PLA22_ORYSJ
ID PLA22_ORYSJ Reviewed; 153 AA.
AC Q9XG81; A0A0P0VVN9; Q0DTA4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable phospholipase A2 homolog 2;
DE EC=3.1.1.4;
DE Flags: Precursor;
GN Name=PLA2-II; OrderedLocusNames=Os03g0261100, LOC_Os03g15460;
GN ORFNames=OsJ_10213;
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 [MRNA].
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).
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-153 IN COMPLEX WITH CALCIUM
RP IONS AND SUBSTRATE ANALOG, AND DISULFIDE BONDS.
RX PubMed=19457861; DOI=10.1074/jbc.m109.008466;
RA Guy J.E., Staahl U., Lindqvist Y.;
RT "Crystal structure of a class XIB phospholipase A2 (PLA2): rice (oryza
RT sativa) isoform-2 pla2 and an octanoate complex.";
RL J. Biol. Chem. 284:19371-19379(2009).
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:0000250}.
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;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AJ238117; CAB40842.1; -; mRNA.
DR EMBL; AP008209; BAF11534.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83356.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE58732.1; -; Genomic_DNA.
DR RefSeq; XP_015629036.1; XM_015773550.1.
DR PDB; 2WG7; X-ray; 2.00 A; A/B=25-153.
DR PDB; 2WG8; X-ray; 2.30 A; A/B/C=26-153.
DR PDB; 2WG9; X-ray; 2.00 A; A/B=25-153.
DR PDBsum; 2WG7; -.
DR PDBsum; 2WG8; -.
DR PDBsum; 2WG9; -.
DR AlphaFoldDB; Q9XG81; -.
DR SMR; Q9XG81; -.
DR STRING; 4530.OS03T0261100-01; -.
DR PRIDE; Q9XG81; -.
DR EnsemblPlants; Os03t0261100-01; Os03t0261100-01; Os03g0261100.
DR GeneID; 4332319; -.
DR Gramene; Os03t0261100-01; Os03t0261100-01; Os03g0261100.
DR KEGG; osa:4332319; -.
DR eggNOG; ENOG502RYYJ; Eukaryota.
DR HOGENOM; CLU_115623_0_0_1; -.
DR InParanoid; Q9XG81; -.
DR OMA; NACESKF; -.
DR OrthoDB; 1422829at2759; -.
DR BRENDA; 3.1.1.4; 4460.
DR EvolutionaryTrace; Q9XG81; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q9XG81; OS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; 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 3D-structure; Calcium; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..153
FT /note="Probable phospholipase A2 homolog 2"
FT /id="PRO_5000065168"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 42..70
FT /evidence="ECO:0000269|PubMed:19457861"
FT DISULFID 46..76
FT /evidence="ECO:0000269|PubMed:19457861"
FT DISULFID 51..123
FT /evidence="ECO:0000269|PubMed:19457861"
FT DISULFID 63..83
FT /evidence="ECO:0000269|PubMed:19457861"
FT DISULFID 82..109
FT /evidence="ECO:0000269|PubMed:19457861"
FT DISULFID 89..102
FT /evidence="ECO:0000269|PubMed:19457861"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2WG7"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2WG9"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2WG7"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2WG7"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2WG7"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:2WG7"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2WG7"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:2WG7"
FT HELIX 125..149
FT /evidence="ECO:0007829|PDB:2WG7"
SQ SEQUENCE 153 AA; 16578 MW; C9AC0BDB1F2885F6 CRC64;
MRFFLKLAPR CSVLLLLLLV TASRGLNIGD LLGSTPAKDQ GCSRTCESQF CTIAPLLRYG
KYCGILYSGC PGERPCDALD ACCMVHDHCV DTHNDDYLNT MCNENLLSCI DRVSGATFPG
NKCNVGQTAS VIRGVIETAV FAGKILHKRD DGQ
