ID   PLA3_ORYSI              Reviewed;         420 AA.
AC   A2WTA0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Phospholipase A1-II 3;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   ORFNames=OsI_03088;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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).
CC   -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of phospholipids
CC       at the sn-1 position. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; CM000126; EAY75196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2WTA0; -.
DR   SMR; A2WTA0; -.
DR   STRING; 39946.A2WTA0; -.
DR   ESTHER; orysa-Q8RZ40; Plant_phospholipase.
DR   EnsemblPlants; BGIOSGA004123-TA; BGIOSGA004123-PA; BGIOSGA004123.
DR   Gramene; BGIOSGA004123-TA; BGIOSGA004123-PA; BGIOSGA004123.
DR   HOGENOM; CLU_018841_0_0_1; -.
DR   OMA; ECYLHAV; -.
DR   Proteomes; UP000007015; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008970; F:phospholipase A1 activity; ISS:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   InterPro; IPR033556; PLA.
DR   PANTHER; PTHR31828; PTHR31828; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..420
FT                   /note="Phospholipase A1-II 3"
FT                   /id="PRO_0000409367"
FT   COILED          367..388
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        240
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        240
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        305
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        343
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   420 AA;  45324 MW;  71326C87313752A2 CRC64;
     MCCFLLVSVL LATTLTDVAS AQRWRQTSGG GKDRWDGLLD PLDADLRRDI IRYGELAQAT
     SDALIGDPAS PFAGASRYAP DAFLRKVRAS DPDAYRVTRF VYATSSVRLP DAFMPRPAPS
     AGAAWSGESN WMGYVAVAAD GVAANAGRRD IVVAWRGTKR AVEWANDLDI TLVPADGVVG
     PGPGWTQPSV HRGFLSVYTS KSFSSPFNKL SAREQVLAEI TRLLRAYKNE NCSITITGHS
     LGAALSTLNA IDIVANGYNV RGSSRVPVPV TAIALASPRV GDDQFKRAFD STPNLSLLRV
     RNAPDIVPTI LPSAFFKDVG AELLVDTRRS PYLKNPAGPA QWHNLECYLH AVAGTQGAGD
     GAGFSLVVDR DLALVNKEVD ALRDEYQVPA AWWVEKNKGM VQNASGRWVL QDHEEGNLAM