ID D7KYW7_ARALL Unreviewed; 384 AA.
AC D7KYW7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=GDSL-motif lipase/hydrolase family protein {ECO:0000313|EMBL:EFH65099.1};
GN ORFNames=ARALYDRAFT_476288 {ECO:0000313|EMBL:EFH65099.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00008668}.
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DR EMBL; GL348714; EFH65099.1; -; Genomic_DNA.
DR RefSeq; XP_002888840.1; XM_002888794.1.
DR AlphaFoldDB; D7KYW7; -.
DR STRING; 81972.D7KYW7; -.
DR EnsemblPlants; fgenesh2_kg.2__1418__AT1G71691.2; fgenesh2_kg.2__1418__AT1G71691.2; fgenesh2_kg.2__1418__AT1G71691.2.
DR Gramene; fgenesh2_kg.2__1418__AT1G71691.2; fgenesh2_kg.2__1418__AT1G71691.2; fgenesh2_kg.2__1418__AT1G71691.2.
DR eggNOG; ENOG502QUVY; Eukaryota.
DR HOGENOM; CLU_015101_0_0_1; -.
DR OrthoDB; 1012174at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
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; SGNH hydrolase; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR PANTHER; PTHR45650; GDSL-LIKE LIPASE/ACYLHYDROLASE-RELATED; 1.
DR PANTHER; PTHR45650:SF22; OS05G0419800 PROTEIN; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EFH65099.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..384
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003101672"
SQ SEQUENCE 384 AA; 41675 MW; B9B2F5B9748F07A9 CRC64;
MAFHFPRLCF FSALLVVVLH LLHGVSGQLV EVEEPISAPP PPLVDLNSGD GIVPALFVFG
DSLIDNGNNN NIPSFAKANY FPYGIDFNGG PTGRFCNGLT MVDGIAQLLG LPLIPAYSEA
TGDQVLRGVN YASAAAGILP DTGGNFVGRI PFDQQIHNFE TTLDQVASKS GGAVAIADSV
TRSLFFIGMG SNDYLNNYLM PNFPTRNQYN SQQFGDLLVQ HYTNQLTRLY NLGGRKFVVA
GLGRMGCIPS ILAQGNDGKC SEEVNQLVLP FNTNVKTMIS NLNQNLPAAK FIYLDIAHMF
EDIVANQAAY GLTTMDKGCC GIGKNRGQIT CLPFETPCPN RDQYVFWDAF HPTEKVNLIM
AKKAFAGDRT VAYPINIQEL ASLN
//
