PLA2A_ARATH
ID PLA2A_ARATH Reviewed; 148 AA.
AC Q8S8N6;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phospholipase A2-alpha {ECO:0000303|PubMed:16140037};
DE EC=3.1.1.4 {ECO:0000269|PubMed:16140037};
DE AltName: Full=Secretory phospholipase A2-alpha;
DE Short=AtsPLA2-alpha;
DE Flags: Precursor;
GN Name=PLA2-ALPHA {ECO:0000303|PubMed:16140037};
GN OrderedLocusNames=At2g06925 {ECO:0000312|Araport:AT2G06925};
GN ORFNames=T4E14.19 {ECO:0000312|EMBL:AAM15017.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16140037; DOI=10.1016/j.bbalip.2005.08.005;
RA Ryu S.B., Lee H.Y., Doelling J.H., Palta J.P.;
RT "Characterization of a cDNA encoding Arabidopsis secretory phospholipase
RT A2-alpha, an enzyme that generates bioactive lysophospholipids and free
RT fatty acids.";
RL Biochim. Biophys. Acta 1736:144-151(2005).
RN [2]
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 [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].
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 [5]
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
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 [8]
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 [9]
RP MUTAGENESIS OF HIS-82; ASP-83 AND SER-99.
RX PubMed=16669612; DOI=10.1021/bi052563z;
RA Mansfeld J., Gebauer S., Dathe K., Ulbrich-Hofmann R.;
RT "Secretory phospholipase A2 from Arabidopsis thaliana: insights into the
RT three-dimensional structure and the amino acids involved in catalysis.";
RL Biochemistry 45:5687-5694(2006).
RN [10]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17692835; DOI=10.1016/j.chemphyslip.2007.07.001;
RA Mansfeld J., Ulbrich-Hofmann R.;
RT "Secretory phospholipase A2-alpha from Arabidopsis thaliana: functional
RT parameters and substrate preference.";
RL Chem. Phys. Lipids 150:156-166(2007).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20525850; DOI=10.1105/tpc.110.074211;
RA Lee O.R., Kim S.J., Kim H.J., Hong J.K., Ryu S.B., Lee S.H., Ganguly A.,
RA Cho H.T.;
RT "Phospholipase A(2) is required for PIN-FORMED protein trafficking to the
RT plasma membrane in the Arabidopsis root.";
RL Plant Cell 22:1812-1825(2010).
RN [12]
RP FUNCTION, INTERACTION WITH MYB30, INDUCTION BY PATHOGEN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20696912; DOI=10.1073/pnas.1009056107;
RA Froidure S., Canonne J., Daniel X., Jauneau A., Briere C., Roby D.,
RA Rivas S.;
RT "AtsPLA2-alpha nuclear relocalization by the Arabidopsis transcription
RT factor AtMYB30 leads to repression of the plant defense response.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15281-15286(2010).
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. Modulates the trafficking of PIN
CC proteins to the plasma membrane (PubMed:16140037, PubMed:20525850).
CC Negatively regulates MYB30 transcriptional activity and hypersensitive
CC response control (PubMed:20696912). {ECO:0000269|PubMed:16140037,
CC ECO:0000269|PubMed:20525850, ECO:0000269|PubMed:20696912}.
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:0000269|PubMed:16140037};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=15.3 umol/min/mg enzyme toward Dioleolyl-phosphoethanolamine (in
CC the presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=9.9 umol/min/mg enzyme toward DOPG (in the presence of 10 mM
CC Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=16.7 umol/min/mg enzyme toward Dioleolyl-phosphocholine (in the
CC presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=19.5 umol/min/mg enzyme toward Dilinoleoyl-phosphocholine (in
CC the presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=20.6 umol/min/mg enzyme toward Dipalmitoyl-phosphocholine (in
CC the presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=27.3 umol/min/mg enzyme toward Dimyristoyl-phosphocholine (in
CC the presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=29.3 umol/min/mg enzyme toward Dilauroyl-phosphocholine (in the
CC presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=35.5 umol/min/mg enzyme toward Didecanoyl-phosphocholine (in the
CC presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=14.4 umol/min/mg enzyme toward Dioctanoyl-phosphocholine (in the
CC presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=5.9 umol/min/mg enzyme toward Diheptanoyl-phosphocholine (in the
CC presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC Vmax=1.1 umol/min/mg enzyme toward Dihexanoyl-phosphocholine (in the
CC presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
CC pH dependence:
CC Optimum pH is 8.5-9. {ECO:0000269|PubMed:17692835};
CC Temperature dependence:
CC Optimum temperature is 30-40 degrees Celsius.
