PLPP5_MOUSE
ID PLPP5_MOUSE Reviewed; 260 AA.
AC Q3UMZ3; Q4KL19;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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:0000312|MGI:MGI:1919160};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-260 (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30042348; DOI=10.3390/ijms19082161;
RA Trezise S., Karnowski A., Fedele P.L., Mithraprabhu S., Liao Y.,
RA D'Costa K., Kueh A.J., Hardy M.P., Owczarek C.M., Herold M.J., Spencer A.,
RA Shi W., Willis S.N., Nutt S.L., Corcoran L.M.;
RT "Mining the Plasma Cell Transcriptome for Novel Cell Surface Proteins.";
RL Int. J. Mol. Sci. 19:0-0(2018).
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:0000269|PubMed:30042348};
CC Multi-pass membrane protein {ECO:0000269|PubMed:30042348}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UMZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UMZ3-2; Sequence=VSP_025243, VSP_025244;
CC -!- TISSUE SPECIFICITY: Specifically expressed by antibody-secreting immune
CC cells. {ECO:0000269|PubMed:30042348}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Plpp5 are viable and display no
CC overt physical defect. {ECO:0000269|PubMed:30042348}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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; AK144593; BAE25955.1; -; mRNA.
DR EMBL; BC099489; AAH99489.1; -; mRNA.
DR CCDS; CCDS40306.1; -. [Q3UMZ3-1]
DR CCDS; CCDS80868.1; -. [Q3UMZ3-2]
DR RefSeq; NP_082276.1; NM_028000.1. [Q3UMZ3-1]
DR AlphaFoldDB; Q3UMZ3; -.
DR STRING; 10090.ENSMUSP00000067035; -.
DR PhosphoSitePlus; Q3UMZ3; -.
DR PaxDb; Q3UMZ3; -.
DR PRIDE; Q3UMZ3; -.
DR ProteomicsDB; 289692; -. [Q3UMZ3-1]
DR ProteomicsDB; 289693; -. [Q3UMZ3-2]
DR Antibodypedia; 23567; 101 antibodies from 25 providers.
DR DNASU; 71910; -.
DR Ensembl; ENSMUST00000068916; ENSMUSP00000067035; ENSMUSG00000031570. [Q3UMZ3-1]
DR Ensembl; ENSMUST00000139836; ENSMUSP00000122437; ENSMUSG00000031570. [Q3UMZ3-2]
DR GeneID; 71910; -.
DR KEGG; mmu:71910; -.
DR UCSC; uc009lgr.1; mouse. [Q3UMZ3-1]
DR UCSC; uc009lgs.1; mouse. [Q3UMZ3-2]
DR CTD; 84513; -.
DR MGI; MGI:1919160; Plpp5.
DR VEuPathDB; HostDB:ENSMUSG00000031570; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000159772; -.
DR HOGENOM; CLU_021458_5_4_1; -.
DR InParanoid; Q3UMZ3; -.
DR OMA; CTPLIVI; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q3UMZ3; -.
DR TreeFam; TF323722; -.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 71910; 0 hits in 41 CRISPR screens.
DR ChiTaRS; Plpp5; mouse.
DR PRO; PR:Q3UMZ3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3UMZ3; protein.
DR Bgee; ENSMUSG00000031570; Expressed in pancreas and 64 other tissues.
DR ExpressionAtlas; Q3UMZ3; baseline and differential.
DR Genevisible; Q3UMZ3; MM.
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; ISS:UniProtKB.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0046839; P:phospholipid dephosphorylation; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..260
FT /note="Phospholipid phosphatase 5"
FT /id="PRO_0000286946"
FT TOPO_DOM 1..50
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30042348"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30042348"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..150
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30042348"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30042348"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..205
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30042348"
FT TRANSMEM 206..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30042348"
FT REGION 104..112
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:Q8NEB5"
FT REGION 145..148
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:Q8NEB5"
FT REGION 197..207
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:Q8NEB5"
FT ACT_SITE 148
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 204
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 208
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT VAR_SEQ 208..226
FT /note="DVLVGSMIGMTFAYVCYRQ -> GWYKDMHRCSQLFMRVLGI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025243"
FT VAR_SEQ 227..260
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025244"
SQ SEQUENCE 260 AA; 29223 MW; 5065F56EC3CCD554 CRC64;
MGTAALGAEL GVRVLLFVAF LVTELLPPFQ RRIQPEELWL YRNPYVEAEY FPTGRMFVIA
FLTPLSLIFL AKFLRKADAT DSKQACLAAS LALALNGVFT NIIKLIVGRP RPDFFYRCFP
DGLAHSDLTC TGDEDVVNEG RKSFPSGHSS FAFAGLAFAS FYLAGKLHCF TPQGRGKSWR
LCAFLSPLLF AAVIALSRTC DYKHHWQDVL VGSMIGMTFA YVCYRQYYPP LTDVECHKPF
QDKHKLPSSQ KPSELHHLEI
