PLPP2_HUMAN
ID PLPP2_HUMAN Reviewed; 288 AA.
AC O43688; A6NLV0; E9PAY8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Phospholipid phosphatase 2 {ECO:0000305};
DE EC=3.1.3.- {ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349};
DE EC=3.1.3.4 {ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349};
DE AltName: Full=Lipid phosphate phosphohydrolase 2;
DE AltName: Full=PAP2-gamma;
DE Short=PAP2-G;
DE AltName: Full=Phosphatidate phosphohydrolase type 2c {ECO:0000303|PubMed:9607309};
DE AltName: Full=Phosphatidic acid phosphatase 2c {ECO:0000303|PubMed:9607309};
DE Short=PAP-2c {ECO:0000303|PubMed:9607309};
DE Short=PAP2c {ECO:0000303|PubMed:9607309};
GN Name=PLPP2 {ECO:0000312|HGNC:HGNC:9230};
GN Synonyms=LPP2, PPAP2C {ECO:0000303|PubMed:9607309};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9570154; DOI=10.1089/dna.1998.17.377;
RA Leung D.W., Tompkins C.K., White T.;
RT "Molecular cloning of two alternatively spliced forms of human phosphatidic
RT acid phosphatase cDNAs that are differentially expressed in normal and
RT tumor cells.";
RL DNA Cell Biol. 17:377-385(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP PATHWAY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=9705349; DOI=10.1074/jbc.273.34.22059;
RA Roberts R., Sciorra V.A., Morris A.J.;
RT "Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of
RT the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a
RT isoform.";
RL J. Biol. Chem. 273:22059-22067(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, PATHWAY, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=9607309; DOI=10.1016/s0014-5793(98)00421-9;
RA Hooks S.B., Ragan S.P., Lynch K.R.;
RT "Identification of a novel human phosphatidic acid phosphatase type 2
RT isoform.";
RL FEBS Lett. 427:188-192(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-214.
RX PubMed=16467304; DOI=10.1074/jbc.m511710200;
RA Morris K.E., Schang L.M., Brindley D.N.;
RT "Lipid phosphate phosphatase-2 activity regulates S-phase entry of the cell
RT cycle in Rat2 fibroblasts.";
RL J. Biol. Chem. 281:9297-9306(2006).
RN [8]
RP SUBUNIT.
RX PubMed=18215144; DOI=10.1042/bj20071607;
RA Long J.S., Pyne N.J., Pyne S.;
RT "Lipid phosphate phosphatases form homo- and hetero-oligomers: catalytic
RT competency, subcellular distribution and function.";
RL Biochem. J. 411:371-377(2008).
CC -!- FUNCTION: Magnesium-independent phospholipid phosphatase that catalyzes
CC the dephosphorylation of a variety of glycerolipid and sphingolipid
CC phosphate esters including phosphatidate/PA, lysophosphatidate/LPA,
CC sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P
CC (PubMed:9705349, PubMed:9607309, PubMed:16467304). Has no apparent
CC extracellular phosphatase activity and therefore most probably acts
CC intracellularly (PubMed:16467304). Also acts on N-oleoyl ethanolamine
CC phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential
CC physiological compound (PubMed:9607309). Through dephosphorylation of
CC these bioactive lipid mediators produces new bioactive compounds and
CC may regulate signal transduction in different cellular processes
CC (Probable). Indirectly regulates, for instance, cell cycle G1/S phase
CC transition through its phospholipid phosphatase activity (By
CC similarity). {ECO:0000250|UniProtKB:Q8K593,
CC ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9607309,
CC ECO:0000269|PubMed:9705349, ECO:0000305|PubMed:16467304}.
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:0000269|PubMed:16467304, ECO:0000269|PubMed:9607309,
CC ECO:0000269|PubMed:9705349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000305|PubMed:9705349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929; Evidence={ECO:0000269|PubMed:9705349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000305|PubMed:9705349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:9607309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000305|PubMed:9607309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol +
CC phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589;
CC Evidence={ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC Evidence={ECO:0000305|PubMed:9705349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-
CC octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937,
CC ChEBI:CHEBI:84973; Evidence={ECO:0000269|PubMed:9607309,
CC ECO:0000269|PubMed:9705349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC Evidence={ECO:0000305|PubMed:9705349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
CC Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC Evidence={ECO:0000269|PubMed:9705349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000305|PubMed:9705349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-
CC enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674;
CC Evidence={ECO:0000269|PubMed:9705349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC Evidence={ECO:0000305|PubMed:9705349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-
CC octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815,
CC ChEBI:CHEBI:85376; Evidence={ECO:0000269|PubMed:9705349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC Evidence={ECO:0000305|PubMed:9705349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-
CC octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466,
CC ChEBI:CHEBI:145465; Evidence={ECO:0000269|PubMed:9607309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC Evidence={ECO:0000305|PubMed:9607309};
CC -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase
CC (PubMed:9705349). Insensitive to N-ethylmaleimide (PubMed:9705349).
