ID   A0A1D6EX91_MAIZE        Unreviewed;      1164 AA.
AC   A0A1D6EX91;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN   ORFNames=ZEAMMB73_Zm00001d006507 {ECO:0000313|EMBL:ONM24106.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM24106.1};
RN   [1] {ECO:0000313|EMBL:ONM24106.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM24106.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CM007648; ONM24106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6EX91; -.
DR   ExpressionAtlas; A0A1D6EX91; baseline and differential.
DR   GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07211; Pat_PNPLA8; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR045217; PNPLA8-like.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR24185; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR   PANTHER; PTHR24185:SF1; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361262};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU361262};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361262}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
SQ   SEQUENCE   1164 AA;  129867 MW;  C61E8EAE2E9BB758 CRC64;
     MKFRAMGRDI NQANHELLHN FWQMLPVELT RLQFLEKLYL DNNKLSVLPP EVGALKNMKV
     LSFNNNMLVS VPVELRQCVM LEELSLEHNK LVRPLLDFRS MPKLRILRLF GNPLEFLPEI
     LPLHNLRHVT LANIRIEAVE SLKSVTVQIE TENSSYFIAA RHKLSAFFSL VFRFSSCHHP
     LLASALVKIM EDRSNHIAIS KEENAVRQLI SMISSDNRHV VEQACLAISS LASDISSAMQ
     LIKCDIMKPI EAVLKSSDEE ELVSVLQVVV TLTFVSDHVA QKVLTKDVLK SLKALCAHKN
     SEVQRLSLFA IGNLAFCLET RRILMHSESM CDLLIRLTIS QECRVSKAAA RALAILGENE
     NLRRAIRGRP VAKKGLRILS MDGGGMKGLA TVQMLKQIEQ GTGKRIHEMF DLICGTSTGG
     MLAMALGIKQ MTLDQCEEIY TKLGKLVFTE PIPKDEAATW KEKIDQLFKS SSQSFRVVVH
     GSKHSADQFE RLLKEMCENE DGDLLIESAV KGIPKVFAVS TLVSVIPAQP YIFRNYQYPP
     GTLEVSPGMA ESPSIGAIGT AVSGAPVGIK RGAFMGSCKH RVWEAIRASS AAPYYLDDFS
     VDANRWQDGA IVANNPTIFA IREAQLLWPD ARIDCLVSIG CGSVPTKSRR GGWRYLDTGQ
     VLIESACSVE RVEETLDTLI PMLPEMQYFR FNPVDERCGM ELDETDPTIW LKLEAATDEY
     IQKNFLSVKN LCELLVPRYQ EEEKPSDIYK SLSFSRLTSL NQGFSESNPI LGWRRVVLLV
     EASFSPDFGK KINHARSLES FCSQNGIRLA LMNSTSGFGK PATALPTPIT SPLFTGSFPS
     SPLLYSPEGT QRISRIDLVP PLSLDGHPTT KSSPPTSPLK SRQPSAHVRS LYDKLQNMPQ
     VGVIHLALQN DSTGSVLSWQ NDVFVVAEPG ELADRFLQSV KTILSTLLRG CNRKGAYSLS
     KISCLSELVA EWPSFEIGGI HHRYIGRQTQ VMEDNQEIGA YMFRRTVPAV HMAPEDVRWM
     VGAWRERIII CSGKYGLAHG LVKAFMDCGA KAVISSSIEP PDSKTIVYHG MDVNRSLENG
     KFVIRDEEAD ESEPEPVSPI SDWEDSDVEK GGNHDVDDEE YLAQFMCLMY DKLFREGVTV
     DTALQQALRS HPKLKYSCHL PNVL
//