ID A2YG60_ORYSI Unreviewed; 404 AA.
AC A2YG60;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=OsI_24152 {ECO:0000313|EMBL:EAZ02071.1};
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 {ECO:0000313|EMBL:EAZ02071.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EAZ02071.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
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., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Lipolytic acyl hydrolase (LAH).
CC {ECO:0000256|RuleBase:RU361262}.
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. {ECO:0000256|ARBA:ARBA00025642}.
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:0000256|RuleBase:RU361262}.
CC -!- SIMILARITY: Belongs to the patatin family.
CC {ECO:0000256|RuleBase:RU361262}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000131; EAZ02071.1; -; Genomic_DNA.
DR AlphaFoldDB; A2YG60; -.
DR STRING; 39946.A2YG60; -.
DR EnsemblPlants; BGIOSGA020684-TA; BGIOSGA020684-PA; BGIOSGA020684.
DR Gramene; BGIOSGA020684-TA; BGIOSGA020684-PA; BGIOSGA020684.
DR HOGENOM; CLU_000288_144_1_1; -.
DR OMA; KPEHPPQ; -.
DR Proteomes; UP000007015; Chromosome 6.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07199; Pat17_PNPLA8_PNPLA9_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR32241:SF16; OS06G0677000 PROTEIN; 1.
DR PANTHER; PTHR32241; PATATIN-LIKE PROTEIN 6; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361262};
KW Lipid degradation {ECO:0000256|RuleBase:RU361262};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361262};
KW Reference proteome {ECO:0000313|Proteomes:UP000007015}.
FT DOMAIN 56..239
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 379..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 41563 MW; 8D69D09BE82F5B0B CRC64;
MATTSSLALP LFAGGGGSDR LSQEIFSILE SNFLFGAPPP EGPAGYYSSV GRVRVLSIDG
GADGGALAAA ALVRLERRLK ELSGNPDARV ADYFDLAAGS GAGGFLAAAL FACRMPAEAA
RDVVARNRKV FSGRRGRGGG LFWRPESVFK KVFGDLTVRD AAKPLLIPCY DMATAAPFVF
SRADAVEADA FDFPLWQVCA AACGVGPAEV ASLDGRTRLR AAAATGGGGA VSNPAAVAVT
HVLHNKREFP FAAGAGDLVV LSLGGNNAAA GPRASSSSLL RIAGACQADM VDQAVSMAFG
ECRATNYIRI QGNGIVAGAA AATAEAAMTE RSVESVLFRG KKVMAQTNGE RLDGVAEQLV
REHHRRMESK APVVLIKPSA TPRTSSSSAS TLITVSTNAS SESP
//
