PLA2D_ARATH
ID PLA2D_ARATH Reviewed; 191 AA.
AC Q8GV50; Q9M0D6;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Phospholipase A2-delta;
DE EC=3.1.1.4;
DE AltName: Full=Secretory phospholipase A2-delta;
DE Short=AtsPLA2-delta;
DE Flags: Precursor;
GN Name=PLA2-DELTA; OrderedLocusNames=At4g29470; ORFNames=F17A13.290;
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 [MRNA].
RA Bahn S.C., Kim H.J., Lee H.Y., Ryu S.B., Shin J.S.;
RT "Cloning and Characterization of Arabidopsis thaliana putative secretory
RT low molecular weight phospholipase A2 isoforms.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) 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 TISSUE SPECIFICITY.
RX PubMed=15748654; DOI=10.1016/j.plipres.2004.10.002;
RA Lee H.Y., Bahn S.C., Shin J.S., Hwang I., Back K., Doelling J.H., Ryu S.B.;
RT "Multiple forms of secretory phospholipase A2 in plants.";
RL Prog. Lipid Res. 44:52-67(2005).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=21278126; DOI=10.1105/tpc.110.074799;
RA Kim H.J., Ok S.H., Bahn S.C., Jang J., Oh S.A., Park S.K., Twell D.,
RA Ryu S.B., Shin J.S.;
RT "Endoplasmic reticulum- and Golgi-localized phospholipase A2 plays critical
RT roles in Arabidopsis pollen development and germination.";
RL Plant Cell 23:94-110(2011).
CC -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and
CC free fatty acids (FFAs) from membrane phospholipids in response to
CC hormones and other external stimuli. Plays a role in pollen development
CC and germination and tube growth. {ECO:0000269|PubMed:21278126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10035};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:21278126}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in flowers but at a low
CC level. Detected specifically in the pollen.
CC {ECO:0000269|PubMed:15748654, ECO:0000269|PubMed:21278126}.
CC -!- DEVELOPMENTAL STAGE: Expressed during pollen germination and tube
CC growth. {ECO:0000269|PubMed:21278126}.
CC -!- MISCELLANEOUS: The enzyme has a slight preference for
CC phosphatidylethanolamine over phosphatidylcholine.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB79705.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY148347; AAN63045.1; -; mRNA.
DR EMBL; AL161575; CAB79705.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85635.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66586.1; -; Genomic_DNA.
DR EMBL; AB493706; BAH30544.1; -; mRNA.
DR PIR; H85343; H85343.
DR RefSeq; NP_001328472.1; NM_001341968.1.
DR RefSeq; NP_194676.2; NM_119092.3.
DR AlphaFoldDB; Q8GV50; -.
DR SMR; Q8GV50; -.
DR STRING; 3702.AT4G29470.1; -.
DR PaxDb; Q8GV50; -.
DR PRIDE; Q8GV50; -.
DR ProteomicsDB; 235064; -.
DR EnsemblPlants; AT4G29470.1; AT4G29470.1; AT4G29470.
DR EnsemblPlants; AT4G29470.2; AT4G29470.2; AT4G29470.
DR GeneID; 829068; -.
DR Gramene; AT4G29470.1; AT4G29470.1; AT4G29470.
DR Gramene; AT4G29470.2; AT4G29470.2; AT4G29470.
DR KEGG; ath:AT4G29470; -.
DR Araport; AT4G29470; -.
DR TAIR; locus:2118359; AT4G29470.
DR eggNOG; ENOG502RZIE; Eukaryota.
DR HOGENOM; CLU_115623_1_0_1; -.
DR InParanoid; Q8GV50; -.
DR OMA; CHKQFQR; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q8GV50; -.
DR BioCyc; ARA:AT4G29470-MON; -.
DR PRO; PR:Q8GV50; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GV50; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IDA:UniProtKB.
DR GO; GO:0009860; P:pollen tube growth; IDA:UniProtKB.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Endoplasmic reticulum; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..191
FT /note="Phospholipase A2-delta"
FT /id="PRO_0000417564"
FT REGION 161..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 29..56
FT /evidence="ECO:0000250"
FT DISULFID 33..62
FT /evidence="ECO:0000250"
FT DISULFID 38..115
FT /evidence="ECO:0000250"
FT DISULFID 49..69
FT /evidence="ECO:0000250"
FT DISULFID 68..93
FT /evidence="ECO:0000250"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
SQ SEQUENCE 191 AA; 20617 MW; 3E6F729E288CB149 CRC64;
MIRGGALTHV ALGLTVFLLL AVVHSQEKCS KTCIAQKCNV LGIRYGKYCG IGYFGCPGEP
PCDDLDDCCM THDNCVDLKG MTYVDCHKQF QRCVNELKQS IQESNNQKVG FSKECPYSTV
IPTVYRGMNY GIFFSGIGNI IIPKKPASAG PVVEVDLARS KADTKDGLGT NQGPQTKDGS
KVSVPMNPSP S
