PLA16_ARATH
ID PLA16_ARATH Reviewed; 529 AA.
AC Q3EBR6; O04340;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phospholipase A1-Igamma2, chloroplastic {ECO:0000303|PubMed:15130548};
DE EC=3.1.1.- {ECO:0000269|PubMed:19527719};
DE AltName: Full=DAD1-like lipase 3 {ECO:0000303|PubMed:24430866};
DE Flags: Precursor;
GN Name=DALL3 {ECO:0000303|PubMed:24430866};
GN OrderedLocusNames=At2g30550 {ECO:0000312|Araport:AT2G30550};
GN ORFNames=T6B20.10 {ECO:0000312|EMBL:AAB63082.2};
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] (ISOFORM 1).
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] (ISOFORM 1).
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 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 INDUCTION BY 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 [7]
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 [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).
RN [10]
RP INTERACTION WITH SBP1, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=31928671; DOI=10.1016/j.plantsci.2019.110357;
RA Dervisi I., Valassakis C., Agalou A., Papandreou N., Podia V.,
RA Haralampidis K., Iconomidou V.A., Kouvelis V.N., Spaink H.P., Roussis A.;
RT "Investigation of the interaction of DAD1-LIKE LIPASE 3 (DALL3) with
RT Selenium Binding Protein 1 (SBP1) in Arabidopsis thaliana.";
RL Plant Sci. 291:110357-110357(2020).
CC -!- FUNCTION: Acylhydrolase with broad specificity (PubMed:19527719).
CC Catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position
CC (PubMed:19527719). Possesses moderate activity toward
CC phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG),
CC digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG)
CC (PubMed:19527719). {ECO:0000269|PubMed:19527719}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000269|PubMed:19527719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000269|PubMed:19527719};
CC -!- SUBUNIT: Interacts with SBP1. {ECO:0000269|PubMed:31928671}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19527719, ECO:0000269|PubMed:31928671}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3EBR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3EBR6-2; Sequence=VSP_039821, VSP_039822;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:19527719). Highly
CC expressed in leaves and stems (PubMed:19527719).
CC {ECO:0000269|PubMed:19527719}.
CC -!- INDUCTION: Slightly induced by wounding (PubMed:18267087). Induced by
CC wounding (PubMed:24430866, PubMed:31928671). Induced by cadmium and
CC selenium in roots (PubMed:31928671). {ECO:0000269|PubMed:18267087,
CC ECO:0000269|PubMed:24430866, ECO:0000269|PubMed:31928671}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {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; U93215; AAB63082.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08407.1; -; Genomic_DNA.
DR EMBL; AY091143; AAM14092.1; -; mRNA.
DR EMBL; AY142594; AAN13163.1; -; mRNA.
DR EMBL; AY086021; AAM63231.1; -; mRNA.
DR PIR; G84709; G84709.
DR RefSeq; NP_565701.1; NM_128607.4. [Q3EBR6-1]
DR AlphaFoldDB; Q3EBR6; -.
DR SMR; Q3EBR6; -.
DR STRING; 3702.AT2G30550.2; -.
DR SwissLipids; SLP:000001920; -. [Q3EBR6-1]
DR ESTHER; arath-PLA16; Plant_phospholipase.
DR PaxDb; Q3EBR6; -.
DR PRIDE; Q3EBR6; -.
DR ProteomicsDB; 236165; -. [Q3EBR6-1]
DR EnsemblPlants; AT2G30550.2; AT2G30550.2; AT2G30550. [Q3EBR6-1]
DR GeneID; 817604; -.
DR Gramene; AT2G30550.2; AT2G30550.2; AT2G30550. [Q3EBR6-1]
DR KEGG; ath:AT2G30550; -.
DR Araport; AT2G30550; -.
DR TAIR; locus:2064321; AT2G30550.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_0_0_1; -.
DR InParanoid; Q3EBR6; -.
DR OrthoDB; 612344at2759; -.
DR PhylomeDB; Q3EBR6; -.
DR BioCyc; ARA:AT2G30550-MON; -.
DR PRO; PR:Q3EBR6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q3EBR6; baseline and differential.
DR Genevisible; Q3EBR6; 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..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..529
FT /note="Phospholipase A1-Igamma2, chloroplastic"
FT /id="PRO_0000398880"
FT MOTIF 316..320
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 318
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 381
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 437
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT VAR_SEQ 450..464
FT /note="HGKGERFVLSSGRDH -> VSFLFYFSLFIYS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039821"
FT VAR_SEQ 465..529
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039822"
SQ SEQUENCE 529 AA; 60402 MW; 2F02B3C51953B020 CRC64;
MAAIPSHNNL LTINHKNSIT GSSSLNTNFS EINFPAKFRV ATRALSRTDE SSLSAVISRL
ERERRERQGL LIEEAEGAGE LWMTAEDIRR RDKKTEEERR LRDTWRKIQG EDDWAGLMDP
MDPILRSELI RYGEMAQACY DAFDFDPASK YCGTSRFTRL EFFDSLGMID SGYEVARYLY
ATSNINLPNF FSKSRWSKVW SKNANWMGYV AVSDDETSRN RLGRRDIAIA WRGTVTKLEW
IADLKDYLKP VTENKIRCPD PAVKVESGFL DLYTDKDTTC KFARFSAREQ ILTEVKRLVE
EHGDDDDSDL SITVTGHSLG GALAILSAYD IAEMRLNRSK KGKVIPVTVL TYGGPRVGNV
RFRERMEELG VKVMRVVNVH DVVPKSPGLF LNESRPHALM KIAEGLPWCY SHVGEELALD
HQNSPFLKPS VDVSTAHNLE AMLHLLDGYH GKGERFVLSS GRDHALVNKA SDFLKEHLQI
PPFWRQDANK GMVRNSEGRW IQAERLRFED HHSPDIHHHL SQLRLDHPC
