InParanoid; Q9M8Y5; -.
DR   OMA; ANAYEMH; -.
DR   OrthoDB; 704138at2759; -.
DR   PhylomeDB; Q9M8Y5; -.
DR   BioCyc; ARA:AT3G04290-MON; -.
DR   PRO; PR:Q9M8Y5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M8Y5; baseline and differential.
DR   Genevisible; Q9M8Y5; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0042538; P:hyperosmotic salinity response; IMP:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010226; P:response to lithium ion; IMP:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IDA:UniProtKB.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..366
FT                   /note="GDSL esterase/lipase LTL1"
FT                   /id="PRO_0000367342"
FT   ACT_SITE        36
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   366 AA;  40149 MW;  BCD0CEAB614BD4E7 CRC64;
     MNINCSPLGF LISLFFIVTF LAPQVKSRAF FVFGDSLVDN GNNDYLVTTA RADNYPYGID
     YPTRRPTGRF SNGLNIPDII SEAIGMPSTL PYLSPHLTGE NLLVGANFAS AGIGILNDTG
     IQFVNIIRIS KQMEYFEQYQ LRVSALIGPE ATQQLVNQAL VLITLGGNDF VNNYYLIPFS
     ARSRQYALPD YVVYLISEYG KILRKLYELG ARRVLVTGTG AMGCAPAELA QHSRNGECYG
     ALQTAAALFN PQLVDLIASV NAEIGQDVFV AANAYQMNMD YLSNPEQFGF VTSKVACCGQ
     GPYNGIGLCT PVSNLCPNRD LYAFWDAFHP TEKANRIIVN QILTGSSKYM HPMNLSTAML
     LDSSKI