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Phospholipase A2-alpha (EC 3.1.1.4) (Secretory phospholipase A2-alpha) (AtsPLA2-alpha)

 PLA2A_ARATH             Reviewed;         148 AA.
Q8S8N6;
13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-APR-2018, entry version 120.
RecName: Full=Phospholipase A2-alpha {ECO:0000303|PubMed:16140037};
EC=3.1.1.4 {ECO:0000269|PubMed:16140037};
AltName: Full=Secretory phospholipase A2-alpha;
Short=AtsPLA2-alpha;
Flags: Precursor;
Name=PLA2-ALPHA {ECO:0000303|PubMed:16140037};
OrderedLocusNames=At2g06925 {ECO:0000312|Araport:AT2G06925};
ORFNames=T4E14.19 {ECO:0000312|EMBL:AAM15017.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=16140037; DOI=10.1016/j.bbalip.2005.08.005;
Ryu S.B., Lee H.Y., Doelling J.H., Palta J.P.;
"Characterization of a cDNA encoding Arabidopsis secretory
phospholipase A2-alpha, an enzyme that generates bioactive
lysophospholipids and free fatty acids.";
Biochim. Biophys. Acta 1736:144-151(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15130548; DOI=10.1016/j.tplants.2004.03.004;
Ryu S.B.;
"Phospholipid-derived signaling mediated by phospholipase A in
plants.";
Trends Plant Sci. 9:229-235(2004).
[8]
TISSUE SPECIFICITY.
PubMed=15748654; DOI=10.1016/j.plipres.2004.10.002;
Lee H.Y., Bahn S.C., Shin J.S., Hwang I., Back K., Doelling J.H.,
Ryu S.B.;
"Multiple forms of secretory phospholipase A2 in plants.";
Prog. Lipid Res. 44:52-67(2005).
[9]
MUTAGENESIS OF HIS-82; ASP-83 AND SER-99.
PubMed=16669612; DOI=10.1021/bi052563z;
Mansfeld J., Gebauer S., Dathe K., Ulbrich-Hofmann R.;
"Secretory phospholipase A2 from Arabidopsis thaliana: insights into
the three-dimensional structure and the amino acids involved in
catalysis.";
Biochemistry 45:5687-5694(2006).
[10]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17692835; DOI=10.1016/j.chemphyslip.2007.07.001;
Mansfeld J., Ulbrich-Hofmann R.;
"Secretory phospholipase A2-alpha from Arabidopsis thaliana:
functional parameters and substrate preference.";
Chem. Phys. Lipids 150:156-166(2007).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20525850; DOI=10.1105/tpc.110.074211;
Lee O.R., Kim S.J., Kim H.J., Hong J.K., Ryu S.B., Lee S.H.,
Ganguly A., Cho H.T.;
"Phospholipase A(2) is required for PIN-FORMED protein trafficking to
the plasma membrane in the Arabidopsis root.";
Plant Cell 22:1812-1825(2010).
[12]
FUNCTION, INTERACTION WITH MYB30, INDUCTION BY PATHOGEN, AND
SUBCELLULAR LOCATION.
PubMed=20696912; DOI=10.1073/pnas.1009056107;
Froidure S., Canonne J., Daniel X., Jauneau A., Briere C., Roby D.,
Rivas S.;
"AtsPLA2-alpha nuclear relocalization by the Arabidopsis transcription
factor AtMYB30 leads to repression of the plant defense response.";
Proc. Natl. Acad. Sci. U.S.A. 107:15281-15286(2010).
-!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids
(LPLs) and free fatty acids (FFAs) from membrane phospholipids in
response to hormones and other external stimuli. Modulates the
trafficking of PIN proteins to the plasma membrane
(PubMed:16140037, PubMed:20525850). Negatively regulates MYB30
transcriptional activity and hypersensitive response control
(PubMed:20696912). {ECO:0000269|PubMed:16140037,
ECO:0000269|PubMed:20525850, ECO:0000269|PubMed:20696912}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate.
{ECO:0000269|PubMed:16140037}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
Note=Binds 1 Ca(2+) ion per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Vmax=15.3 umol/min/mg enzyme toward Dioleolyl-
phosphoethanolamine (in the presence of 10 mM Calcium)
{ECO:0000269|PubMed:17692835};
Vmax=9.9 umol/min/mg enzyme toward DOPG (in the presence of 10
mM Calcium) {ECO:0000269|PubMed:17692835};
Vmax=16.7 umol/min/mg enzyme toward Dioleolyl-phosphocholine (in
the presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
Vmax=19.5 umol/min/mg enzyme toward Dilinoleoyl-phosphocholine
(in the presence of 10 mM Calcium)
{ECO:0000269|PubMed:17692835};
Vmax=20.6 umol/min/mg enzyme toward Dipalmitoyl-phosphocholine
(in the presence of 10 mM Calcium)
{ECO:0000269|PubMed:17692835};
Vmax=27.3 umol/min/mg enzyme toward Dimyristoyl-phosphocholine
(in the presence of 10 mM Calcium)
{ECO:0000269|PubMed:17692835};
Vmax=29.3 umol/min/mg enzyme toward Dilauroyl-phosphocholine (in
the presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
Vmax=35.5 umol/min/mg enzyme toward Didecanoyl-phosphocholine
(in the presence of 10 mM Calcium)
{ECO:0000269|PubMed:17692835};
Vmax=14.4 umol/min/mg enzyme toward Dioctanoyl-phosphocholine
(in the presence of 10 mM Calcium)
{ECO:0000269|PubMed:17692835};
Vmax=5.9 umol/min/mg enzyme toward Diheptanoyl-phosphocholine
(in the presence of 10 mM Calcium)
{ECO:0000269|PubMed:17692835};
Vmax=1.1 umol/min/mg enzyme toward Dihexanoyl-phosphocholine (in
the presence of 10 mM Calcium) {ECO:0000269|PubMed:17692835};
pH dependence:
Optimum pH is 8.5-9. {ECO:0000269|PubMed:17692835};
Temperature dependence:
Optimum temperature is 30-40 degrees Celsius.
