PLP2_ORYSJ
ID PLP2_ORYSJ Reviewed; 405 AA.
AC Q6ZJD3; Q0J507;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Patatin-like protein 2;
DE Short=OsPLP2;
DE EC=3.1.1.-;
GN Name=PLP2; OrderedLocusNames=Os08g0477500, LOC_Os08g37250;
GN ORFNames=OJ1666_A04.9, OsJ_27671;
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=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 [2]
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 [3]
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 [4]
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF23958.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003917; BAD08998.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23958.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000145; EAZ43081.1; -; Genomic_DNA.
DR RefSeq; XP_015648579.1; XM_015793093.1.
DR AlphaFoldDB; Q6ZJD3; -.
DR SMR; Q6ZJD3; -.
DR STRING; 39947.Q6ZJD3; -.
DR PaxDb; Q6ZJD3; -.
DR PRIDE; Q6ZJD3; -.
DR GeneID; 4345833; -.
DR KEGG; osa:4345833; -.
DR InParanoid; Q6ZJD3; -.
DR OrthoDB; 1209603at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
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_0000425823"
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
