PLA17_ARATH
ID PLA17_ARATH Reviewed; 527 AA.
AC Q9C8J6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phospholipase A1-Igamma3, chloroplastic {ECO:0000303|PubMed:15130548};
DE EC=3.1.1.- {ECO:0000269|PubMed:19527719};
DE AltName: Full=DAD1-like lipase 2 {ECO:0000303|PubMed:24430866};
DE Flags: Precursor;
GN Name=DALL2 {ECO:0000303|PubMed:24430866};
GN OrderedLocusNames=At1g51440 {ECO:0000312|Araport:AT1G51440};
GN ORFNames=F5D21.19 {ECO:0000312|EMBL:AAG52635.1};
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=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].
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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.
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, 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. Moderate activity toward
CC phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG),
CC digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG).
CC {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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19527719}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers. Lower levels in
CC seedlings, leaves and stems. {ECO:0000269|PubMed:19527719}.
CC -!- INDUCTION: Not induced by wounding (PubMed:18267087). Slightly induced
CC by wounding (PubMed:24430866). {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; AC024261; AAG52635.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32668.1; -; Genomic_DNA.
DR EMBL; AF424572; AAL11566.1; -; mRNA.
DR EMBL; AY142023; AAM98287.1; -; mRNA.
DR EMBL; AK226962; BAE99030.1; -; mRNA.
DR PIR; F96552; F96552.
DR RefSeq; NP_564590.1; NM_104022.5.
DR AlphaFoldDB; Q9C8J6; -.
DR SMR; Q9C8J6; -.
DR STRING; 3702.AT1G51440.1; -.
DR SwissLipids; SLP:000001921; -.
DR ESTHER; arath-PLA17; Plant_phospholipase.
DR PaxDb; Q9C8J6; -.
DR PRIDE; Q9C8J6; -.
DR ProteomicsDB; 235067; -.
DR EnsemblPlants; AT1G51440.1; AT1G51440.1; AT1G51440.
DR GeneID; 841569; -.
DR Gramene; AT1G51440.1; AT1G51440.1; AT1G51440.
DR KEGG; ath:AT1G51440; -.
DR Araport; AT1G51440; -.
DR TAIR; locus:2033959; AT1G51440.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_1_0_1; -.
DR InParanoid; Q9C8J6; -.
DR OMA; YCGTCKY; -.
DR OrthoDB; 612344at2759; -.
DR PhylomeDB; Q9C8J6; -.
DR BioCyc; ARA:AT1G51440-MON; -.
DR PRO; PR:Q9C8J6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8J6; baseline and differential.
DR Genevisible; Q9C8J6; 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 Chloroplast; Hydrolase; Lipid degradation; Lipid metabolism; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..527
FT /note="Phospholipase A1-Igamma3, chloroplastic"
FT /id="PRO_0000398881"
FT REGION 55..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 300..304
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT COMPBIAS 65..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 302
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 423
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
SQ SEQUENCE 527 AA; 60321 MW; 2161452F6CF71A92 CRC64;
MASLSLPITL KNPRFFSSSP QNIFKTQPQT LVLTTKFKTC SIICSSSCTS ISSSTTQQKQ
SNKQTHVSDN KREEKAEEEE EEKEVSLREI WREVQGCNNW EGQLDPMNNH LRREIIRYGE
FAQACYDSFD FDPHSKYCGS CKYHPSDFFL NLDLHLHKGY TITRYLYATS NINLPNFFQK
SKLSSIWSQH ANWMGFVAVA TDEEEVSRLG RRDIVIAWRG TVTYLEWIYD LKDILCSANF
GDDPSIKIEL GFHDLYTKKE DSCKFSSFSA REQVLAEVKR LIEYYGTEEE GHKTSITVTG
HSLGASLALV SAYDIAELNL NHVPENNYKI PITVFSFSGP RVGNLRFKER CDELGVKVLR
VVNVHDKVPS VPGIFTNEKF QFQKYVEEKT SFPWSYAHVG VELALDHKKS PFLKPTKDLG
CAHNLEALLH LVDGYHGKDE EAEKRFCLVT KRDIALVNKS CDFLRGEYHV PPCWRQDENK
GMVKNGDGQW VLPDRPLLEP HGPEDIAHHL QQVLGKVNDD NFKPTTT
