LIP2_ARATH
ID LIP2_ARATH Reviewed; 418 AA.
AC Q67ZU1; Q681B0; Q6VY31; Q94AE7; Q9FMT2; Q9FMT3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Triacylglycerol lipase 2;
DE EC=3.1.1.3;
DE Flags: Precursor;
GN Name=LIP2; OrderedLocusNames=At5g14180; ORFNames=MUA22.18, MUA22.19;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 110-418.
RC STRAIN=cv. Columbia;
RA Benveniste P., Noiriel A., Bouvier-Nave P., Schaller H.;
RT "Sterol (triglyceride) ester hydrolase from Arabidopsis thaliana.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-418.
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).
CC -!- FUNCTION: Triacylglycerol (TAG) lipase. May be involved for TAG storage
CC breakdown during seed germination (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK82499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB08297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB08298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB007650; BAB08297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB007650; BAB08298.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91996.1; -; Genomic_DNA.
DR EMBL; AK175707; BAD43470.1; -; mRNA.
DR EMBL; AK176026; BAD43789.1; -; mRNA.
DR EMBL; AY320231; AAQ84586.1; -; mRNA.
DR EMBL; AY048236; AAK82499.1; ALT_INIT; mRNA.
DR EMBL; AY091711; AAM10310.1; -; mRNA.
DR RefSeq; NP_568295.2; NM_121422.4.
DR AlphaFoldDB; Q67ZU1; -.
DR SMR; Q67ZU1; -.
DR BioGRID; 16546; 1.
DR STRING; 3702.AT5G14180.1; -.
DR ESTHER; arath-LIP2; Acidic_Lipase.
DR MEROPS; S33.A64; -.
DR PaxDb; Q67ZU1; -.
DR PRIDE; Q67ZU1; -.
DR EnsemblPlants; AT5G14180.1; AT5G14180.1; AT5G14180.
DR GeneID; 831268; -.
DR Gramene; AT5G14180.1; AT5G14180.1; AT5G14180.
DR KEGG; ath:AT5G14180; -.
DR Araport; AT5G14180; -.
DR TAIR; locus:2174648; AT5G14180.
DR eggNOG; KOG2624; Eukaryota.
DR HOGENOM; CLU_010974_1_1_1; -.
DR InParanoid; Q67ZU1; -.
DR OMA; HKYWPTY; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; Q67ZU1; -.
DR BioCyc; ARA:AT5G14180-MON; -.
DR PRO; PR:Q67ZU1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q67ZU1; baseline and differential.
DR Genevisible; Q67ZU1; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IDA:TAIR.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0002213; P:defense response to insect; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..418
FT /note="Triacylglycerol lipase 2"
FT /id="PRO_0000234337"
FT ACT_SITE 190
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 393
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 191
FT /note="L -> Q (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="A -> G (in Ref. 4; AAQ84586)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="S -> A (in Ref. 4; AAQ84586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46048 MW; 613F11551D34A6D7 CRC64;
MAGSVMVPSV SIGLALSVLI FFALSLKTLE ARGTFGRLAG QPPQRTAAGG ICASSVHIFG
YKCEEHDVVT QDGYILNMQR IPEGRAGAVA GDGGKRQPVL IQHGILVDGM SWLLNPADQN
LPLILADQGF DVWMGNTRGT RFSRRHKYLN PSQRAFWNWT WDELVSYDLP AMFDHIHGLT
GQKIHYLGHS LGTLIGFASF SEKGLVDQVR SAAMLSPVAY LSHMTTVIGD IAAKTFLAEA
TSILGWPEFN PKSGLVGDFI KAICLKAGID CYDLVSVITG KNCCLNASTI DLFLANEPQS
TSTKNMIHLA QTVRDKELRK YNYGSSDRNI KHYGQAIPPA YNISAIPHEL PLFFSYGGLD
SLADVKDVEF LLDQFKYHDI DKMNVQFVKD YAHADFIMGV TAKDVVYNQV ATFFKRQA
