PLA14_ARATH
ID PLA14_ARATH Reviewed; 517 AA.
AC O23522; F4JML8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phospholipase A1-Ibeta2, chloroplastic;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=At4g16820; ORFNames=dl4435w, FCAALL.42;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-43, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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, 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 SUBCELLULAR LOCATION, 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).
CC -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of
CC phosphatidylcholine at the sn-1 position. Has a strong galactolipase
CC activity toward digalactosyldiacylglycerol (DGDG). Hydrolyzes
CC triacylglycerol (TAG), but has a low activity toward
CC phosphatidylcholine (PC) and monogalactosyldiacylglycerol (MGDG).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Hihgest expression in flowers and
CC seedlings. {ECO:0000269|PubMed:19527719}.
CC -!- INDUCTION: Not induced by wounding. {ECO:0000269|PubMed:18267087}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10455.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80953.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97342; CAB10455.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161545; CAB80953.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83808.1; -; Genomic_DNA.
DR PIR; E71435; E71435.
DR RefSeq; NP_567515.1; NM_117784.2.
DR AlphaFoldDB; O23522; -.
DR SMR; O23522; -.
DR STRING; 3702.AT4G16820.1; -.
DR ESTHER; arath-AT4G16820; Plant_phospholipase.
DR iPTMnet; O23522; -.
DR PaxDb; O23522; -.
DR PRIDE; O23522; -.
DR EnsemblPlants; AT4G16820.1; AT4G16820.1; AT4G16820.
DR GeneID; 827388; -.
DR Gramene; AT4G16820.1; AT4G16820.1; AT4G16820.
DR KEGG; ath:AT4G16820; -.
DR Araport; AT4G16820; -.
DR TAIR; locus:2129181; AT4G16820.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_3_1_1; -.
DR InParanoid; O23522; -.
DR OMA; PNADMAC; -.
DR OrthoDB; 612344at2759; -.
DR BioCyc; ARA:AT4G16820-MON; -.
DR PRO; PR:O23522; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23522; baseline and differential.
DR Genevisible; O23522; 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; Isopeptide bond; Lipid degradation;
KW Lipid metabolism; Plastid; Reference proteome; Transit peptide;
KW Ubl conjugation.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..517
FT /note="Phospholipase A1-Ibeta2, chloroplastic"
FT /id="PRO_0000398878"
FT ACT_SITE 327
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255"
FT ACT_SITE 384
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 451
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 517 AA; 57640 MW; A18EA5AE738459E0 CRC64;
MQTLTPNADI FHAKRRRFTC NTHTSTLIPT KPLSVSPARK TNKEHLRNLE NVLRTSSNSI
DHIENVTSRQ EKTTKNTSTS SLLGGLNLAR IWPQMKAAVD EMSPKNLKRL QRLLSKSSEE
RSPKSKLGSK WRELHGLNNW AGLLDPLDEN LRRELVRYGE FVQAAYHAFH SDPEGSPRHV
ALPDGSFKVT KSLYATSSVR LPKWIDDVAP DLRWMTKQTS WVGYVAVCDD PREIRRMGRR
EIVIALRGTA TLLEWSENFR PNLVSMPEPK PDQSDPTRPK VECGFNSLYT TGDQHAPSLA
ESLVGEISRL VELYAGEELS ISVTGHSLGA AIALLAADDI AERVPHAPPV AVFSFGGPRV
GNREFADRLD SKGVKVLRVV NSQDVVTKVP GIFADNDKQG QSRNNGRSPG GIMEMVERNN
PWAYSHVGAE LRVDMKMSPY LKPNADVACC HDLEAYLHLV DGFLASNCPF RANAKRSLRK
LLDEQRSNVK VLYTGKSLRL NRTFHDNGDV LPSPSSS
