PLA2C_ARATH
ID PLA2C_ARATH Reviewed; 187 AA.
AC Q9M0D7;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phospholipase A2-gamma;
DE EC=3.1.1.4;
DE AltName: Full=Secretory phospholipase A2-gamma;
DE Short=AtsPLA2-gamma;
DE Flags: Precursor;
GN Name=PLA2-GAMMA; OrderedLocusNames=At4g29460; ORFNames=F17A13.280;
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], CATALYTIC ACTIVITY, FUNCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14550557; DOI=10.1016/s0014-5793(03)00982-7;
RA Bahn S.C., Lee H.Y., Kim H.J., Ryu S.B., Shin J.S.;
RT "Characterization of Arabidopsis secretory phospholipase A2-gamma cDNA and
RT its enzymatic properties.";
RL FEBS Lett. 553:113-118(2003).
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 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 [6]
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:14550557,
CC 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 ECO:0000269|PubMed:14550557};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted. Golgi apparatus, trans-Golgi network.
CC Endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Strongly expressed in mature flowers but weakly
CC expressed in other tissues. Detected in buds, open flowers and in
CC pollen. {ECO:0000269|PubMed:14550557, ECO:0000269|PubMed:15748654,
CC 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}.
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DR EMBL; AY148346; AAN63044.1; -; mRNA.
DR EMBL; AL161575; CAB79704.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85634.1; -; Genomic_DNA.
DR PIR; G85343; G85343.
DR RefSeq; NP_194675.1; NM_119091.3.
DR AlphaFoldDB; Q9M0D7; -.
DR SMR; Q9M0D7; -.
DR STRING; 3702.AT4G29460.1; -.
DR PaxDb; Q9M0D7; -.
DR PRIDE; Q9M0D7; -.
DR EnsemblPlants; AT4G29460.1; AT4G29460.1; AT4G29460.
DR GeneID; 829067; -.
DR Gramene; AT4G29460.1; AT4G29460.1; AT4G29460.
DR KEGG; ath:AT4G29460; -.
DR Araport; AT4G29460; -.
DR TAIR; locus:2118354; AT4G29460.
DR eggNOG; ENOG502RZIE; Eukaryota.
DR HOGENOM; CLU_115623_1_0_1; -.
DR InParanoid; Q9M0D7; -.
DR OMA; CPYSIVI; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q9M0D7; -.
DR BioCyc; ARA:AT4G29460-MON; -.
DR BioCyc; MetaCyc:AT4G29460-MON; -.
DR BRENDA; 3.1.1.4; 399.
DR PRO; PR:Q9M0D7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0D7; 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:0005794; C:Golgi apparatus; IDA: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 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 1: Evidence at protein level;
KW Calcium; Disulfide bond; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..187
FT /note="Phospholipase A2-gamma"
FT /id="PRO_0000417563"
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 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
