PLP2_ARATH
ID PLP2_ARATH Reviewed; 407 AA.
AC O48723; Q8LDK8;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Patatin-like protein 2;
DE Short=AtPLP2;
DE EC=3.1.1.-;
DE AltName: Full=Patatin-related phospholipase A IIalpha;
DE Short=pPLAIIa;
DE AltName: Full=Phospholipase A IIA;
DE Short=AtPLAIIA;
GN Name=PLP2; OrderedLocusNames=At2g26560; ORFNames=T9J22.23;
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=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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12226489; DOI=10.1104/pp.006288;
RA Holk A., Rietz S., Zahn M., Quader H., Scherer G.F.;
RT "Molecular identification of cytosolic, patatin-related phospholipases A
RT from Arabidopsis with potential functions in plant signal transduction.";
RL Plant Physiol. 130:90-101(2002).
RN [6]
RP INDUCTION.
RX PubMed=14634163; DOI=10.1093/pcp/pcg138;
RA Narusaka Y., Narusaka M., Seki M., Fujita M., Ishida J., Nakashima M.,
RA Enju A., Sakurai T., Satou M., Kamiya A., Park P., Kobayashi M.,
RA Shinozaki K.;
RT "Expression profiles of Arabidopsis phospholipase A IIA gene in response to
RT biotic and abiotic stresses.";
RL Plant Cell Physiol. 44:1246-1252(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16297072; DOI=10.1111/j.1365-313x.2005.02578.x;
RA La Camera S., Geoffroy P., Samaha H., Ndiaye A., Rahim G., Legrand M.,
RA Heitz T.;
RT "A pathogen-inducible patatin-like lipid acyl hydrolase facilitates fungal
RT and bacterial host colonization in Arabidopsis.";
RL Plant J. 44:810-825(2005).
RN [8]
RP FUNCTION.
RX PubMed=19271961; DOI=10.1094/mpmi-22-4-0469;
RA La Camera S., Balague C., Gobel C., Geoffroy P., Legrand M., Feussner I.,
RA Roby D., Heitz T.;
RT "The Arabidopsis patatin-like protein 2 (PLP2) plays an essential role in
RT cell death execution and differentially affects biosynthesis of oxylipins
RT and resistance to pathogens.";
RL Mol. Plant Microbe Interact. 22:469-481(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22259021; DOI=10.1093/mp/ssr118;
RA Yang W.Y., Zheng Y., Bahn S.C., Pan X.Q., Li M.Y., Vu H.S., Roth M.R.,
RA Scheu B., Welti R., Hong Y.Y., Wang X.M.;
RT "The patatin-containing phospholipase A pPLAIIalpha modulates oxylipin
RT formation and water loss in Arabidopsis thaliana.";
RL Mol. Plant 5:452-460(2012).
CC -!- FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH)
CC activity. Catalyzes the hydrolysis of the galactolipids
CC monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol
CC (DGDG), and less efficiently the phoshpolipids phosphatidylcholine
CC (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG),
CC phosphatidic acid (PA), phosphatidylserine (PS) and
CC phosphatidylinositol (PI). Favors the release of fatty acid at the sn-1
CC position for PC or PE and the sn-2 position for PG, PA, PS and PI.
CC Negatively affects disease resistance to the necrotic fungal pathogen
CC Botrytis cinerea and the avirulent bacteria Pseudomonas syringae by
CC promoting cell death and reducing the efficiency of the hypersensitive
CC response, respectively. However, PLP2 contributes to resistance to
CC cucumber mosaic virus (CMV), an obligate parasite inducing
CC hypersensitive response. May negatively regulate oxylipin production,
CC possibly via participating in membrane repair that includes removal of
CC oxidatively modified lipids. {ECO:0000269|PubMed:16297072,
CC ECO:0000269|PubMed:19271961, ECO:0000269|PubMed:22259021}.
CC -!- INTERACTION:
CC O48723; Q39070: CYCB2-2; NbExp=3; IntAct=EBI-4443426, EBI-2651372;
CC O48723; O48723: PLP2; NbExp=4; IntAct=EBI-4443426, EBI-4443426;
CC O48723; Q9FHZ1: SCL23; NbExp=5; IntAct=EBI-4443426, EBI-1238460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12226489,
CC ECO:0000269|PubMed:16297072}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in roots.