CC Inhibited by sphingosine, zinc ions and modestly by propanolol
CC (PubMed:9705349, PubMed:9607309). {ECO:0000269|PubMed:9607309,
CC ECO:0000269|PubMed:9705349}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC {ECO:0000269|PubMed:9607309};
CC KM=340 uM for (9Z)-octadecenoyl-sn-glycero-3-phosphate
CC {ECO:0000269|PubMed:9607309};
CC KM=138 uM for N-oleoyl ethanolamine phosphatidic acid
CC {ECO:0000269|PubMed:9607309};
CC Vmax=0.15 nmol/min/mg enzyme with 1,2-dihexadecanoyl-sn-glycero-3-
CC phosphate as substrate {ECO:0000269|PubMed:9705349};
CC Vmax=0.20 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-
CC phosphate as substrate {ECO:0000269|PubMed:9705349};
CC Vmax=0.17 nmol/min/mg enzyme with N-(octanoyl)-sphing-4-enine-1-
CC phosphate as substrate {ECO:0000269|PubMed:9705349};
CC Vmax=0.69 nmol/min/mg enzyme with sphing-4-enine 1-phosphate as
CC substrate {ECO:0000269|PubMed:9705349};
CC Vmax=34 nmol/min/mg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphate as substrate {ECO:0000269|PubMed:9607309};
CC Vmax=49 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-
CC phosphate as substrate {ECO:0000269|PubMed:9607309};
CC Vmax=17 nmol/min/mg enzyme with N-oleoyl ethanolamine phosphatidic
CC acid as substrate {ECO:0000269|PubMed:9607309};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9607309,
CC ECO:0000269|PubMed:9705349}.
CC -!- SUBUNIT: Forms functional homodimers and homooligomers
CC (PubMed:18215144). Can also form heterooligomers with PLPP1 and PLPP3
CC (PubMed:18215144). {ECO:0000269|PubMed:18215144}.
CC -!- INTERACTION:
CC O43688; P41235-3: HNF4A; NbExp=3; IntAct=EBI-722017, EBI-12690684;
CC O43688; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-722017, EBI-10266796;
CC O43688; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-722017, EBI-945833;
CC O43688; P42857: NSG1; NbExp=3; IntAct=EBI-722017, EBI-6380741;
CC O43688; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-722017, EBI-11996766;
CC O43688; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-722017, EBI-12190699;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16467304,
CC ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000255}.
CC Cell membrane {ECO:0000269|PubMed:16467304,
CC ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000255}.
CC Early endosome membrane {ECO:0000269|PubMed:16467304}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16467304}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O43688-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43688-2; Sequence=VSP_037765;
CC Name=3;
CC IsoId=O43688-3; Sequence=VSP_047366;
CC -!- TISSUE SPECIFICITY: Found mainly in brain, pancreas and placenta.
CC {ECO:0000269|PubMed:9607309}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9705349}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AF035959; AAC15968.1; -; mRNA.
DR EMBL; AF047760; AAC32104.1; -; mRNA.
DR EMBL; AF056083; AAC25666.1; -; mRNA.
DR EMBL; BT007021; AAP35667.1; -; mRNA.
DR EMBL; AC016588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002806; AAH02806.1; -; mRNA.
DR CCDS; CCDS12023.1; -. [O43688-1]
DR CCDS; CCDS12024.1; -. [O43688-2]
DR CCDS; CCDS45889.1; -. [O43688-3]
DR RefSeq; NP_003703.1; NM_003712.3. [O43688-1]
DR RefSeq; NP_803545.1; NM_177526.2. [O43688-3]
DR RefSeq; NP_808211.1; NM_177543.2. [O43688-2]
DR AlphaFoldDB; O43688; -.
DR BioGRID; 114170; 30.
DR IntAct; O43688; 12.
DR STRING; 9606.ENSP00000329697; -.
