ID A0A1D6ENZ5_MAIZE Unreviewed; 341 AA.
AC A0A1D6ENZ5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Lipid phosphate phosphatase 2 {ECO:0000313|EMBL:ONM21513.1};
GN ORFNames=ZEAMMB73_Zm00001d005579 {ECO:0000313|EMBL:ONM21513.1};
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:ONM21513.1};
RN [1] {ECO:0000313|EMBL:ONM21513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM21513.1};
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 -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; CM007648; ONM21504.1; -; Genomic_DNA.
DR EMBL; CM007648; ONM21513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6ENZ5; -.
DR IntAct; A0A1D6ENZ5; 3.
DR STRING; 4577.A0A1D6ENZ5; -.
DR eggNOG; KOG3030; Eukaryota.
DR InParanoid; A0A1D6ENZ5; -.
DR ExpressionAtlas; A0A1D6ENZ5; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd03390; PAP2_containing_1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10165:SF199; OS09G0308900 PROTEIN; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..271
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 341 AA; 38284 MW; 10424A161FB10168 CRC64;
MYYHRQNSSG RLMYLSIKID PLSAVEFGSE TMADQLGSYT IRSHGMILAR LHMYDWIILL
LLAVIDGLLN IIEPFHRFVG KDMMTDLRYP MKGNTVPFWA VPLIGIILPW AIFVGIYFKK
KNFYDLHHGI LGILYSVLIT AVITDAIKDG VGRPRPDFFW RCFPNGNDVY DNITTGVICN
GVKSVIKEGH KSFPSGHSSW SFAGLGFLAW YLAGKLTAFD RKGHIAKLCI VFLPLLTAAL
VAVSRVDDYW HHWQDVFAGG LIGLTVASFC YLQFFPYPFD GDALWPHAYA VRLAEEGNSR
NANSYSVRPT EIETVDIPGH GGIITLRDTL NDVESGSARR L
//