CC {ECO:0000269|PubMed:12226489}.
CC -!- INDUCTION: By infection with the fungal pathogens B.cinerea and
CC A.brassicicola, and avirulent and virulent strains of P.syringae pv
CC tomato DC3000 (at protein level). Induced by ethylene and copper.
CC {ECO:0000269|PubMed:14634163, ECO:0000269|PubMed:16297072}.
CC -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC motif define the oxyanion hole, and stabilize the oxyanion that forms
CC during the nucleophilic attack by the catalytic serine during substrate
CC cleavage. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but leaves of mutant plants contain decreased levels of
CC lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine(LPE),
CC but increased levels of free linolenic acid, jasmonic acid and methyl
CC jasmonate, as well as the oxylipin-biosynthetic intermediates 13-
CC hydroperoxylinolenic acid and 12-oxophytodienoic acid.
CC {ECO:0000269|PubMed:22259021}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63157.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002505; AAC14504.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07858.1; -; Genomic_DNA.
DR EMBL; AY062644; AAL32722.1; -; mRNA.
DR EMBL; AY093305; AAM13304.1; -; mRNA.
DR EMBL; AY085946; AAM63157.1; ALT_INIT; mRNA.
DR PIR; T00989; T00989.
DR RefSeq; NP_180224.1; NM_128213.4.
DR AlphaFoldDB; O48723; -.
DR SMR; O48723; -.
DR BioGRID; 2549; 4.
DR IntAct; O48723; 3.
DR STRING; 3702.AT2G26560.1; -.
DR PaxDb; O48723; -.
DR PRIDE; O48723; -.
DR ProteomicsDB; 236635; -.
DR DNASU; 817197; -.
DR EnsemblPlants; AT2G26560.1; AT2G26560.1; AT2G26560.
DR GeneID; 817197; -.
DR Gramene; AT2G26560.1; AT2G26560.1; AT2G26560.
DR KEGG; ath:AT2G26560; -.
DR Araport; AT2G26560; -.
DR TAIR; locus:2066286; AT2G26560.
DR eggNOG; KOG0513; Eukaryota.
DR HOGENOM; CLU_000288_144_0_1; -.
DR InParanoid; O48723; -.
DR OMA; YETTNEH; -.
DR OrthoDB; 1209603at2759; -.
DR PhylomeDB; O48723; -.
DR BioCyc; ARA:AT2G26560-MON; -.
DR BRENDA; 3.1.1.23; 399.
DR PRO; PR:O48723; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48723; baseline and differential.
DR Genevisible; O48723; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016298; F:lipase activity; IDA:TAIR.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IDA:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism; Phosphoprotein;
KW Plant defense; Reference proteome.
FT CHAIN 1..407
FT /note="Patatin-like protein 2"
FT /id="PRO_0000425814"
FT DOMAIN 22..228
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 26..31
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 64..68
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 215..217
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23179"
FT CONFLICT 384
FT /note="A -> E (in Ref. 4; AAM63157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 44239 MW; AC113497DFB647C4 CRC64;
MQMDSPKSPL QPPTYGNLVT ILSIDGGGIR GLIPAVILGF LESELQKLDG EEARLADYFD
VIAGTSTGGL VTAMLTAPNK EGRPLFAASE IKDFYLEQCP KIFPQDHFPF SAAKKLVKSL
TGPKYDGKYL HQLIHAKLGD TKLSQTLTNV VIPTFDIKHL QPTIFSSYEV KNHPLKDATL
ADIAISTSAA PTYLPAHFFK VEDLNGNAKE YNLIDGGVAA NNPALLAIGE VTNEISGGSS
DFFPIRPNDY GRFLVLSLGT GNHKAEEKFN AKEVAGWGLL NWLTHDNSTP IIDAFSQASS
DMVDFHLSAV FRALHSEANY IRIQDDTLTG DAASVDIATV ENLDILAKTG DELLKKPVAR
VNLDSGCNEN AYETTNEHAL IKLAGILSKE KKIRDIRSPH AKAPIRI
