PLA13_ARATH
ID PLA13_ARATH Reviewed; 484 AA.
AC Q9SIN9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Phospholipase A1-Ialpha2, chloroplastic {ECO:0000303|PubMed:15130548};
DE EC=3.1.1.- {ECO:0000269|PubMed:19527719};
DE AltName: Full=DAD1-like lipase 5 {ECO:0000303|PubMed:24430866};
DE Flags: Precursor;
GN Name=DALL5 {ECO:0000303|PubMed:24430866};
GN OrderedLocusNames=At2g31690 {ECO:0000312|Araport:AT2G31690};
GN ORFNames=T9H9.21 {ECO:0000312|EMBL:AAD24845.1};
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=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;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15130548; DOI=10.1016/j.tplants.2004.03.004;
RA Ryu S.B.;
RT "Phospholipid-derived signaling mediated by phospholipase A in plants.";
RL Trends Plant Sci. 9:229-235(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17259290; DOI=10.1104/pp.106.090811;
RA Padham A.K., Hopkins M.T., Wang T.W., McNamara L.M., Lo M.,
RA Richardson L.G., Smith M.D., Taylor C.A., Thompson J.E.;
RT "Characterization of a plastid triacylglycerol lipase from Arabidopsis.";
RL Plant Physiol. 143:1372-1384(2007).
RN [6]
RP INDUCTION.
RX PubMed=18267087; DOI=10.1016/j.devcel.2007.11.010;
RA Hyun Y., Choi S., Hwang H.J., Yu J., Nam S.J., Ko J., Park J.Y., Seo Y.S.,
RA Kim E.Y., Ryu S.B., Kim W.T., Lee Y.H., Kang H., Lee I.;
RT "Cooperation and functional diversification of two closely related
RT galactolipase genes for jasmonate biosynthesis.";
RL Dev. Cell 14:183-192(2008).
RN [7]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19527719; DOI=10.1016/j.febslet.2009.06.021;
RA Seo Y.S., Kim E.Y., Kim J.H., Kim W.T.;
RT "Enzymatic characterization of class I DAD1-like acylhydrolase members
RT targeted to chloroplast in Arabidopsis.";
RL FEBS Lett. 583:2301-2307(2009).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=20348210; DOI=10.1104/pp.110.155093;
RA Ellinger D., Stingl N., Kubigsteltig I.I., Bals T., Juenger M.,
RA Pollmann S., Berger S., Schuenemann D., Mueller M.J.;
RT "DONGLE and DEFECTIVE IN ANTHER DEHISCENCE1 lipases are not essential for
RT wound- and pathogen-induced jasmonate biosynthesis: redundant lipases
RT contribute to jasmonate formation.";
RL Plant Physiol. 153:114-127(2010).
RN [9]
RP INDUCTION BY WOUNDING.
RX PubMed=24430866; DOI=10.1007/s00299-013-1561-8;
RA Rudus I., Terai H., Shimizu T., Kojima H., Hattori K., Nishimori Y.,
RA Tsukagoshi H., Kamiya Y., Seo M., Nakamura K., Kepczynski J., Ishiguro S.;
RT "Wound-induced expression of DEFECTIVE IN ANTHER DEHISCENCE1 and DAD1-like
RT lipase genes is mediated by both CORONATINE INSENSITIVE1-dependent and
RT independent pathways in Arabidopsis thaliana.";
RL Plant Cell Rep. 33:849-860(2014).
CC -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of
CC phosphatidylcholine at the sn-1 position. Has a strong galactolipase
CC activity toward monogalactosyldiacylglycerol (MGDG) and
CC digalactosyldiacylglycerol (DGDG). Low triacylglycerol (TAG) lipase
CC activity. Plays a role in plant growth and in leaf senescence.