{ECO:0000269|PubMed:17692835};
-!- SUBUNIT: Interacts with MYB30. {ECO:0000269|PubMed:20696912}.
-!- INTERACTION:
Q9SCU7:MYB30; NbExp=4; IntAct=EBI-15869996, EBI-4466599;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20696912}.
Golgi apparatus {ECO:0000269|PubMed:20525850}. Cytoplasmic vesicle
{ECO:0000269|PubMed:20696912}. Nucleus
{ECO:0000269|PubMed:20696912}. Note=Relocalization from
cytoplasmic vesicles to nucleus is MYB30-mediated.
{ECO:0000269|PubMed:20696912}.
-!- TISSUE SPECIFICITY: Ubiquitous but expressed at a low level.
{ECO:0000269|PubMed:15748654, ECO:0000269|PubMed:16140037}.
-!- INDUCTION: Induced 6 hours post pathogen infection in the area
immediately neighboring the inoculated zone.
{ECO:0000269|PubMed:20696912}.
-!- MISCELLANEOUS: The enzyme has a preference towards linoleoyl acyl
chain over palmitoyl acyl chain. It also has a slight preference
for phosphatidylethanolamine over phosphatidylcholine.
-!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY344842; AAR04682.1; -; mRNA.
EMBL; AC005171; AAM15017.1; -; Genomic_DNA.
EMBL; CP002685; AEC06025.1; -; Genomic_DNA.
EMBL; AY136317; AAM96983.1; -; mRNA.
EMBL; BT002200; AAN72211.1; -; mRNA.
EMBL; AK221680; BAD95375.1; -; mRNA.
EMBL; AY088532; AAM66065.1; -; mRNA.
RefSeq; NP_565337.1; NM_126670.3.
UniGene; At.23179; -.
ProteinModelPortal; Q8S8N6; -.
SMR; Q8S8N6; -.
DIP; DIP-59549N; -.
IntAct; Q8S8N6; 1.
STRING; 3702.AT2G06925.1; -.
PaxDb; Q8S8N6; -.
EnsemblPlants; AT2G06925.1; AT2G06925.1; AT2G06925.
GeneID; 815261; -.
Gramene; AT2G06925.1; AT2G06925.1; AT2G06925.
KEGG; ath:AT2G06925; -.
Araport; AT2G06925; -.
TAIR; locus:505006241; AT2G06925.
eggNOG; ENOG410IXQN; Eukaryota.
eggNOG; ENOG410YKKM; LUCA.
HOGENOM; HOG000239931; -.
InParanoid; Q8S8N6; -.
KO; K01047; -.
OMA; CQVDDVI; -.
OrthoDB; EOG09360R76; -.
PhylomeDB; Q8S8N6; -.
BioCyc; ARA:AT2G06925-MONOMER; -.
BioCyc; MetaCyc:AT2G06925-MONOMER; -.
BRENDA; 3.1.1.4; 399.
PRO; PR:Q8S8N6; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q8S8N6; baseline and differential.
Genevisible; Q8S8N6; AT.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005773; C:vacuole; TAS:TAIR.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Cytoplasmic vesicle; Disulfide bond;
Golgi apparatus; Hydrolase; Lipid degradation; Lipid metabolism;
Metal-binding; Nucleus; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 148 Phospholipase A2-alpha.
/FTId=PRO_0000417561.
ACT_SITE 82 82 {ECO:0000255|PROSITE-ProRule:PRU10035}.
METAL 58 58 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 60 60 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 63 63 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 83 83 Calcium. {ECO:0000250}.
DISULFID 38 66 {ECO:0000250}.
DISULFID 42 72 {ECO:0000250}.
DISULFID 47 122 {ECO:0000250}.
DISULFID 59 79 {ECO:0000250}.
DISULFID 78 105 {ECO:0000250}.
DISULFID 85 98 {ECO:0000250}.
MUTAGEN 82 82 H->Q: Abolishes activity.
{ECO:0000269|PubMed:16669612}.
MUTAGEN 83 83 D->N: Prevents calcium binding and
decreases activity.
{ECO:0000269|PubMed:16669612}.
MUTAGEN 99 99 S->A,D: Drastically reduces the activity.
{ECO:0000269|PubMed:16669612}.
SEQUENCE 148 AA; 16322 MW; 287B27490D6B9922 CRC64;
MAAPIILFSF LLFFSVSVSA LNVGVQLIHP SISLTKECSR KCESEFCSVP PFLRYGKYCG
LLYSGCPGER PCDGLDSCCM KHDACVQSKN NDYLSQECSQ KFINCMNNFS QKKQPTFKGN
KCDADEVIDV ISIVMEAALI AGKVLKKP


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