GDL12_ARATH
ID GDL12_ARATH Reviewed; 383 AA.
AC Q9FPE4; Q3E7H0; Q8GZ57; Q9SHP9; Q9SHQ1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=GDSL esterase/lipase At1g28660;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase At1g28660;
DE Flags: Precursor;
GN OrderedLocusNames=At1g28660; ORFNames=F1K23.13;
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FPE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FPE4-2; Sequence=VSP_036690;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24544.2; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 4 genes: At1g28640, At1g28650, At1g28660 and At1g28670.; Evidence={ECO:0000305};
CC Sequence=BAC41872.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC007508; AAF24544.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31010.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31011.1; -; Genomic_DNA.
DR EMBL; AK117196; BAC41872.1; ALT_SEQ; mRNA.
DR EMBL; AF327417; AAG42007.1; -; mRNA.
DR EMBL; BT001957; AAN71956.1; -; mRNA.
DR RefSeq; NP_564314.1; NM_102633.3. [Q9FPE4-1]
DR RefSeq; NP_849723.1; NM_179392.2. [Q9FPE4-2]
DR AlphaFoldDB; Q9FPE4; -.
DR SMR; Q9FPE4; -.
DR STRING; 3702.AT1G28660.1; -.
DR PaxDb; Q9FPE4; -.
DR PRIDE; Q9FPE4; -.
DR ProteomicsDB; 224748; -. [Q9FPE4-1]
DR EnsemblPlants; AT1G28660.1; AT1G28660.1; AT1G28660. [Q9FPE4-1]
DR EnsemblPlants; AT1G28660.2; AT1G28660.2; AT1G28660. [Q9FPE4-2]
DR GeneID; 839766; -.
DR Gramene; AT1G28660.1; AT1G28660.1; AT1G28660. [Q9FPE4-1]
DR Gramene; AT1G28660.2; AT1G28660.2; AT1G28660. [Q9FPE4-2]
DR KEGG; ath:AT1G28660; -.
DR Araport; AT1G28660; -.
DR TAIR; locus:2018703; AT1G28660.
DR eggNOG; ENOG502QSMM; Eukaryota.
DR OMA; NEECGYR; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q9FPE4; -.
DR BioCyc; ARA:AT1G28660-MON; -.
DR BRENDA; 3.1.1.49; 399.
DR PRO; PR:Q9FPE4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FPE4; baseline and differential.
DR Genevisible; Q9FPE4; 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 Alternative splicing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..383
FT /note="GDSL esterase/lipase At1g28660"
FT /id="PRO_0000367354"
FT ACT_SITE 42
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 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 210
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_036690"
SQ SEQUENCE 383 AA; 42034 MW; 9BE00FC81BFC47DA CRC64;
MASSLKKLIS SFLLVLYSTT IIVASSESRC RRFTSIISFG DSIADTGNIL HLSDVNHLPQ
TAFFPYGESF FHPPSGRASD GRLIIDFIAE FLGLPYVPPY FGSQNVSFEQ GINFAVYGAT
ALDRAYFVAK GIESDFTNVS LGVQLDIFKQ ILPNLCASSS RDCREMLGDS LILMGEIGGN
DFFYPSSEGK SINETKLQDL IIKAISSAIV DLIALGGKTF LVPGGFPAGC SAACLTQYQN
ATEEDYDPLT GCIPRLNELG EHDNEQLKTE LKRLQKLYPD VNIIYADYHN SLYRFYQEPA
KYGFKNKPLA ACCGVGGKYN FTIGKECGYE GVSYCQNPSE YVNWDGYHLT EAAYQKMAEG
ILNGPYATPA FDWSCLGSGT VDT
