PLIP2_ARATH
ID PLIP2_ARATH Reviewed; 713 AA.
AC F4HXL0; B9DI25; Q8L739; Q94AE2; Q9FWY4;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Phospholipase A1 PLIP2, chloroplastic {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000269|PubMed:29666162};
DE AltName: Full=Galactolipase PLIP2 {ECO:0000305};
DE EC=3.1.1.26 {ECO:0000269|PubMed:29666162};
DE AltName: Full=Protein PLASTID LIPASE 2 {ECO:0000303|PubMed:29666162};
DE Flags: Precursor;
GN Name=PLIP2 {ECO:0000303|PubMed:29666162};
GN OrderedLocusNames=At1g02660 {ECO:0000312|Araport:AT1G02660};
GN ORFNames=T14P4.6 {ECO:0000312|EMBL:AAG10634.1};
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 [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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 164-713.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP MUTAGENESIS OF SER-428.
RX PubMed=29666162; DOI=10.1105/tpc.18.00250;
RA Wang K., Guo Q., Froehlich J.E., Hersh H.L., Zienkiewicz A., Howe G.A.,
RA Benning C.;
RT "Two abscisic acid responsive plastid lipase genes involved in jasmonic
RT acid biosynthesis in Arabidopsis thaliana.";
RL Plant Cell 30:1006-1022(2018).
CC -!- FUNCTION: Sn-1-specific phospholipase A1 that catalyzes the initial
CC step of oxylipins and jasmonate (JA) biosynthesis. Hydrolyzes
CC polyunsaturated acyl groups preferentially from chloroplastic
CC monogalactosyldiacylglycerol (MGDG). May function downstream of
CC abscisic acid (ABA) and provide a link between ABA-mediated abiotic
CC stress responses and oxylipin and JA signalings. In vitro, possesses
CC broad substrate specificity. Can hydrolyze the galactolipids
CC monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol
CC (DGDG), the sulfolipid sulfoquinovosyldiacylglycerol (SQDG), and the
CC phoshpolipids phosphatidylcholine (PC), and phosphatidylglycerol (PG).
CC {ECO:0000269|PubMed:29666162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-
CC beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+);
CC Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26;
CC Evidence={ECO:0000269|PubMed:29666162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190;
CC Evidence={ECO:0000269|PubMed:29666162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:29666162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000269|PubMed:29666162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001,
CC ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:29666162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000269|PubMed:29666162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H(+); Xref=Rhea:RHEA:56448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76071;
CC Evidence={ECO:0000269|PubMed:29666162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56449;
CC Evidence={ECO:0000269|PubMed:29666162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:40823, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75034,
CC ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:29666162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40824;
CC Evidence={ECO:0000269|PubMed:29666162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H(+) + octadecanoate; Xref=Rhea:RHEA:56636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:76084, ChEBI:CHEBI:84822;
CC Evidence={ECO:0000269|PubMed:29666162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56637;
CC Evidence={ECO:0000269|PubMed:29666162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine +
CC H2O = (9Z,12Z)-octadecadienoate + 2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:56640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:42027, ChEBI:CHEBI:76084;
CC Evidence={ECO:0000269|PubMed:29666162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56641;
CC Evidence={ECO:0000269|PubMed:29666162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38787, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74667,
CC ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:29666162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38788;
CC Evidence={ECO:0000269|PubMed:29666162};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:29666162}; Peripheral membrane protein
CC {ECO:0000305}. Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:29666162}.
CC -!- INDUCTION: Induced by abscisic acid (ABA) and cold stress.
CC {ECO:0000269|PubMed:29666162}.
CC -!- MISCELLANEOUS: Plants overexpressing PLIP3 exhibit stunted growth and
CC accumulate anthocyanin under normal growth conditions.
CC {ECO:0000269|PubMed:29666162}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG10634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022521; AAG10634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27455.1; -; Genomic_DNA.
