GDL71_ARATH
ID GDL71_ARATH Reviewed; 359 AA.
AC Q9LZS7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=GDSL esterase/lipase At5g03610;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase At5g03610;
DE Flags: Precursor;
GN OrderedLocusNames=At5g03610; ORFNames=F17C15.30;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 [5]
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 [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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL162506; CAB82926.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90633.1; -; Genomic_DNA.
DR EMBL; AF360329; AAK26039.1; -; mRNA.
DR EMBL; AY085113; AAM61667.1; -; mRNA.
DR PIR; T48388; T48388.
DR RefSeq; NP_195981.1; NM_120442.4.
DR AlphaFoldDB; Q9LZS7; -.
DR SMR; Q9LZS7; -.
DR IntAct; Q9LZS7; 1.
DR STRING; 3702.AT5G03610.1; -.
DR PaxDb; Q9LZS7; -.
DR PRIDE; Q9LZS7; -.
DR ProteomicsDB; 221987; -.
DR EnsemblPlants; AT5G03610.1; AT5G03610.1; AT5G03610.
DR GeneID; 831778; -.
DR Gramene; AT5G03610.1; AT5G03610.1; AT5G03610.
DR KEGG; ath:AT5G03610; -.
DR Araport; AT5G03610; -.
DR TAIR; locus:2144558; AT5G03610.
DR eggNOG; ENOG502QU3Y; Eukaryota.
DR HOGENOM; CLU_015101_12_0_1; -.
DR InParanoid; Q9LZS7; -.
DR OMA; IPYRWRN; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q9LZS7; -.
DR BioCyc; ARA:AT5G03610-MON; -.
DR PRO; PR:Q9LZS7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZS7; baseline and differential.
DR Genevisible; Q9LZS7; 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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..359
FT /note="GDSL esterase/lipase At5g03610"
FT /id="PRO_0000367411"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 332
FT /evidence="ECO:0000250"
FT ACT_SITE 335
FT /evidence="ECO:0000250"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 359 AA; 40106 MW; DC11EFA10828FD5B CRC64;
MDSLIKLFFC LFIFLCTSLL FGEINGVEGS NQNHHLYPFR PTKLFVFGDS YADTGNIKKA
FSSSWKFPYG ITFPGKPAGR FSDGRVATDF LAKFVGIKSP IPYFWKDYAG KKRLQYGMNF
AYGGTGVFNT QTPLPNMTTQ IDIFQNILTT GDIYYPPELT SSVALVSVAG NDYSNFIALN
RPASEFPAFI KQVVDQTEVN LRRIHALGVK KIAVPSLQPL GCLPPFTFVT SFQRCNETQN
ALVNLHNNLL QQVVAKLNNE TKQSTFIILD LYNAFLTVFK NKGSNPGSTR FESPLKPCCV
GVSREYNCGS VDEKGVKKYI VCDNPKTAFF WDGLHPTEEG WRSVYSVLRE SLTASLIKA