DR SwissLipids; SLP:000001977; -.
DR DEPOD; PLPP2; -.
DR GlyConnect; 1460; 1 N-Linked glycan (1 site).
DR GlyGen; O43688; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; O43688; -.
DR PhosphoSitePlus; O43688; -.
DR BioMuta; PLPP2; -.
DR EPD; O43688; -.
DR jPOST; O43688; -.
DR MassIVE; O43688; -.
DR MaxQB; O43688; -.
DR PaxDb; O43688; -.
DR PeptideAtlas; O43688; -.
DR PRIDE; O43688; -.
DR ProteomicsDB; 19106; -.
DR ProteomicsDB; 49117; -. [O43688-1]
DR ProteomicsDB; 49118; -. [O43688-2]
DR Antibodypedia; 22287; 169 antibodies from 22 providers.
DR DNASU; 8612; -.
DR Ensembl; ENST00000269812.7; ENSP00000269812.2; ENSG00000141934.10. [O43688-3]
DR Ensembl; ENST00000327790.7; ENSP00000329697.1; ENSG00000141934.10. [O43688-2]
DR Ensembl; ENST00000434325.7; ENSP00000388565.2; ENSG00000141934.10. [O43688-1]
DR GeneID; 8612; -.
DR KEGG; hsa:8612; -.
DR MANE-Select; ENST00000434325.7; ENSP00000388565.2; NM_003712.4; NP_003703.1.
DR UCSC; uc002loh.5; human. [O43688-1]
DR CTD; 8612; -.
DR DisGeNET; 8612; -.
DR GeneCards; PLPP2; -.
DR HGNC; HGNC:9230; PLPP2.
DR HPA; ENSG00000141934; Low tissue specificity.
DR MIM; 607126; gene.
DR neXtProt; NX_O43688; -.
DR OpenTargets; ENSG00000141934; -.
DR PharmGKB; PA33554; -.
DR VEuPathDB; HostDB:ENSG00000141934; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000155885; -.
DR InParanoid; O43688; -.
DR OMA; MDVVCVL; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; O43688; -.
DR TreeFam; TF316040; -.
DR PathwayCommons; O43688; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; O43688; -.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 8612; 24 hits in 1073 CRISPR screens.
DR ChiTaRS; PLPP2; human.
DR GeneWiki; Phosphatidic_acid_phosphatase_2c; -.
DR GenomeRNAi; 8612; -.
DR Pharos; O43688; Tbio.
DR PRO; PR:O43688; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43688; protein.
DR Bgee; ENSG00000141934; Expressed in olfactory segment of nasal mucosa and 130 other tissues.
DR ExpressionAtlas; O43688; baseline and differential.
DR Genevisible; O43688; HS.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR GO; GO:0006670; P:sphingosine metabolic process; IDA:UniProtKB.
DR InterPro; IPR028674; LPP2.
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; PTHR10165; 1.
DR PANTHER; PTHR10165:SF25; PTHR10165:SF25; 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; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Hydrolase; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Phospholipid phosphatase 2"
FT /id="PRO_0000220909"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..51
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..162
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..226
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 117..125
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 165..168
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 213..224
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 168
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 224
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047366"
FT VAR_SEQ 1..17
FT /note="MQRRWVFVLLDVLCLLV -> MGVARGPGSRGQHPPPRQQEVCAEGPRARLH
FT PAPPGLG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037765"
FT VARIANT 180
FT /note="A -> V (in dbSNP:rs1138439)"
FT /id="VAR_061541"
FT MUTAGEN 214
FT /note="R->K: Loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:16467304"
SQ SEQUENCE 288 AA; 32574 MW; F7C6A09A28DA9AC8 CRC64;
MQRRWVFVLL DVLCLLVASL PFAILTLVNA PYKRGFYCGD DSIRYPYRPD TITHGLMAGV
TITATVILVS AGEAYLVYTD RLYSRSDFNN YVAAVYKVLG TFLFGAAVSQ SLTDLAKYMI
GRLRPNFLAV CDPDWSRVNC SVYVQLEKVC RGNPADVTEA RLSFYSGHSS FGMYCMVFLA
LYVQARLCWK WARLLRPTVQ FFLVAFALYV GYTRVSDYKH HWSDVLVGLL QGALVAALTV
CYISDFFKAR PPQHCLKEEE LERKPSLSLT LTLGEADHNH YGYPHSSS