DR EMBL; AY048246; AAK82508.1; -; mRNA.
DR EMBL; AY139797; AAM98103.1; -; mRNA.
DR EMBL; AK317736; BAH20392.1; -; mRNA.
DR PIR; F86156; F86156.
DR RefSeq; NP_563660.1; NM_100146.3.
DR AlphaFoldDB; F4HXL0; -.
DR SMR; F4HXL0; -.
DR STRING; 3702.AT1G02660.1; -.
DR SwissLipids; SLP:000001917; -.
DR ESTHER; arath-T14P4.6; Lipase_3.
DR PaxDb; F4HXL0; -.
DR PRIDE; F4HXL0; -.
DR ProteomicsDB; 235006; -.
DR EnsemblPlants; AT1G02660.1; AT1G02660.1; AT1G02660.
DR GeneID; 839544; -.
DR Gramene; AT1G02660.1; AT1G02660.1; AT1G02660.
DR KEGG; ath:AT1G02660; -.
DR Araport; AT1G02660; -.
DR TAIR; locus:2196045; AT1G02660.
DR eggNOG; ENOG502QU4P; Eukaryota.
DR HOGENOM; CLU_016443_0_0_1; -.
DR InParanoid; F4HXL0; -.
DR OMA; HATFRFT; -.
DR OrthoDB; 510921at2759; -.
DR PRO; PR:F4HXL0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HXL0; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0102549; F:1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047714; F:galactolipase activity; IDA:TAIR.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 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 GO; GO:0031349; P:positive regulation of defense response; IMP:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR InterPro; IPR043367; PLIP1/2/3.
DR PANTHER; PTHR46483; PTHR46483; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..713
FT /note="Phospholipase A1 PLIP2, chloroplastic"
FT /id="PRO_0000444794"
FT REGION 118..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 426..430
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT COMPBIAS 120..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 428
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 489
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 608
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT MUTAGEN 428
FT /note="S->A: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:29666162"
FT CONFLICT 616
FT /note="A -> P (in Ref. 3; AAK82508)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="G -> V (in Ref. 3; AAK82508/AAM98103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 78346 MW; 2B904DE3E01DEA25 CRC64;
MDSLCLNSGL HGVIPAITAV GNGGCGGVVE VRATASAPSQ KRGPFGFSFK YPLTPFWSRG
GGGGIASRRR SGLCLDDAVL VDSGDSRKPI AEETAVEMDT ERRNGSWVLK ILDVQSTWKH
EEEEDDDEVE DEDGDEDEEV ELDDAVVSED DGGCDVCSVL EDDGNEANKF QLDRESFSKL
LRRVTLPESK LYAQLSYLGN LAYSISKIKP ANLSKYYGLR FVTSSAEKTE SALKAENGEV
SGETKPIVEA EEEVEEEEKN KSRKISASAA YEIVASAASY LHSRTNNILP FNSSSKAENS
DKHDVNLTNA ESSSDVAYSV TSVVAAEEDV KQAVADDLKS TISSPCDWFI CDDDQSHTRF
VVIQGSESLA SWQANLLFEP IEFEGLGAIV HRGIYEAAKG MYEQMLPEVK AHIKTHGTSA
KFRFTGHSLG GSLSLLLNLM LLVRGEVPAS SLLPVITYGA PFVLCGGDRL LKKLGLPKSH
VQAIVMHRDI VPRAFSCNYP YHVAELLKAV NGNFRSHPCL NKQSMLYSPM GELLILQPDE
TFSPGHELLP SGNGLYLLTS DFESPDIEDS DEERLRAAQT VFLNTPHPLD ILSDRSAYGS
SGTIQRDHDM NSYLKAVRSV IRKEVNQIRR AKREHRRSLW WPILVARESG SSGIAVSNGQ
INGQDFSGMM QTGRKSLQRF SRLVASQHMP LIVVMLFPVK LLFLGAFNVF SFR
