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

 PLA2C_ARATH             Reviewed;         187 AA.
Q9M0D7;
13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 108.
RecName: Full=Phospholipase A2-gamma;
EC=3.1.1.4;
AltName: Full=Secretory phospholipase A2-gamma;
Short=AtsPLA2-gamma;
Flags: Precursor;
Name=PLA2-GAMMA; OrderedLocusNames=At4g29460; ORFNames=F17A13.280;
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], CATALYTIC ACTIVITY, FUNCTION, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=14550557; DOI=10.1016/S0014-5793(03)00982-7;
Bahn S.C., Lee H.Y., Kim H.J., Ryu S.B., Shin J.S.;
"Characterization of Arabidopsis secretory phospholipase A2-gamma cDNA
and its enzymatic properties.";
FEBS Lett. 553:113-118(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(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]
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).
[5]
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).
[6]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
PubMed=21278126; DOI=10.1105/tpc.110.074799;
Kim H.J., Ok S.H., Bahn S.C., Jang J., Oh S.A., Park S.K., Twell D.,
Ryu S.B., Shin J.S.;
"Endoplasmic reticulum- and Golgi-localized phospholipase A2 plays
critical roles in Arabidopsis pollen development and germination.";
Plant Cell 23:94-110(2011).
-!- 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. Plays a role in
pollen development and germination and tube growth.
{ECO:0000269|PubMed:14550557, ECO:0000269|PubMed:21278126}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000269|PubMed:14550557}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 1 Ca(2+) ion per subunit.;
-!- SUBCELLULAR LOCATION: Secreted. Golgi apparatus, trans-Golgi
network. Endoplasmic reticulum.
-!- TISSUE SPECIFICITY: Strongly expressed in mature flowers but
weakly expressed in other tissues. Detected in buds, open flowers
and in pollen. {ECO:0000269|PubMed:14550557,
ECO:0000269|PubMed:15748654, ECO:0000269|PubMed:21278126}.
-!- DEVELOPMENTAL STAGE: Expressed during pollen germination and tube
growth. {ECO:0000269|PubMed:21278126}.
-!- MISCELLANEOUS: The enzyme has a slight preference for
phosphatidylethanolamine over phosphatidylcholine.
-!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY148346; AAN63044.1; -; mRNA.
EMBL; AL161575; CAB79704.1; -; Genomic_DNA.
EMBL; CP002687; AEE85634.1; -; Genomic_DNA.
PIR; G85343; G85343.
RefSeq; NP_194675.1; NM_119091.3.
UniGene; At.31919; -.
ProteinModelPortal; Q9M0D7; -.
SMR; Q9M0D7; -.
STRING; 3702.AT4G29460.1; -.
PaxDb; Q9M0D7; -.
EnsemblPlants; AT4G29460.1; AT4G29460.1; AT4G29460.
GeneID; 829067; -.
Gramene; AT4G29460.1; AT4G29460.1; AT4G29460.
KEGG; ath:AT4G29460; -.
Araport; AT4G29460; -.
TAIR; locus:2118354; AT4G29460.
eggNOG; ENOG410IZP9; Eukaryota.
eggNOG; ENOG410YKKG; LUCA.
HOGENOM; HOG000239638; -.
InParanoid; Q9M0D7; -.
OMA; QFKRCVN; -.
OrthoDB; EOG09360SCS; -.
PhylomeDB; Q9M0D7; -.
BioCyc; ARA:AT4G29460-MONOMER; -.
BioCyc; MetaCyc:AT4G29460-MONOMER; -.
BRENDA; 3.1.1.4; 399.
PRO; PR:Q9M0D7; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9M0D7; baseline and differential.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA: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.
GO; GO:0009555; P:pollen development; IMP:TAIR.
GO; GO:0009846; P:pollen germination; IDA:UniProtKB.
GO; GO:0009860; P:pollen tube growth; IDA:UniProtKB.
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; Disulfide bond; Endoplasmic reticulum;
Golgi apparatus; Hydrolase; Lipid degradation; Lipid metabolism;
Metal-binding; Reference proteome; Secreted; Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 187 Phospholipase A2-gamma.
/FTId=PRO_0000417563.
ACT_SITE 72 72 {ECO:0000255|PROSITE-ProRule:PRU10035}.
METAL 48 48 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 50 50 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 53 53 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 73 73 Calcium. {ECO:0000250}.
DISULFID 29 56 {ECO:0000250}.
DISULFID 33 62 {ECO:0000250}.
DISULFID 38 115 {ECO:0000250}.
DISULFID 49 69 {ECO:0000250}.
DISULFID 68 93 {ECO:0000250}.
DISULFID 75 86 {ECO:0000250}.
SEQUENCE 187 AA; 20038 MW; 912F67A37D54081E CRC64;
MITGLALSRV AFGLTAFLLL AVVSSQEKCS NTCIAQNCNS LGIRYGKYCG IGYFGCPGEP
PCDDLDACCM THDNCVDLKG MTYVNCHKQF KRCVNKLSKS IKHSNGEKIG FSTQCPYSIV
IPTVFNGMDY GIFFSGIGNI FNPPVLGSVP VVEVDLARSK VDTKDGLGTK LGLQTKEGSK
VSASLNI


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