GDL49_ARATH
ID GDL49_ARATH Reviewed; 379 AA.
AC Q9MAA1; Q8H143; Q8LE24;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=GDSL esterase/lipase At3g05180;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase At3g05180;
DE Flags: Precursor;
GN OrderedLocusNames=At3g05180; ORFNames=T12H1.15;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AC009177; AAF27024.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74201.1; -; Genomic_DNA.
DR EMBL; AY056157; AAL07236.1; -; mRNA.
DR EMBL; BT000788; AAN31927.1; -; mRNA.
DR EMBL; AY085661; AAM62882.1; -; mRNA.
DR RefSeq; NP_187169.1; NM_111391.4.
DR AlphaFoldDB; Q9MAA1; -.
DR PaxDb; Q9MAA1; -.
DR PRIDE; Q9MAA1; -.
DR ProteomicsDB; 247097; -.
DR EnsemblPlants; AT3G05180.1; AT3G05180.1; AT3G05180.
DR GeneID; 819682; -.
DR Gramene; AT3G05180.1; AT3G05180.1; AT3G05180.
DR KEGG; ath:AT3G05180; -.
DR Araport; AT3G05180; -.
DR TAIR; locus:2096269; AT3G05180.
DR eggNOG; ENOG502QRTJ; Eukaryota.
DR HOGENOM; CLU_015101_2_0_1; -.
DR InParanoid; Q9MAA1; -.
DR OMA; GARNYWI; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q9MAA1; -.
DR BioCyc; ARA:AT3G05180-MON; -.
DR PRO; PR:Q9MAA1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MAA1; baseline and differential.
DR Genevisible; Q9MAA1; AT.
DR GO; GO:0048046; C:apoplast; 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 GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..379
FT /note="GDSL esterase/lipase At3g05180"
FT /id="PRO_0000367390"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /evidence="ECO:0000250"
FT ACT_SITE 352
FT /evidence="ECO:0000250"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 189
FT /note="V -> L (in Ref. 4; AAM62882)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="E -> K (in Ref. 4; AAM62882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42344 MW; EBEB2D05C75F6AD2 CRC64;
METLFHTLLR LLLFVAISHT LSPLAGSFRI SNDFPAVFNF GDSNSDTGEL SSGLGFLPQP
SYEITFFRSP TSGRFCNGRL IVDFLMEAID RPYLRPYLDS ISRQTYRRGC NFAAAASTIQ
KANAASYSPF GFGVQVSQFI TFKSKVLQLI QQDEELQRYL PSEYFFSNGL YMFDIGQNDI
AGAFYTKTVD QVLALVPIIL DIFQDGIKRL YAEGARNYWI HNTGPLGCLA QVVSIFGEDK
SKLDEFGCVS DHNQAAKLFN LQLHGLFKKL PQQYPNSRFT YVDIFSIKSD LILNHSKYGF
DHSIMVCCGT GGPPLNYDDQ VGCGKTARSN GTIITAKPCY DSSKYVNWDG IHYTEAANRF
VALHILTGKY SETASSLNL
