GDL18_ARATH
ID GDL18_ARATH Reviewed; 391 AA.
AC Q1H583; Q8LB78; Q9SYF6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=GDSL esterase/lipase 22;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase At1g54000;
DE AltName: Full=GDSL esterase/lipase At1g54000;
DE Flags: Precursor;
GN Name=GLL22; OrderedLocusNames=At1g54000; ORFNames=F15I1.8;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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).
RN [7]
RP IDENTIFICATION IN THE PYK10 COMPLEX.
RX PubMed=18467340; DOI=10.1093/pcp/pcn075;
RA Nagano A.J., Fukao Y., Fujiwara M., Nishimura M., Hara-Nishimura I.;
RT "Antagonistic jacalin-related lectins regulate the size of ER body-type
RT beta-glucosidase complexes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:969-980(2008).
CC -!- SUBUNIT: Component of the PYK10 complex, at least composed of
CC PYK10/BGLU23, BGLU21, BGLU22, JAL22, JAL23, PBP1/JAL30, PBP2/JAL31,
CC JAL32, JAL33, JAL34, JAL35, GLL22 and GLL23.
CC {ECO:0000269|PubMed:18467340}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25772.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM64922.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006577; AAD25772.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33033.1; -; Genomic_DNA.
DR EMBL; BT025581; ABF58999.1; -; mRNA.
DR EMBL; AY087372; AAM64922.1; ALT_INIT; mRNA.
DR PIR; E96580; E96580.
DR RefSeq; NP_175802.1; NM_104277.4.
DR AlphaFoldDB; Q1H583; -.
DR SMR; Q1H583; -.
DR BioGRID; 27063; 2.
DR IntAct; Q1H583; 1.
DR STRING; 3702.AT1G54000.1; -.
DR MetOSite; Q1H583; -.
DR SwissPalm; Q1H583; -.
DR PaxDb; Q1H583; -.
DR PRIDE; Q1H583; -.
DR ProteomicsDB; 247085; -.
DR EnsemblPlants; AT1G54000.1; AT1G54000.1; AT1G54000.
DR GeneID; 841838; -.
DR Gramene; AT1G54000.1; AT1G54000.1; AT1G54000.
DR KEGG; ath:AT1G54000; -.
DR Araport; AT1G54000; -.
DR TAIR; locus:2014370; AT1G54000.
DR eggNOG; ENOG502S4IX; Eukaryota.
DR HOGENOM; CLU_015101_7_0_1; -.
DR InParanoid; Q1H583; -.
DR OMA; MMANNCN; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q1H583; -.
DR BioCyc; ARA:AT1G54000-MON; -.
DR PRO; PR:Q1H583; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q1H583; baseline and differential.
DR Genevisible; Q1H583; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
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 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..391
FT /note="GDSL esterase/lipase 22"
FT /id="PRO_0000367360"
FT REGION 372..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 322
FT /evidence="ECO:0000250"
FT ACT_SITE 325
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 15
FT /note="I -> F (in Ref. 4; AAM64922)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="N -> S (in Ref. 4; AAM64922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 43194 MW; 01F562BAE8F5A467 CRC64;
MMANNCNLVS VLCVILVLTL FHNPITVAGQ NSPVVALFTF GDSNFDAGNK QTLTKTLVAQ
GFWPYGKSRD DPNGKFSDGL ITPDFLAKFM KIPLAIAPAL QPNVNVSRGA SFAVEGATLL
GAPVESMTLN QQVKKFNQMK AANWNDDFVA KSVFMIYIGA NDYLNFTKNN PTADASAQQA
FVTSVTNKLK NDISALYSSG ASKFVIQTLA PLGCLPIVRQ EYNTGMDQCY EKLNDLAKQH
NEKIGPMLNE MARNSPASAP FQFTVFDFYN AVLTRTQRNQ NFRFFVTNAS CCGVGSHDAY
GCGLPNVHSK LCEYQRSFLF FDGRHNSEKA QEMFAHLLFG ADTNVVQPMN VRELTVYPVD
EPMREFWVPP TPATVHASDS SSSTSRGYEY Y
