ID GDL53_ARATH Reviewed; 380 AA.
AC Q9LIN2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=GDSL esterase/lipase At3g26430 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:23430565};
DE AltName: Full=Extracellular lipase At3g26430 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At3g26430 {ECO:0000312|Araport:AT3G26430};
GN ORFNames=F20C19.19 {ECO:0000312|EMBL:BAB02204.1};
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=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 [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 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 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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=23430565; DOI=10.1007/s11103-013-0021-8;
RA Muralidharan M., Buss K., Larrimore K.E., Segerson N.A., Kannan L.,
RA Mor T.S.;
RT "The Arabidopsis thaliana ortholog of a purported maize cholinesterase gene
RT encodes a GDSL-lipase.";
RL Plant Mol. Biol. 81:565-576(2013).
CC -!- FUNCTION: Lipase that can hydrolyze p-nitrophenyl butyrate and p-
CC nitrophenyl palmitate in vitro (PubMed:23430565). Possesses low
CC activity against p-nitrophenyl acetate (PubMed:23430565). Substrate
CC preference is p-nitrophenyl palmitate > p-nitrophenyl butyrate >> p-
CC nitrophenyl acetate (PubMed:23430565). Lacks cholinesterase activity
CC (PubMed:23430565). {ECO:0000269|PubMed:23430565}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:23430565};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393;
CC Evidence={ECO:0000269|PubMed:23430565};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:23430565};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:23430565};
CC -!- ACTIVITY REGULATION: Lipase activity is inhibited by
CC phenylmethylsulfonyl fluoride (PMSF), but not neostigmine bromide (NB).
CC {ECO:0000269|PubMed:23430565}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:23430565};
CC KM=2.0 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:23430565};
CC KM=1.2 mM for p-nitrophenyl palmitate {ECO:0000269|PubMed:23430565};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AP001298; BAB02204.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77155.1; -; Genomic_DNA.
DR EMBL; AY062535; AAL32613.1; -; mRNA.
DR EMBL; AY093315; AAM13314.1; -; mRNA.
DR RefSeq; NP_189274.1; NM_113550.3.
DR AlphaFoldDB; Q9LIN2; -.
DR SMR; Q9LIN2; -.
DR STRING; 3702.Q9LIN2; -.
DR SwissLipids; SLP:000001881; -.
DR PaxDb; 3702-AT3G26430-1; -.
DR ProteomicsDB; 247098; -.
DR EnsemblPlants; AT3G26430.1; AT3G26430.1; AT3G26430.
DR GeneID; 822247; -.
DR Gramene; AT3G26430.1; AT3G26430.1; AT3G26430.
DR KEGG; ath:AT3G26430; -.
DR Araport; AT3G26430; -.
DR TAIR; AT3G26430; -.
DR eggNOG; ENOG502QQGV; Eukaryota.
DR HOGENOM; CLU_015101_2_0_1; -.
DR InParanoid; Q9LIN2; -.
DR OMA; ANKWIFQ; -.
DR OrthoDB; 1201565at2759; -.
DR PhylomeDB; Q9LIN2; -.
DR BioCyc; ARA:AT3G26430-MONOMER; -.
DR PRO; PR:Q9LIN2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIN2; baseline and differential.
DR Genevisible; Q9LIN2; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IDA:TAIR.
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; SGNH hydrolase; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR PANTHER; PTHR22835:SF117; GDSL-LIKE LIPASE_ACYLHYDROLASE; 1.
DR PANTHER; PTHR22835; ZINC FINGER FYVE DOMAIN CONTAINING PROTEIN; 1.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..380
FT /note="GDSL esterase/lipase At3g26430"
FT /id="PRO_0000367394"
FT ACT_SITE 38
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0ADA1"
FT ACT_SITE 346
FT /evidence="ECO:0000250|UniProtKB:P0ADA1"
FT ACT_SITE 349
FT /evidence="ECO:0000250|UniProtKB:P0ADA1"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 380 AA; 42062 MW; 21807167FB18D019 CRC64;
METNLLLVKC VLLASCLIHP RACSPSCNFP AIFNFGDSNS DTGGLSASFG QAPYPNGQTF
FHSPSGRFSD GRLIIDFIAE ELGLPYLNAF LDSIGSNFSH GANFATAGST VRPPNATIAQ
SGVSPISLDV QLVQFSDFIT RSQLIRNRGG VFKKLLPKKE YFSQALYTFD IGQNDLTAGL
KLNMTSDQIK AYIPDVHDQL SNVIRKVYSK GGRRFWIHNT APLGCLPYVL DRFPVPASQI
DNHGCAIPRN EIARYYNSEL KRRVIELRKE LSEAAFTYVD IYSIKLTLIT QAKKLGFRYP
LVACCGHGGK YNFNKLIKCG AKVMIKGKEI VLAKSCNDVS FRVSWDGIHF TETTNSWIFQ
QINDGAFSDP PLPVKSACTR
//