CC {ECO:0000269|PubMed:17259290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-
CC sn-glycerol + H2O = a fatty acid + acyl-3-O-[alpha-D-galactosyl-
CC (1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28396,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90310;
CC Evidence={ECO:0000269|PubMed:19527719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373;
CC Evidence={ECO:0000269|PubMed:19527719};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + H2O = a
CC fatty acid + an acyl-3-O-(beta-D-galactosyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:57084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17615, ChEBI:CHEBI:28868, ChEBI:CHEBI:141434;
CC Evidence={ECO:0000269|PubMed:19527719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57085;
CC Evidence={ECO:0000269|PubMed:19527719};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:17259290, ECO:0000269|PubMed:19527719}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in flowers and
CC leaves. {ECO:0000269|PubMed:17259290, ECO:0000269|PubMed:19527719}.
CC -!- DEVELOPMENTAL STAGE: Induced during senescence.
CC {ECO:0000269|PubMed:17259290}.
CC -!- INDUCTION: Induced by wounding (PubMed:24430866). Not induced by
CC wounding (PubMed:18267087). {ECO:0000269|PubMed:18267087,
CC ECO:0000269|PubMed:24430866}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under standard growth
CC phenotype. {ECO:0000269|PubMed:20348210}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AC007071; AAD24845.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08573.1; -; Genomic_DNA.
DR EMBL; DQ056559; AAY78709.1; -; mRNA.
DR PIR; H84723; H84723.
DR RefSeq; NP_180727.1; NM_128726.1.
DR AlphaFoldDB; Q9SIN9; -.
DR SMR; Q9SIN9; -.
DR STRING; 3702.AT2G31690.1; -.
DR SwissLipids; SLP:000001922; -.
DR ESTHER; arath-PLA13; Plant_phospholipase.
DR PaxDb; Q9SIN9; -.
DR PRIDE; Q9SIN9; -.
DR EnsemblPlants; AT2G31690.1; AT2G31690.1; AT2G31690.
DR GeneID; 817725; -.
DR Gramene; AT2G31690.1; AT2G31690.1; AT2G31690.
DR KEGG; ath:AT2G31690; -.
DR Araport; AT2G31690; -.
DR TAIR; locus:2065873; AT2G31690.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_2_0_1; -.
DR InParanoid; Q9SIN9; -.
DR OMA; CPSRWIG; -.
DR OrthoDB; 612344at2759; -.
DR PhylomeDB; Q9SIN9; -.
DR BioCyc; ARA:AT2G31690-MON; -.
DR PRO; PR:Q9SIN9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIN9; baseline and differential.
DR Genevisible; Q9SIN9; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; IEA:UniProtKB-SubCell.
DR GO; GO:0047714; F:galactolipase activity; IDA:TAIR.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:TAIR.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:TAIR.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IDA:TAIR.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Lipid degradation; Lipid metabolism; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..484
FT /note="Phospholipase A1-Ialpha2, chloroplastic"
FT /id="PRO_0000398877"
FT MOTIF 295..299
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 297
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 411
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
SQ SEQUENCE 484 AA; 54924 MW; 74650CD21BB783D3 CRC64;
MALIQNPNMK HAPFLRNRSP QQTLFIPYTL SLPISYQNPK RLKTANSSSS SSLLAPVILN
SPVASSSPPP IYCAPKFPCS SGAATVPLSR VWREIQGCNN WKDLIEPLNP LLQQEITRYG
NLVSTCYKAF DLDPNSKRYL NCKYGKQTLL KETEIDQPED YQVTKYIYAT PDININISPI
QNEMNRRARW VGYVAASSDD SVKRLGRRDI VVTFRGTVTN PEWLANFMSS LTPARFHPHN
PRLDVKVESG FLSLYTSDES ESKFGLESCR QQLLSEISRL MNKYKGEEMS ITLAGHSMGS
SLAQLLAYDI AELGLNRRIG KGDIPVTVFS FAGPRVGNLE FKKRCEELGV KVLRITNVND
PVTKLPGVLF NENFRVLGGF YELPWSCSCY VHVGVELTLD FFDVQNISCV HDLQTYIDLL
NQRRTNSRSV DSDEDEDSDN VALEFLKTNG EKMMFLKRQR MMYWSNAVDL LFSFSNHMSY
CNIF
