PLA12_ARATH
ID PLA12_ARATH Reviewed; 471 AA.
AC Q9MA46;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Galactolipase DONGLE, chloroplastic {ECO:0000305};
DE EC=3.1.1.26 {ECO:0000269|PubMed:19527719};
DE EC=3.1.1.32 {ECO:0000269|PubMed:19527719};
DE AltName: Full=Phospholipase A1 DONGLE {ECO:0000303|PubMed:18267087};
DE AltName: Full=Phospholipase A1-Ialpha1 {ECO:0000303|PubMed:15130548};
DE Flags: Precursor;
GN Name=DGL {ECO:0000303|PubMed:18267087};
GN OrderedLocusNames=At1g05800 {ECO:0000312|Araport:AT1G05800};
GN ORFNames=T20M3.6 {ECO:0000312|EMBL:AAF29385.1};
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION BY WOUNDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [2]
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 [3]
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 [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 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY WOUNDING, AND DISRUPTION
RP 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 [7]
RP INDUCTION.
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: Sn-1-specific phospholipase that releases free fatty acids
CC from phosphatidylcholine. Has a higher galactolipase activity than
CC phospholipase A1 activity when digalactosyldiacylglycerol (DGDG) is
CC used as substrate. Catalyzes the initial step of jasmonic acid
CC biosynthesis. Required for the biosynthesis of basal-level endogenous
CC jasmonate in vegetative tissues. Regulates leaves growth. Not essential
CC for jasmonate biosynthesis after wounding or upon pathogen infection.
CC {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:20348210}.
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:19527719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190;
CC Evidence={ECO:0000269|PubMed:19527719};
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:19527719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000269|PubMed:19527719};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:18267087};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:19527719,
CC ECO:0000269|PubMed:20348210}. Note=PubMed:20348210 shows a localization
CC in lipid droplets.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and seedlings. Not detected in
CC flowers, siliques or roots. {ECO:0000269|PubMed:18267087,
CC ECO:0000269|PubMed:19527719}.
CC -!- INDUCTION: Induced by wounding (PubMed:18267087, PubMed:20348210,
CC PubMed:24430866). Induced by methyl jasmonate (PubMed:24430866).
CC {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:20348210,
CC ECO:0000269|PubMed:24430866}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under standard growth
CC phenotype. {ECO:0000269|PubMed:20348210}.
CC -!- MISCELLANEOUS: Overexpression of DGL causes a dwarf phenotype.
CC {ECO:0000269|PubMed:18267087}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; EU411040; ACA48222.1; -; Genomic_DNA.
DR EMBL; AC009999; AAF29385.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27895.1; -; Genomic_DNA.
DR PIR; E86192; E86192.
DR RefSeq; NP_563748.1; NM_100460.1.
DR AlphaFoldDB; Q9MA46; -.
DR SMR; Q9MA46; -.
DR STRING; 3702.AT1G05800.1; -.
DR SwissLipids; SLP:000001923; -.
DR ESTHER; arath-PLA12; Plant_phospholipase.
DR PaxDb; Q9MA46; -.
DR PRIDE; Q9MA46; -.
DR EnsemblPlants; AT1G05800.1; AT1G05800.1; AT1G05800.
DR GeneID; 837089; -.
DR Gramene; AT1G05800.1; AT1G05800.1; AT1G05800.
DR KEGG; ath:AT1G05800; -.
DR Araport; AT1G05800; -.
DR TAIR; locus:2198728; AT1G05800.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_2_0_1; -.
DR InParanoid; Q9MA46; -.
DR OMA; KWIGYIA; -.
DR OrthoDB; 612344at2759; -.
DR PhylomeDB; Q9MA46; -.
DR BioCyc; ARA:AT1G05800-MON; -.
DR PRO; PR:Q9MA46; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MA46; baseline and differential.
DR Genevisible; Q9MA46; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005811; C:lipid droplet; IDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP: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..88
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 89..471
FT /note="Galactolipase DONGLE, chloroplastic"
FT /id="PRO_0000398876"
FT REGION 44..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 284..288
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 286
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 400
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
SQ SEQUENCE 471 AA; 52800 MW; 3D1ADE6CE98CF1A4 CRC64;
MAAKVFTQNP IYSQSLVRDK TPQQKHNLDH FSISQHTSKR LVVSSSTMSP PISSSPLSLP
SSSSSQAIPP SRAPAVTLPL SRVWREIQGS NNWENLIEPL SPILQQEITR YGNLLSASYK
GFDLNPNSKR YLSCKYGKKN LLKESGIHDP DGYQVTKYIY ATPDINLNPI KNEPNRARWI
GYVAVSSDES VKRLGRRDIL VTFRGTVTNH EWLANLKSSL TPARLDPHNP RPDVKVESGF
LGLYTSGESE SKFGLESCRE QLLSEISRLM NKHKGEEISI TLAGHSMGSS LAQLLAYDIA
ELGMNQRRDE KPVPVTVFSF AGPRVGNLGF KKRCEELGVK VLRITNVNDP ITKLPGFLFN
ENFRSLGGVY ELPWSCSCYT HVGVELTLDF FDVQNISCVH DLETYITLVN RPRCSKLAVN
EDNFGGEFLN RTSELMFSKG RRQALHFTNA ATNAAYLLCS ISNHMLYYNI F
