PLA2B_ARATH
ID PLA2B_ARATH Reviewed; 147 AA.
AC Q8GZB4; O82208;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phospholipase A2-beta;
DE EC=3.1.1.4;
DE AltName: Full=Secretory phospholipase A2-beta;
DE Short=AtsPLA2-beta;
DE Flags: Precursor;
GN Name=PLA2-BETA; OrderedLocusNames=At2g19690; ORFNames=F6F22.28;
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, TISSUE
RP SPECIFICITY, INDUCTION BY AUXIN, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12953106; DOI=10.1105/tpc.014423;
RA Lee H.Y., Bahn S.C., Kang Y.M., Lee K.H., Kim H.J., Noh E.K., Palta J.P.,
RA Shin J.S., Ryu S.B.;
RT "Secretory low molecular weight phospholipase A2 plays important roles in
RT cell elongation and shoot gravitropism in Arabidopsis.";
RL Plant Cell 15:1990-2002(2003).
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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, DISRUPTION PHENOTYPE, INDUCTION BY LIGHT, ACTIVITY REGULATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=18725378; DOI=10.1093/jxb/ern208;
RA Seo J., Lee H.Y., Choi H., Choi Y., Lee Y., Kim Y.W., Ryu S.B., Lee Y.;
RT "Phospholipase A2beta mediates light-induced stomatal opening in
RT Arabidopsis.";
RL J. Exp. Bot. 59:3587-3594(2008).
RN [8]
RP 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 [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL 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. Regulates the process of cell
CC elongation and plays important roles in shoot gravitropism by mediating
CC auxin-induced cell elongation. Involved in stomatal opening in response
CC to light. Plays a role in pollen development and germination and tube
CC growth. {ECO:0000269|PubMed:12953106, ECO:0000269|PubMed:18725378,
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:12953106};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by aristolochic acid.
CC {ECO:0000269|PubMed:18725378}.
CC -!- SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8GZB4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous but expressed at a low level. Detected
CC in vascular tissues and in the guard cells. Predominantly detected in
CC pollen. {ECO:0000269|PubMed:12953106, ECO:0000269|PubMed:15748654,
CC ECO:0000269|PubMed:18725378, ECO:0000269|PubMed:21278126}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the actively growing young stages of
CC Arabidopsis seedlings. When plants grew, however, expression was
CC evident only in cotyledons, primary leaves, and hypocotyls. The
CC activity decreased in the secondary leaves, being detectable only in
CC vascular tissues. In the roots as well, expression was localized mostly
CC in vascular tissues. Expression becomes highly active when floral
CC shoots bolted, especially in the young or actively growing tissues of
CC inflorescence stems. Continuously expressed during pollen development.
CC {ECO:0000269|PubMed:12953106, ECO:0000269|PubMed:21278126}.
CC -!- INDUCTION: By auxin. By light. {ECO:0000269|PubMed:12953106,
CC ECO:0000269|PubMed:18725378}.
CC -!- DISRUPTION PHENOTYPE: RNAi mutant exhibits delayed light-induced
CC stomatal opening. {ECO:0000269|PubMed:18725378}.
CC -!- MISCELLANEOUS: The enzyme has a preference towards palmitoyl acyl chain
CC over linoleoyl acyl chain. It also has a slight preference for
CC phosphatidylethanolamine over phosphatidylcholine.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62146.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF541915; AAN77229.1; -; mRNA.
DR EMBL; AC005169; AAC62146.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06913.1; -; Genomic_DNA.
DR EMBL; BX821623; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; H84579; H84579.
DR RefSeq; NP_179559.2; NM_127527.4. [Q8GZB4-1]
DR AlphaFoldDB; Q8GZB4; -.
DR SMR; Q8GZB4; -.
DR STRING; 3702.AT2G19690.2; -.
DR PaxDb; Q8GZB4; -.
DR PRIDE; Q8GZB4; -.
DR ProteomicsDB; 236743; -. [Q8GZB4-1]
DR EnsemblPlants; AT2G19690.1; AT2G19690.1; AT2G19690. [Q8GZB4-1]
DR GeneID; 816488; -.
DR Gramene; AT2G19690.1; AT2G19690.1; AT2G19690. [Q8GZB4-1]
DR KEGG; ath:AT2G19690; -.
DR Araport; AT2G19690; -.
DR eggNOG; ENOG502RZIE; Eukaryota.
DR HOGENOM; CLU_115623_1_0_1; -.
DR InParanoid; Q8GZB4; -.
DR OMA; HEKFKTC; -.
DR PhylomeDB; Q8GZB4; -.
DR BioCyc; ARA:AT2G19690-MON; -.
DR PRO; PR:Q8GZB4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GZB4; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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: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:0009630; P:gravitropism; IMP:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0009846; P:pollen germination; IDA:UniProtKB.
DR GO; GO:0009860; P:pollen tube growth; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP: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 Alternative splicing; Calcium; Disulfide bond; Endoplasmic reticulum;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..147
FT /note="Phospholipase A2-beta"
FT /id="PRO_0000417562"
FT MOTIF 144..147
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 31..58
FT /evidence="ECO:0000250"
FT DISULFID 35..64
FT /evidence="ECO:0000250"
FT DISULFID 40..117
FT /evidence="ECO:0000250"
FT DISULFID 51..71
FT /evidence="ECO:0000250"
FT DISULFID 70..95
FT /evidence="ECO:0000250"
FT DISULFID 77..88
FT /evidence="ECO:0000250"
SQ SEQUENCE 147 AA; 16286 MW; C60D376FE4AB63D4 CRC64;
MMFRTSLMRF AAAFFAIVFV VLVGVARSEE CTRTCIAQNC DTLSIRYGKY CGIGHSGCPG
EEPCDDLDAC CKIHDHCVEL NGMTNISCHK KFQRCVNRLS KAIKQSKNKK VGFSTKCPYS
VVIPTVNQGM DIGILFSQLG NDMKTEL
