PLPP5_XENLA
ID PLPP5_XENLA Reviewed; 266 AA.
AC Q6GQ62;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Phospholipid phosphatase 5 {ECO:0000250|UniProtKB:Q8NEB5};
DE EC=3.1.3.4 {ECO:0000250|UniProtKB:Q8NEB5};
DE EC=3.1.3.81 {ECO:0000250|UniProtKB:Q8NEB5};
GN Name=plpp5 {ECO:0000250|UniProtKB:Q8NEB5};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Magnesium-independent phospholipid phosphatase with broad
CC substrate specificity. Preferentially catalyzes the conversion of
CC diacylglycerol pyrophosphate into phosphatidate but can also act on
CC phosphatidate and lysophosphatidate. Phospholipid phosphatases are
CC involved in both the synthesis of lipids and the generation or
CC degradation of lipid-signaling molecules.
CC {ECO:0000250|UniProtKB:Q8NEB5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.1.3.81;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-diphosphate + H2O = 1,2-
CC dioctanoyl-sn-glycero-3-phosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:42856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:78229, ChEBI:CHEBI:82765;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42857;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phosphate + H2O = 1,2-dioctanoyl-
CC sn-glycerol + phosphate; Xref=Rhea:RHEA:42860, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:76979, ChEBI:CHEBI:78229;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42861;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB5};
CC -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase.
CC Inhibited by N-ethylmaleimide. {ECO:0000250|UniProtKB:Q8NEB5}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:Q8NEB5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3UMZ3};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3UMZ3}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72886.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC072886; AAH72886.1; ALT_INIT; mRNA.
DR RefSeq; NP_001085524.2; NM_001092055.1.
DR RefSeq; XP_018106412.1; XM_018250923.1.
DR AlphaFoldDB; Q6GQ62; -.
DR DNASU; 443950; -.
DR GeneID; 443950; -.
DR KEGG; xla:443950; -.
DR CTD; 443950; -.
DR Xenbase; XB-GENE-6251520; plpp5.L.
DR OMA; TAPMFFI; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 443950; Expressed in liver and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR InterPro; IPR028668; PLPP4/5.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR PANTHER; PTHR10165:SF87; PTHR10165:SF87; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Hydrolase; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..266
FT /note="Phospholipid phosphatase 5"
FT /id="PRO_0000286947"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..53
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q3UMZ3"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3UMZ3"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..146
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q3UMZ3"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3UMZ3"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..206
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q3UMZ3"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3UMZ3"
FT REGION 107..115
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:Q8NEB5"
FT REGION 148..151
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:Q8NEB5"
FT REGION 200..210
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:Q8NEB5"
FT REGION 246..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 211
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
SQ SEQUENCE 266 AA; 29904 MW; 2DD95FC5BFCC921B CRC64;
MDKRILEGFA AEFIIRLLLF GIFLISETMH PFERVIQPEE MWLYRNPYVV SDRIPTNSMF
LISFLTPLSV VALARLFWKA DGTDSREAGL AASLSLALNG IFTNTVKLIV GRPRPDFLFR
CFPDGQESPG LHCTGDPELV IEGRKSFPSG HSSFAFAGLG FTALYLAGKL RCFSPCGRGH
SWRLCASLIP LLCAIAIALS RTCDYKHHWQ DVVVGAFIGL FFAFLCYRQY YPSLVERDCH
QPYRNKGRMS GAQERKLSTP GYSLDV
