ID A0A0E0RAU8_ORYRU Unreviewed; 401 AA.
AC A0A0E0RAU8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI11G21110.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI11G21110.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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|ARBA:ARBA00010240, ECO:0000256|RuleBase:RU361262}.
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DR AlphaFoldDB; A0A0E0RAU8; -.
DR STRING; 4529.A0A0E0RAU8; -.
DR EnsemblPlants; ORUFI11G21110.1; ORUFI11G21110.1; ORUFI11G21110.
DR Gramene; ORUFI11G21110.1; ORUFI11G21110.1; ORUFI11G21110.
DR eggNOG; KOG0513; Eukaryota.
DR HOGENOM; CLU_000288_144_0_1; -.
DR OMA; ANVRMTE; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07214; Pat17_isozyme_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; PTHR32176:SF27; PATATIN; 1.
DR PANTHER; PTHR32176; XYLOSE ISOMERASE; 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:UP000008022}.
FT DOMAIN 35..242
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43452 MW; 561ABE87ACBE4F92 CRC64;
MASNGEATTE SETAAPAPVP EPTPPPCQGR LITVLSIDGG GIRGLVPATI LACLEAKLQE
LDGPEARIAD YFDVIAGTST GALITSMLAA PDDNRQPLFA ADDLTKFYLE NGPKIFPQQR
VGFLTPVANL IGTVRGPKYD GSFLHDKIKS LTHDVTIADT VTNIVVPAFD VKYLQPIIFS
TYEAKNEPLK NAHLSDICIS TSAAPTYFLA HFFKTTSPSG ESREFHLIDR GVAANNPILS
IYHLTMVAMS MISKEVLREN QDFKLGKPAD YRHYLVISIG TGTATMAEKY TAPACAKWGV
LRWLYDSGFT PLIDIFSHAS ADMDDSLVGH TSSVDIATEE NMEALIGIGK DLLKKPVARV
NIDTGVHEPV DGEGTNEEAL ARFAKKLSEE RRLRRNSLSS S
//
