PLIP3_ARATH
ID PLIP3_ARATH Reviewed; 649 AA.
AC Q940L4; Q9LZK6;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phospholipase A1 PLIP3, chloroplastic {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000269|PubMed:29666162};
DE AltName: Full=Galactolipase PLIP3 {ECO:0000305};
DE EC=3.1.1.26 {ECO:0000269|PubMed:29666162};
DE AltName: Full=Protein PLASTID LIPASE 3 {ECO:0000303|PubMed:29666162};
DE Flags: Precursor;
GN Name=PLIP3 {ECO:0000303|PubMed:29666162};
GN OrderedLocusNames=At3g62590 {ECO:0000312|Araport:AT3G62590};
GN ORFNames=F26K9_20 {ECO:0000312|EMBL:CAB83109.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP MUTAGENESIS OF SER-385.
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 phosphatidylglycerol (PG). May function downstream of abscisic acid
CC (ABA), and provide a link between ABA-mediated abiotic stress responses
CC and oxylipin and JA signalings. In vitro, possesses broad substrate
CC 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-(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}.
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=CAB83109.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162651; CAB83109.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80367.1; -; Genomic_DNA.
DR EMBL; AY054280; AAL06939.1; -; mRNA.
DR EMBL; BT002305; AAN73302.1; -; mRNA.
DR PIR; T48048; T48048.
DR RefSeq; NP_567131.1; NM_116124.3.
DR AlphaFoldDB; Q940L4; -.
DR SMR; Q940L4; -.
DR STRING; 3702.AT3G62590.1; -.
DR SwissLipids; SLP:000001916; -.
DR ESTHER; arath-AT3g62590; Lipase_3.
DR PaxDb; Q940L4; -.
DR PRIDE; Q940L4; -.
DR ProteomicsDB; 234727; -.
DR EnsemblPlants; AT3G62590.1; AT3G62590.1; AT3G62590.
DR GeneID; 825433; -.
DR Gramene; AT3G62590.1; AT3G62590.1; AT3G62590.
DR KEGG; ath:AT3G62590; -.
DR Araport; AT3G62590; -.
DR TAIR; locus:2081720; AT3G62590.
DR eggNOG; ENOG502QU4P; Eukaryota.
DR HOGENOM; CLU_016443_0_0_1; -.
DR InParanoid; Q940L4; -.
DR OMA; DFCRIDD; -.
DR OrthoDB; 510921at2759; -.
DR PhylomeDB; Q940L4; -.
DR PRO; PR:Q940L4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q940L4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; 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; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:TAIR.
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.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 27..649
FT /note="Phospholipase A1 PLIP3, chloroplastic"
FT /id="PRO_0000444795"
FT REGION 104..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 383..387
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 385
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 446
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 560
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT MUTAGEN 385
FT /note="S->A: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:29666162"
SQ SEQUENCE 649 AA; 73044 MW; A38199AB94CD462D CRC64;
MEGVFLKMSV VGVSPMIPVG PSSFICAIGG SVEEKSTAAS LPRWVSLRRL RPLEFLRIGG
KREEKGTVRD DDAVLLERRD RNRNENDNGN WVLKILEVGS IWKGKRQRSG GGGGGEEDEE
EEVAEPKKKE DLCEECDFCR IDDDDEDEEK EKTVFEFSEM LSKIPVEDAQ MFAKLSFLGN
LAYSIPKIKP ENLLKYQKLR FVTSSIEKRM SLKVEENNNG EEDEEKKKLI NPAVAYRIAA
SAASRLFSHS KSVLPFGSSK RQDNEEASLL ATADSVTAVV AAKEEVKQAV ADDLKSNRSP
PCEWFVCDDD KSGTRFFFIQ GSDSLASWQA NLLFEPVPFE DLDVLVHRGI YEAAKGIYEQ
MLPEVHAHLN SRGKNRAFLR FSGHSLGGSL SLLVNLMLLI RGQVPASSLL PVITFGSPCI
MCGGDRLLQK LGLPKSHLLG ISMHRDIVPR AFSCNYPNRA AKLLKALNGN FRNHPCLNNQ
NVLYSPMGKL LILQPSERFS PPHPLLPPGS GLYLLASKNT DETEKSLRAA KILFFNSPHP
LEILSDRRSY GSEGKIKRNH DMSSYLKALR HVIRKELKQM KAERDQWLRK FFIINILFSG
RDSLKLITRF VASRSSQLVI IFFLPIRLLI MSVYSVVFHH SQAHFSFFK
