LIP1_ARATH
ID LIP1_ARATH Reviewed; 393 AA.
AC Q71DJ5; Q1H5B7; Q9SKL5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Triacylglycerol lipase 1 {ECO:0000303|PubMed:16226259};
DE EC=3.1.1.3 {ECO:0000269|PubMed:16226259};
DE Flags: Precursor;
GN Name=LIP1 {ECO:0000303|PubMed:16226259};
GN OrderedLocusNames=At2g15230 {ECO:0000312|Araport:AT2G15230};
GN ORFNames=F15A23.3 {ECO:0000312|EMBL:AAD25569.1};
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 [MRNA], PROTEIN SEQUENCE OF 21-28, FUNCTION, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=16226259; DOI=10.1016/j.febslet.2005.09.072;
RA El-Kouhen K., Blangy S., Ortiz E., Gardies A.-M., Ferte N., Arondel V.;
RT "Identification and characterization of a triacylglycerol lipase in
RT Arabidopsis homologous to mammalian acid lipases.";
RL FEBS Lett. 579:6067-6073(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Benveniste P., Noiriel A., Nave P., Schaller H.;
RT "Triacylglycerol (steryl ester) hydrolase from Arabidopsis thaliana is
RT involved in lipid homeostasy.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP REVIEW ON ACYL-LIPID METABOLISM.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
RN [8]
RP FUNCTION, INDUCTION BY IMBIBITION; GIBBERELLINS AND DELLA PROTEINS, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=24989044; DOI=10.1105/tpc.114.127647;
RA Rombola-Caldentey B., Rueda-Romero P., Iglesias-Fernandez R., Carbonero P.,
RA Onate-Sanchez L.;
RT "Arabidopsis DELLA and two HD-ZIP transcription factors regulate GA
RT signaling in the epidermis through the L1 box cis-element.";
RL Plant Cell 26:2905-2919(2014).
CC -!- FUNCTION: Triacylglycerol (TAG) lipase active on triolein, trioctanoin,
CC tributyrin and 1,3-Diolein, but not on phospho- and galactolipids
CC (PubMed:16226259). Involved but dispensable for TAG storage breakdown
CC during seed germination (PubMed:16226259, PubMed:24989044).
CC {ECO:0000269|PubMed:16226259, ECO:0000269|PubMed:24989044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:16226259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000269|PubMed:16226259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:16226259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000269|PubMed:16226259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC ChEBI:CHEBI:88066; Evidence={ECO:0000269|PubMed:16226259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000269|PubMed:16226259};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=45 umol/min/mg enzyme with triolein as a substrate
CC {ECO:0000269|PubMed:16226259};
CC pH dependence:
CC Optimum pH is 6. Active between pH 4-7.
CC {ECO:0000269|PubMed:16226259};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000269|PubMed:16226259}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, flowers and
CC siliques (PubMed:16226259). Specifically expressed in the epidermis
CC (PubMed:24989044). {ECO:0000269|PubMed:16226259,
CC ECO:0000269|PubMed:24989044}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in seeds upon imbibition.
CC {ECO:0000269|PubMed:24989044}.
CC -!- INDUCTION: Stimulated during seed imbibition (PubMed:24989044). Induced
CC by gibberellins (GAs) and repressed by DELLA proteins (e.g. GAI/RGA2,
CC RGA/RGA1/GRS and RGL2/SCL19) in an ATML1- and PDF2-dependent manner
CC (PubMed:24989044). Upon seed imbibition, increased GA levels in the
CC epidermis reduce DELLA proteins abundance and release, in turn, ATML1
CC and PDF2 which activate LIP1 expression, thus enhancing germination
CC potential (PubMed:24989044). {ECO:0000269|PubMed:24989044}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF530477; AAN77143.1; -; mRNA.
DR EMBL; AC006298; AAD25569.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06377.1; -; Genomic_DNA.
DR EMBL; BT025547; ABF58965.1; -; mRNA.
DR EMBL; AK229578; BAF01428.1; -; mRNA.
DR PIR; E84526; E84526.
DR RefSeq; NP_179126.2; NM_127084.3.
DR AlphaFoldDB; Q71DJ5; -.
DR SMR; Q71DJ5; -.
DR STRING; 3702.AT2G15230.1; -.
DR SwissLipids; SLP:000001907; -.
DR ESTHER; arath-At2g15230; Acidic_Lipase.
DR MEROPS; S33.A61; -.
DR PaxDb; Q71DJ5; -.
DR PRIDE; Q71DJ5; -.
DR ProteomicsDB; 238607; -.
DR EnsemblPlants; AT2G15230.1; AT2G15230.1; AT2G15230.
DR GeneID; 816012; -.
DR Gramene; AT2G15230.1; AT2G15230.1; AT2G15230.
DR KEGG; ath:AT2G15230; -.
DR Araport; AT2G15230; -.
DR TAIR; locus:2041834; AT2G15230.
DR eggNOG; KOG2624; Eukaryota.
DR HOGENOM; CLU_010974_1_1_1; -.
DR InParanoid; Q71DJ5; -.
DR OMA; DGEHVDC; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; Q71DJ5; -.
DR BioCyc; ARA:AT2G15230-MON; -.
DR BRENDA; 3.1.1.3; 399.
DR UniPathway; UPA00230; -.
DR PRO; PR:Q71DJ5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q71DJ5; baseline and differential.
DR Genevisible; Q71DJ5; AT.
DR GO; GO:0005615; C:extracellular space; TAS:TAIR.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:TAIR.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:2000033; P:regulation of seed dormancy process; IEP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IEP:UniProtKB.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006693; AB_hydrolase_lipase.
DR InterPro; IPR025483; Lipase_euk.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Gibberellin signaling pathway; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:16226259"
FT CHAIN 21..393
FT /note="Triacylglycerol lipase 1"
FT /id="PRO_0000234336"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 363
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 393 AA; 44231 MW; C904556DCB44178D CRC64;
MKWLLVAVLT SLTIFSALTQ SHLLHGSPVN SLCADLIHPA NYSCTEHSIQ TKDGYILALQ
RVASLGPRLQ SGPPVLLQHG LFMAGDVWFL NSPKESLGFI LADHGFDVWV GNVRGTRYSY
GHVTLSDTDK EFWDWSWQDL AMYDLAEMIQ YLYSISNSKI FLVGHSQGTI MSFAALTQPH
VAEMVEAAAL LCPISYLDHV TAPLVERMVF MHLDQMVVAL GLHQINFRSD MLVKLVDSLC
EGHMDCTDFL TSITGTNCCF NASKIEYYLD YEPHPSSVKN IRHLFQMIRK GTFAQYDYGY
FKNLRTYGLS KPPEFILSHI PASLPMWMGY GGTDGLADVT DVEHTLAELP SSPELLYLED
YGHIDFVLGS SAKEDVYKHM IQFFRAKVKS SSW