CC {ECO:0000269|PubMed:17692835};
CC -!- SUBUNIT: Interacts with MYB30. {ECO:0000269|PubMed:20696912}.
CC -!- INTERACTION:
CC Q8S8N6; Q9SCU7: MYB30; NbExp=4; IntAct=EBI-15869996, EBI-4466599;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20696912}. Golgi
CC apparatus {ECO:0000269|PubMed:20525850}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:20696912}. Nucleus {ECO:0000269|PubMed:20696912}.
CC Note=Relocalization from cytoplasmic vesicles to nucleus is MYB30-
CC mediated. {ECO:0000269|PubMed:20696912}.
CC -!- TISSUE SPECIFICITY: Ubiquitous but expressed at a low level.
CC {ECO:0000269|PubMed:15748654, ECO:0000269|PubMed:16140037}.
CC -!- INDUCTION: Induced 6 hours post pathogen infection in the area
CC immediately neighboring the inoculated zone.
CC {ECO:0000269|PubMed:20696912}.
CC -!- MISCELLANEOUS: The enzyme has a preference towards linoleoyl acyl chain
CC over palmitoyl acyl chain. It also has a slight preference for
CC phosphatidylethanolamine over phosphatidylcholine.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AY344842; AAR04682.1; -; mRNA.
DR EMBL; AC005171; AAM15017.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06025.1; -; Genomic_DNA.
DR EMBL; AY136317; AAM96983.1; -; mRNA.
DR EMBL; BT002200; AAN72211.1; -; mRNA.
DR EMBL; AK221680; BAD95375.1; -; mRNA.
DR EMBL; AY088532; AAM66065.1; -; mRNA.
DR RefSeq; NP_565337.1; NM_126670.3.
DR AlphaFoldDB; Q8S8N6; -.
DR SMR; Q8S8N6; -.
DR DIP; DIP-59549N; -.
DR IntAct; Q8S8N6; 1.
DR STRING; 3702.AT2G06925.1; -.
DR PaxDb; Q8S8N6; -.
DR PRIDE; Q8S8N6; -.
DR ProteomicsDB; 234764; -.
DR EnsemblPlants; AT2G06925.1; AT2G06925.1; AT2G06925.
DR GeneID; 815261; -.
DR Gramene; AT2G06925.1; AT2G06925.1; AT2G06925.
DR KEGG; ath:AT2G06925; -.
DR Araport; AT2G06925; -.
DR TAIR; locus:505006241; AT2G06925.
DR eggNOG; ENOG502RYYJ; Eukaryota.
DR HOGENOM; CLU_115623_0_0_1; -.
DR InParanoid; Q8S8N6; -.
DR OMA; SKECSRQ; -.
DR PhylomeDB; Q8S8N6; -.
DR BioCyc; ARA:AT2G06925-MON; -.
DR BioCyc; MetaCyc:AT2G06925-MON; -.
DR BRENDA; 3.1.1.4; 399.
DR PRO; PR:Q8S8N6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8N6; baseline and differential.
DR Genevisible; Q8S8N6; AT.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; TAS:TAIR.
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:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
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 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 1: Evidence at protein level;
KW Calcium; Cytoplasmic vesicle; Disulfide bond; Golgi apparatus; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Nucleus;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..148
FT /note="Phospholipase A2-alpha"
FT /id="PRO_0000417561"
FT ACT_SITE 82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 38..66
FT /evidence="ECO:0000250"
FT DISULFID 42..72
FT /evidence="ECO:0000250"
FT DISULFID 47..122
FT /evidence="ECO:0000250"
FT DISULFID 59..79
FT /evidence="ECO:0000250"
FT DISULFID 78..105
FT /evidence="ECO:0000250"
FT DISULFID 85..98
FT /evidence="ECO:0000250"
FT MUTAGEN 82
FT /note="H->Q: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:16669612"
FT MUTAGEN 83
FT /note="D->N: Prevents calcium binding and decreases
FT activity."
FT /evidence="ECO:0000269|PubMed:16669612"
FT MUTAGEN 99
FT /note="S->A,D: Drastically reduces the activity."
FT /evidence="ECO:0000269|PubMed:16669612"
SQ SEQUENCE 148 AA; 16322 MW; 287B27490D6B9922 CRC64;
MAAPIILFSF LLFFSVSVSA LNVGVQLIHP SISLTKECSR KCESEFCSVP PFLRYGKYCG
LLYSGCPGER PCDGLDSCCM KHDACVQSKN NDYLSQECSQ KFINCMNNFS QKKQPTFKGN
KCDADEVIDV ISIVMEAALI AGKVLKKP
