PLA11_ARATH
ID PLA11_ARATH Reviewed; 447 AA.
AC Q948R1; F4IV22; O22170;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phospholipase A(1) DAD1, chloroplastic {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000269|PubMed:11595796, ECO:0000269|PubMed:19527719};
DE AltName: Full=Phospholipase A1-Ibeta1 {ECO:0000303|PubMed:15130548};
DE AltName: Full=Protein DEFECTIVE IN ANTHER DEHISCENCE 1 {ECO:0000303|PubMed:11595796};
DE Short=AtDAD1 {ECO:0000303|PubMed:11595796};
DE Flags: Precursor;
GN Name=DAD1 {ECO:0000303|PubMed:11595796};
GN OrderedLocusNames=At2g44810 {ECO:0000312|Araport:AT2G44810};
GN ORFNames=T13E15.18 {ECO:0000312|Araport:AT2G44810};
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, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INDUCTION BY WOUNDING, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11595796; DOI=10.2307/3871502;
RA Ishiguro S., Kawai-Oda A., Ueda J., Nishida I., Okada K.;
RT "The DEFECTIVE IN ANTHER DEHISCIENCE gene encodes a novel phospholipase A1
RT catalyzing the initial step of jasmonic acid biosynthesis, which
RT synchronizes pollen maturation, anther dehiscence, and flower opening in
RT Arabidopsis.";
RL Plant Cell 13:2191-2209(2001).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 77-447.
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 [5]
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 [6]
RP REGULATION.
RX PubMed=17981996; DOI=10.1105/tpc.107.055467;
RA Ito T., Ng K.H., Lim T.S., Yu H., Meyerowitz E.M.;
RT "The homeotic protein AGAMOUS controls late stamen development by
RT regulating a jasmonate biosynthetic gene in Arabidopsis.";
RL Plant Cell 19:3516-3529(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP WOUNDING.
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 [8]
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 [9]
RP FUNCTION, AND INDUCTION BY WOUNDING.
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 [10]
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 phospholipids. Low activity on galactolipids and triacylglycerols.
CC Catalyzes the initial step of jasmonic acid biosynthesis. Not essential
CC for jasmonate biosynthesis after wounding or upon pathogen infection.
CC {ECO:0000269|PubMed:11595796, ECO:0000269|PubMed:18267087,
CC ECO:0000269|PubMed:20348210}.
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:11595796, ECO:0000269|PubMed:19527719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000269|PubMed:11595796, ECO:0000269|PubMed:19527719};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:73002, ChEBI:CHEBI:76084;
CC Evidence={ECO:0000269|PubMed:11595796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC Evidence={ECO:0000269|PubMed:11595796};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:11595796};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11595796, ECO:0000269|PubMed:18267087,
CC ECO:0000269|PubMed:19527719}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds, but not in leaves or
CC roots. Restricted to the stamen filaments immediately before flower
CC opening. {ECO:0000269|PubMed:11595796, ECO:0000269|PubMed:18267087,
CC ECO:0000269|PubMed:19527719}.
CC -!- INDUCTION: Induced by wounding (PubMed:11595796, PubMed:18267087,
CC PubMed:20348210, PubMed:24430866). Induced by methyl jasmonate
CC (PubMed:24430866). {ECO:0000269|PubMed:11595796,
CC ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:20348210,
CC ECO:0000269|PubMed:24430866}.
CC -!- DISRUPTION PHENOTYPE: Defective in anther dehiscence and pollen
CC maturation. Delayed flower buds opening. {ECO:0000269|PubMed:11595796}.
CC -!- MISCELLANEOUS: Directly regulated at the transcription level by the
CC floral homeotic gene AGAMOUS. {ECO:0000269|PubMed:17981996}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC31843.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL69449.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM14879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEC10469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB060156; BAB69954.1; -; Genomic_DNA.
DR EMBL; AC002388; AAC31843.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC003672; AAM14879.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC10469.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; ANM62456.1; -; Genomic_DNA.
DR EMBL; AY074633; AAL69449.1; ALT_INIT; mRNA.
DR PIR; T00412; T01607.
DR RefSeq; NP_001324613.1; NM_001337097.1.
DR RefSeq; NP_182008.1; NM_130045.4.
DR AlphaFoldDB; Q948R1; -.
DR SMR; Q948R1; -.
DR STRING; 3702.AT2G44810.1; -.
DR SwissLipids; SLP:000001795; -.
DR ESTHER; arath-PLA11; Plant_phospholipase.
DR PaxDb; Q948R1; -.
DR PRIDE; Q948R1; -.
DR EnsemblPlants; AT2G44810.2; AT2G44810.2; AT2G44810.
DR GeneID; 819090; -.
DR Gramene; AT2G44810.2; AT2G44810.2; AT2G44810.
DR KEGG; ath:AT2G44810; -.
DR Araport; AT2G44810; -.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_2_0_1; -.
DR InParanoid; Q948R1; -.
DR OrthoDB; 612344at2759; -.
DR PhylomeDB; Q948R1; -.
DR BioCyc; MetaCyc:AT2G44810-MON; -.
DR BRENDA; 3.1.1.32; 399.
DR PRO; PR:Q948R1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q948R1; baseline and differential.
DR Genevisible; Q948R1; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
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:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Lipid degradation; Lipid metabolism; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..447
FT /note="Phospholipase A(1) DAD1, chloroplastic"
FT /id="PRO_0000398875"
FT MOTIF 293..297
FT /note="GXSXG"
FT /evidence="ECO:0000305|PubMed:19527719"
FT ACT_SITE 295
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305|PubMed:19527719"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:19527719"
FT ACT_SITE 418
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:19527719"
SQ SEQUENCE 447 AA; 49960 MW; 0EA3ABFD6545B5A1 CRC64;
MRFSLSPVRP HSVVVPSLPK QDVVSYISGT TSNRQCRCVL TLPSPSVSTS RPPVLPKPET
WESLLLNHDQ IPGEFSPTGS SIPVKLGRRW MEYQGLQNWD GLLDPLDDNL RREILRYGQF
VESAYQAFDF DPSSPTYGTC RFPRSTLLER SGLPNSGYRL TKNLRATSGI NLPRWIEKAP
SWMATQSSWI GYVAVCQDKE EISRLGRRDV VISFRGTATC LEWLENLRAT LTHLPNGPTG
ANLNGSNSGP MVESGFLSLY TSGVHSLRDM VREEIARLLQ SYGDEPLSVT ITGHSLGAAI
ATLAAYDIKT TFKRAPMVTV ISFGGPRVGN RCFRKLLEKQ GTKVLRIVNS DDVITKVPGV
VLENREQDNV KMTASIMPSW IQRRVEETPW VYAEIGKELR LSSRDSPHLS SINVATCHEL
KTYLHLVDGF VSSTCPFRET ARRVLHR
