ID   PLA1_ORYSI              Reviewed;         393 AA.
AC   A2WT95;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Phospholipase A1-II 1;
DE            EC=3.1.1.-;
GN   ORFNames=OsI_03083;
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: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAY75191.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM000126; EAY75191.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A2WT95; -.
DR   SMR; A2WT95; -.
DR   STRING; 39946.A2WT95; -.
DR   Proteomes; UP000007015; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..393
FT                   /note="Phospholipase A1-II 1"
FT                   /id="PRO_0000409363"
FT   COILED          200..220
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        225
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        225
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        284
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        321
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
SQ   SEQUENCE   393 AA;  43956 MW;  8855CF6335E57BB0 CRC64;
     MSSLRGLGNI ARRWRELNGV SYWKGLLDPL DVDLRNNIIN YGELSQAAYT GLNRERRSRY
     AGSCLFSRKD FLSRVDVSNP NLYVITKFIY AMCTVSLPDA FMIKSWSKAA WSKQSNWMGF
     VAVATDEGKE VLGRRDVVVA WRGTIRMVEW MDDLDISLVP ASEIVRPGSA DDPCVHGGWL
     SVYTSADPES QYNKQSARYQ VLNEIKRLQD MYEHEETSIT ITGHSLGAAL ATINATDIVS
     NGYNKSCPVS AFVFGSPRVG NPDFQKAFDS APDLRLLRIR NSPDVVPNWP KLGYSDAGTE
     LMIDTGKSPY LKAPGNPLTW HDMECYMHGV AGTQGSNGGF KLEIDRDIAL VNKHEDALKN
     EYAIPSSWWV VQNKGMVKGT DGRWHLADHE DDD