ID   PLP2_ORYSI              Reviewed;         405 AA.
AC   A2YW91;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Patatin-like protein 2;
DE            EC=3.1.1.-;
GN   Name=PLP2; ORFNames=OsI_29602;
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: Possesses non-specific lipolytic acyl hydrolase (LAH)
CC       activity. Hydrolyzes phospholipids as well as galactolipids. May play a
CC       role in disease resistance (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC       motif define the oxyanion hole, and stabilize the oxyanion that forms
CC       during the nucleophilic attack by the catalytic serine during substrate
CC       cleavage. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR   EMBL; CM000133; EAZ07352.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2YW91; -.
DR   SMR; A2YW91; -.
DR   EnsemblPlants; BGIOSGA026808-TA; BGIOSGA026808-PA; BGIOSGA026808.
DR   Gramene; BGIOSGA026808-TA; BGIOSGA026808-PA; BGIOSGA026808.
DR   HOGENOM; CLU_000288_144_0_1; -.
DR   OMA; NNMENSS; -.
DR   Proteomes; UP000007015; Chromosome 8.
DR   GO; GO:0016298; F:lipase activity; IEA:UniProt.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Plant defense;
KW   Reference proteome.
FT   CHAIN           1..405
FT                   /note="Patatin-like protein 2"
FT                   /id="PRO_0000425826"
FT   DOMAIN          24..230
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           28..33
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           66..70
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           217..219
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        68
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   405 AA;  44494 MW;  B929180B48D33729 CRC64;
     MASASSPEGA SSSSPEKVKM VTVLSIDGGG VRGIIPATIL AFLEKELQKL DGPDARIADY
     FDVVAGTSTG GLLTAMLTAP NENNRPLFAA DELAKFYIEH SPSIFPQKNW VLSKIAGTLR
     MVSGPKYDGK YLHSLLREKL GDTRLDKALT NVVIPTFDIA NLQPTIFSKF ELKYKPLKNA
     LLSDISISTS AAPTFFPAHY FETKDDNGQT REFNLVDGGV AANNPTLCAM SQVSKYIILE
     DKEDCDFFPV KPTEYGKFMV ISIGCGSNHD QKYKAKDAAK WGIFNWLIKG SSAPIIDMFT
     SASADMVDIH LGVLFSALQC EKNYLRIQYD QLTGSAGSID DCSKENMDNL VKIGEMLLDK
     NVSRVDLETG HYVDVAGEGT NRDQLAKFAK QLSDERRRRQ NEPSN