ID   GDL81_ARATH             Reviewed;         369 AA.
AC   Q9FJ25; F4JZZ2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=GDSL esterase/lipase At5g41890;
DE            EC=3.1.1.-;
GN   OrderedLocusNames=At5g41890; ORFNames=K16L22.18;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(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   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   [4]
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FJ25-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FJ25-2; Sequence=VSP_042247;
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; AB016871; BAB10664.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94740.1; -; Genomic_DNA.
DR   RefSeq; NP_199004.2; NM_123554.3. [Q9FJ25-2]
DR   AlphaFoldDB; Q9FJ25; -.
DR   SMR; Q9FJ25; -.
DR   STRING; 3702.AT5G41890.1; -.
DR   PaxDb; Q9FJ25; -.
DR   PRIDE; Q9FJ25; -.
DR   ProteomicsDB; 221991; -. [Q9FJ25-1]
DR   EnsemblPlants; AT5G41890.1; AT5G41890.1; AT5G41890. [Q9FJ25-2]
DR   GeneID; 834194; -.
DR   Gramene; AT5G41890.1; AT5G41890.1; AT5G41890. [Q9FJ25-2]
DR   KEGG; ath:AT5G41890; -.
DR   Araport; AT5G41890; -.
DR   TAIR; locus:2153000; AT5G41890.
DR   eggNOG; ENOG502QR7P; Eukaryota.
DR   HOGENOM; CLU_015101_0_0_1; -.
DR   InParanoid; Q9FJ25; -.
DR   OMA; PSVFQDS; -.
DR   OrthoDB; 704138at2759; -.
DR   PhylomeDB; Q9FJ25; -.
DR   BioCyc; ARA:AT5G41890-MON; -.
DR   PRO; PR:Q9FJ25; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJ25; baseline and differential.
DR   Genevisible; Q9FJ25; AT.
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   3: Inferred from homology;
KW   Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..369
FT                   /note="GDSL esterase/lipase At5g41890"
FT                   /id="PRO_0000367421"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        334
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        337
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..19
FT                   /note="MCTQDETIFVLHDQQSNNS -> MDFTYRCSLKPFNCTFLLLWLSHFQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042247"
SQ   SEQUENCE   369 AA;  40742 MW;  6B1A21B319CDB20A CRC64;
     MCTQDETIFV LHDQQSNNSA AQSFTNFIFG DSLVDVGNNN YIFTLSKADS SPYGIDFAPS
     NGQPTGRFTN GRTISDIVGE ALGAKSPPPP YLEPNTEANT IRNGINYASG AAGILDDTGL
     LFIGRVPLRE QVSNFEKSRE YMVRVIGENG TKEMLKNAMF TITIGSNDIL NYIQPSIPFF
     SQDKLPTDVL QDSMVLHLTT HLKRLHQLGG RKFVVVGVGP LGCIPFARAL NLIPAGKCSE
     QVNQVVRGYN MKLIHSLKTL NNELRSEDYN TTFVYANSYD LFLKLVLNYQ LFGLKNADKP
     CCGGYFPPFA CFKGPNQNSS QAACEDRSKF VFWDAYHPTE AANLIVAKAL LDGDQTVATP
     FNIRYLNDL