PLA15_ARATH
ID PLA15_ARATH Reviewed; 515 AA.
AC Q941F1; Q9M9Y7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phospholipase A1-Igamma1, chloroplastic {ECO:0000303|PubMed:15130548};
DE EC=3.1.1.-;
DE AltName: Full=DAD1-like lipase 4 {ECO:0000303|PubMed:24430866};
DE Flags: Precursor;
GN Name=DALL4 {ECO:0000303|PubMed:24430866};
GN OrderedLocusNames=At1g06800 {ECO:0000312|Araport:AT1G06800};
GN ORFNames=F4H5.11, F4H5_10;
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=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 [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] (ISOFORMS 1 AND 2).
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 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 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 [6]
RP CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP ALTERNATIVE SPLICING.
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 [7]
RP FUNCTION, AND 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 [8]
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 with a broad specificity. Catalyzes the
CC hydrolysis of phosphatidylcholine at the sn-1 position. Moderate
CC activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol
CC (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG).
CC May display dual sn-1/sn-2 substrate specificity. Could be involved in
CC early wound response. {ECO:0000269|PubMed:19527719,
CC ECO:0000269|PubMed:20348210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000269|PubMed:19527719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488;
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 -!- 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19527719}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q941F1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q941F1-2; Sequence=VSP_039819, VSP_039820;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in leaves.
CC {ECO:0000269|PubMed:19527719}.
CC -!- INDUCTION: Not induced by wounding (PubMed:18267087). Induced by
CC wounding (PubMed:24430866). {ECO:0000269|PubMed:18267087,
CC ECO:0000269|PubMed:24430866}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under standard growth
CC phenotype. Decreased dinor-12-oxo-phytodienoic acid (dnOPDA) formation.
CC {ECO:0000269|PubMed:20348210}.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AC011001; AAF63138.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28039.1; -; Genomic_DNA.
DR EMBL; AY099599; AAM20450.1; -; mRNA.
DR EMBL; AY052199; AAK97670.1; -; mRNA.
DR EMBL; BT002718; AAO11634.1; -; mRNA.
DR PIR; H86202; H86202.
DR RefSeq; NP_563772.1; NM_100557.2.
DR RefSeq; NP_849603.1; NM_179272.2. [Q941F1-1]
DR AlphaFoldDB; Q941F1; -.
DR SMR; Q941F1; -.
DR STRING; 3702.AT1G06800.1; -.
DR SwissLipids; SLP:000001919; -. [Q941F1-1]
DR ESTHER; arath-PLA15; Plant_phospholipase.
DR PaxDb; Q941F1; -.
DR PRIDE; Q941F1; -.
DR ProteomicsDB; 234964; -. [Q941F1-1]
DR EnsemblPlants; AT1G06800.1; AT1G06800.1; AT1G06800. [Q941F1-1]
DR GeneID; 837191; -.
DR Gramene; AT1G06800.1; AT1G06800.1; AT1G06800. [Q941F1-1]
DR KEGG; ath:AT1G06800; -.
DR Araport; AT1G06800; -.
DR TAIR; locus:2033066; AT1G06800.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_0_0_1; -.
DR InParanoid; Q941F1; -.
DR OrthoDB; 612344at2759; -.
DR PhylomeDB; Q941F1; -.
DR BioCyc; ARA:AT1G06800-MON; -.
DR PRO; PR:Q941F1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q941F1; baseline and differential.
DR Genevisible; Q941F1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
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: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 Alternative splicing; Chloroplast; Hydrolase; Lipid degradation;
KW Lipid metabolism; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..515
FT /note="Phospholipase A1-Igamma1, chloroplastic"
FT /id="PRO_0000398879"
FT MOTIF 301..305
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 303
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 366
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 422
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT VAR_SEQ 434..444
FT /note="YHGKGQRFVLS -> SVILLFITF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_039819"
FT VAR_SEQ 445..515
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_039820"
SQ SEQUENCE 515 AA; 58445 MW; DD59442CB9166451 CRC64;
MATIPSHNLR PHTTNQRTQY SLSFRPHFSR STLITFPARS SPARAMSRTD EEASISTRLE
QESYGLTTAE DIRRRDGEAK ESKRLRDTWR KIQGEDDWAG LMDPMDPVLR SELIRYGEMA
QACYDAFDFD PFSRYCGSCR FTRRHLFDSL GIIDSGYEVA RYLYATSNIN LPNFFSKSRW
SKVWSKNANW MGYVAVSDDN EATRCRLGRR DIAIAWRGTV TRLEWIADLK DFLKPVSGNG
FRCPDPAVKA ESGFLDLYTD KDTSCNFSKF SAREQVLTEV KRLVERYGDE EGEELSITVT
GHSLGGALAV LSAYDVAEMG VNRTRKGKVI PVTAFTYGGP RVGNIRFKER IEKLGVKVLR
VVNEHDVVAK SPGLFLNERA PQALMKLAGG LPWCYSHVGE MLPLDHQKSP FLKPTVDLST
AHNLEALLHL LDGYHGKGQR FVLSSGRDPA LVNKASDFLK DHFMVPPYWR QDANKGMVRN
TDGRWIQPDR IRADDQHAPD IHQLLTQLHH PSQLL
