GDL7_ARATH
ID GDL7_ARATH Reviewed; 390 AA.
AC Q9FXJ2; Q3ED51;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=GDSL esterase/lipase At1g28580;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase At1g28580;
DE Flags: Precursor;
GN OrderedLocusNames=At1g28580; ORFNames=F1K23.18;
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=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 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 [4]
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 [5]
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=Q9FXJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FXJ2-2; Sequence=VSP_036687;
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AC007508; AAG22836.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30996.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30997.1; -; Genomic_DNA.
DR EMBL; AF361608; AAK32776.1; -; mRNA.
DR EMBL; AY045814; AAK76488.1; -; mRNA.
DR EMBL; AY074841; AAL69539.1; -; mRNA.
DR EMBL; AY079395; AAL85126.1; -; mRNA.
DR PIR; E86411; E86411.
DR RefSeq; NP_174180.1; NM_102626.4. [Q9FXJ2-1]
DR RefSeq; NP_973931.1; NM_202202.2. [Q9FXJ2-2]
DR AlphaFoldDB; Q9FXJ2; -.
DR SMR; Q9FXJ2; -.
DR STRING; 3702.AT1G28580.1; -.
DR iPTMnet; Q9FXJ2; -.
DR PaxDb; Q9FXJ2; -.
DR PRIDE; Q9FXJ2; -.
DR ProteomicsDB; 247110; -. [Q9FXJ2-1]
DR EnsemblPlants; AT1G28580.1; AT1G28580.1; AT1G28580. [Q9FXJ2-1]
DR EnsemblPlants; AT1G28580.2; AT1G28580.2; AT1G28580. [Q9FXJ2-2]
DR GeneID; 839758; -.
DR Gramene; AT1G28580.1; AT1G28580.1; AT1G28580. [Q9FXJ2-1]
DR Gramene; AT1G28580.2; AT1G28580.2; AT1G28580. [Q9FXJ2-2]
DR KEGG; ath:AT1G28580; -.
DR Araport; AT1G28580; -.
DR TAIR; locus:2018758; AT1G28580.
DR eggNOG; ENOG502QSMM; Eukaryota.
DR HOGENOM; CLU_015101_2_1_1; -.
DR InParanoid; Q9FXJ2; -.
DR OMA; SETKCRE; -.
DR PhylomeDB; Q9FXJ2; -.
DR BioCyc; ARA:AT1G28580-MON; -.
DR PRO; PR:Q9FXJ2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXJ2; baseline and differential.
DR Genevisible; Q9FXJ2; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; 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 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..390
FT /note="GDSL esterase/lipase At1g28580"
FT /id="PRO_0000367349"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 347
FT /evidence="ECO:0000250"
FT ACT_SITE 350
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..90
FT /note="MAYPGSPILMKLLVFIFLSTFVVTNVSSETKCREFKSIISFGDSIADTGNLL
FT GLSDPKDLPHMAFPPYGENFFHHPTGRFSNGRLIIDFI -> MFFSLVLFT (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036687"
SQ SEQUENCE 390 AA; 43025 MW; 47C5ECFADB9ECF40 CRC64;
MAYPGSPILM KLLVFIFLST FVVTNVSSET KCREFKSIIS FGDSIADTGN LLGLSDPKDL
PHMAFPPYGE NFFHHPTGRF SNGRLIIDFI AEFLGLPLVP PFYGSHNANF EKGVNFAVGG
ATALERSFLE DRGIHFPYTN VSLGVQLNSF KESLPSICGS PSDCRDMIEN ALILMGEIGG
NDYNYAFFVD KGIEEIKELM PLVITTISSA ITELIGMGGR TFLVPGEFPV GCSVLYLTSH
QTSNMEEYDP LTGCLKWLNK FGENHGEQLR AELNRLQKLY PHVNIIYADY YNALFHLYQE
PAKFGFMNRP LSACCGAGGP YNYTVGRKCG TDIVESCDDP SKYVAWDGVH MTEAAYRLMA
EGILNGPYAI PPFDWSCRSS GVKNSGSSDT
