PLA23_ORYSJ
ID PLA23_ORYSJ Reviewed; 163 AA.
AC Q10E50; A0A0P0W1Z7; Q94GR5;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Phospholipase A2 homolog 3;
DE EC=3.1.1.4;
DE Flags: Precursor;
GN Name=PLA2-III; OrderedLocusNames=Os03g0708000, LOC_Os03g50030;
GN ORFNames=OsJ_12288, OSJNBb0022E02.7;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP PROTEIN SEQUENCE OF 44-59, FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Nipponbare; TISSUE=Shoot;
RX PubMed=10608658; DOI=10.1023/a:1006323405788;
RA Staahl U., Lee M., Sjoedahl S., Archer D., Cellini F., Ek B., Iannacone R.,
RA MacKenzie D., Semeraro L., Tramontano E., Stymme S.;
RT "Plant low-molecular-weight phospholipase A2S (PLA2s) are structurally
RT related to the animal secretory PLA2s and are present as a family of
RT isoforms in rice (Oryza sativa).";
RL Plant Mol. Biol. 41:481-490(1999).
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. {ECO:0000269|PubMed:10608658}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by EGTA. {ECO:0000269|PubMed:10608658}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AC087797; AAK50122.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98479.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12948.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85989.1; -; Genomic_DNA.
DR EMBL; CM000140; EAZ28314.1; -; Genomic_DNA.
DR EMBL; AK105828; BAG97387.1; -; mRNA.
DR RefSeq; XP_015628413.1; XM_015772927.1.
DR AlphaFoldDB; Q10E50; -.
DR SMR; Q10E50; -.
DR STRING; 4530.OS03T0708000-01; -.
DR PaxDb; Q10E50; -.
DR PRIDE; Q10E50; -.
DR EnsemblPlants; Os03t0708000-01; Os03t0708000-01; Os03g0708000.
DR GeneID; 4333862; -.
DR Gramene; Os03t0708000-01; Os03t0708000-01; Os03g0708000.
DR KEGG; osa:4333862; -.
DR eggNOG; ENOG502RYYJ; Eukaryota.
DR HOGENOM; CLU_115623_0_0_1; -.
DR InParanoid; Q10E50; -.
DR OMA; SKECSRQ; -.
DR OrthoDB; 1422829at2759; -.
DR PlantReactome; R-OSA-1119332; Jasmonic acid biosynthesis.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10E50; OS.
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: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; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..43
FT /evidence="ECO:0000269|PubMed:10608658"
FT CHAIN 44..163
FT /note="Phospholipase A2 homolog 3"
FT /id="PRO_0000387496"
FT ACT_SITE 99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 55..83
FT /evidence="ECO:0000250"
FT DISULFID 59..89
FT /evidence="ECO:0000250"
FT DISULFID 64..137
FT /evidence="ECO:0000250"
FT DISULFID 76..96
FT /evidence="ECO:0000250"
FT DISULFID 95..121
FT /evidence="ECO:0000250"
FT DISULFID 102..114
FT /evidence="ECO:0000250"
SQ SEQUENCE 163 AA; 17114 MW; 2C33E13B60A28BD2 CRC64;
MARGGSFSRL RLRAGVVVAA AAAALLLFAV VAPPAAALNI GLQSAGDGAS KAGLCSRTCE
SDHCTTPPLL RYGKYCGILY SGCPGEQPCD ELDACCMHHD NCVQAKNDYL STACNEELLE
CLARLREGSS TFQGNKCMID EVIDVISLVI EAAVVAGRLL HKP
