GLIP2_ARATH
ID GLIP2_ARATH Reviewed; 376 AA.
AC Q9SYF0; F4HTF4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=GDSL esterase/lipase 2;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase 2;
DE Flags: Precursor;
GN Name=GLIP2; OrderedLocusNames=At1g53940; ORFNames=F15I1.2;
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 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 [4]
RP GENE FAMILY.
RX PubMed=16126835; DOI=10.1105/tpc.105.034819;
RA Oh I.S., Park A.R., Bae M.S., Kwon S.J., Kim Y.S., Lee J.E., Kang N.Y.,
RA Lee S., Cheong H., Park O.K.;
RT "Secretome analysis reveals an Arabidopsis lipase involved in defense
RT against Alternaria brassicicola.";
RL Plant Cell 17:2832-2847(2005).
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).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY SA; JA
RP AND ET.
RX PubMed=19146828; DOI=10.1016/j.bbrc.2009.01.006;
RA Lee D.S., Kim B.K., Kwon S.J., Jin H.C., Park O.K.;
RT "Arabidopsis GDSL lipase 2 plays a role in pathogen defense via negative
RT regulation of auxin signaling.";
RL Biochem. Biophys. Res. Commun. 379:1038-1042(2009).
CC -!- FUNCTION: Involved in the resistance to the necrotropic bacteria
CC Erwinia carotovora, probably via negative regulation of auxin
CC signaling. Possesses lipase and antimicrobial activities, inhibiting
CC germination of fungal spores (e.g. Alternaria brassicicola).
CC {ECO:0000269|PubMed:19146828}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed seedlings, roots and stems.
CC {ECO:0000269|PubMed:19146828}.
CC -!- INDUCTION: In roots, by salicylic acid (SA), jasmonic acid (JA), and
CC ethylene (ET) treatments. {ECO:0000269|PubMed:19146828}.
CC -!- DISRUPTION PHENOTYPE: In glip2, enhanced auxin responses, and higher
CC susceptibility to E.carotovora. {ECO:0000269|PubMed:19146828}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AC006577; AAD25766.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59524.1; -; Genomic_DNA.
DR PIR; G96579; G96579.
DR RefSeq; NP_175797.2; NM_104272.2.
DR AlphaFoldDB; Q9SYF0; -.
DR SMR; Q9SYF0; -.
DR STRING; 3702.AT1G53940.1; -.
DR PaxDb; Q9SYF0; -.
DR PRIDE; Q9SYF0; -.
DR ProteomicsDB; 230478; -.
DR EnsemblPlants; AT1G53940.2; AT1G53940.2; AT1G53940.
DR GeneID; 841833; -.
DR Gramene; AT1G53940.2; AT1G53940.2; AT1G53940.
DR KEGG; ath:AT1G53940; -.
DR Araport; AT1G53940; -.
DR eggNOG; ENOG502QQ4G; Eukaryota.
DR HOGENOM; CLU_015101_0_2_1; -.
DR InParanoid; Q9SYF0; -.
DR OMA; FTCINLI; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q9SYF0; -.
DR BioCyc; ARA:AT1G53940-MON; -.
DR PRO; PR:Q9SYF0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYF0; baseline and differential.
DR Genevisible; Q9SYF0; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IDA:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0098542; P:defense response to other organism; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
DR GO; GO:0010930; P:negative regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR044552; GLIP1-5/GLL25.
DR InterPro; IPR008265; Lipase_GDSL_AS.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR PANTHER; PTHR45966; PTHR45966; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE 2: Evidence at transcript level;
KW Auxin signaling pathway; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Plant defense; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..376
FT /note="GDSL esterase/lipase 2"
FT /id="PRO_0000367335"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 340
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /evidence="ECO:0000250"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 376 AA; 42014 MW; DC5AD0A1CCFB1864 CRC64;
MENSRSTLII FFAYTTIILI GSINCRDNNN NNLVTNQSAL FVFGDSVFDA GNNNYIDTLP
SFRSNYWPYG QTTFKFPTGR VSDGRTIPDF IAEYAWLPLI PAYLQPSNGK NQFPYGVSFA
SAGAGALVGT FPGMVINLKS QLNNFKKVEK LLRSTLGEAQ GKMVISRAVY LFHIGVNDYQ
YPFSTNSSIF QSSPQEIYVD FVVGNTTAVI KEVYKIGGRK FGFLNMGAYD CAPASLIIDQ
TKIGTCFKPV TELINLHNEK LESGLRRLER ELSGFKYALH DYHTSLSVRM NNPSKYGFKE
GKMACCGTGP LRGINTCGGR MGVSQSYELC EKVTDYLFFD HFHLTEKAHQ QIAELIWSGP
TNVTKPYNLQ ALFELN
