GDL83_ARATH
ID GDL83_ARATH Reviewed; 372 AA.
AC Q9FJ45; Q8LE77;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=GDSL esterase/lipase At5g45910;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase At5g45910;
DE Flags: Precursor;
GN OrderedLocusNames=At5g45910; ORFNames=K15I22.11;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM62801.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB016870; BAB09319.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95314.1; -; Genomic_DNA.
DR EMBL; AY085579; AAM62801.1; ALT_INIT; mRNA.
DR RefSeq; NP_199403.1; NM_123959.1.
DR AlphaFoldDB; Q9FJ45; -.
DR SMR; Q9FJ45; -.
DR STRING; 3702.AT5G45910.1; -.
DR PaxDb; Q9FJ45; -.
DR PRIDE; Q9FJ45; -.
DR ProteomicsDB; 221993; -.
DR EnsemblPlants; AT5G45910.1; AT5G45910.1; AT5G45910.
DR GeneID; 834631; -.
DR Gramene; AT5G45910.1; AT5G45910.1; AT5G45910.
DR KEGG; ath:AT5G45910; -.
DR Araport; AT5G45910; -.
DR TAIR; locus:2152385; AT5G45910.
DR eggNOG; ENOG502QU5U; Eukaryota.
DR HOGENOM; CLU_015101_2_1_1; -.
DR InParanoid; Q9FJ45; -.
DR OMA; STFANWD; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q9FJ45; -.
DR BioCyc; ARA:AT5G45910-MON; -.
DR PRO; PR:Q9FJ45; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ45; baseline and differential.
DR Genevisible; Q9FJ45; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..372
FT /note="GDSL esterase/lipase At5g45910"
FT /id="PRO_0000367423"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 345
FT /evidence="ECO:0000250"
FT ACT_SITE 348
FT /evidence="ECO:0000250"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 163
FT /note="Q -> R (in Ref. 3; AAM62801)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="G -> S (in Ref. 3; AAM62801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41534 MW; E583DCAB18014915 CRC64;
MRINMLFIVA FSFLVSVRSL PMRPTLKYES IFNFGDSLSD TGNFLLSGDV DSPNIGRLPY
GQTFFNRSTG RCSDGRLIID FIAEASGLPY IPPYLQSLRT NDSVDFKRGA NFAVAGATAN
EFSFFKNRGL SVTLLTNKTL DIQLDWFKKL KPSLCKTKPE CEQYFRKSLF LVGEIGGNDY
NYPLLAFRSF KHAMDLVPFV INKIMDVTSA LIEEGAMTLI VPGNLPIGCS AALLERFNDN
SGWLYDSRNQ CYMPLNNLAK LHNDKLKKGL AALRKKYPYA KIIYADYYSS AMQFFNSPSK
YGFTGSVLKA CCGGGDGRYN VQPNVRCGEK GSTTCEDPST YANWDGIHLT EAAYRHIATG
LISGRFTMPT YN
